WO2003016903A2 - Dispositif et procede permettant de determiner une substance a analyser - Google Patents

Dispositif et procede permettant de determiner une substance a analyser Download PDF

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Publication number
WO2003016903A2
WO2003016903A2 PCT/AT2002/000246 AT0200246W WO03016903A2 WO 2003016903 A2 WO2003016903 A2 WO 2003016903A2 AT 0200246 W AT0200246 W AT 0200246W WO 03016903 A2 WO03016903 A2 WO 03016903A2
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WO
WIPO (PCT)
Prior art keywords
analyte
reagent
group
upper limit
lower limit
Prior art date
Application number
PCT/AT2002/000246
Other languages
German (de)
English (en)
Other versions
WO2003016903A8 (fr
WO2003016903A3 (fr
Inventor
Walter Pils
Dietmar Pils
Original Assignee
Walter Pils
Dietmar Pils
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Priority claimed from AT0096302A external-priority patent/AT501069A1/de
Application filed by Walter Pils, Dietmar Pils filed Critical Walter Pils
Priority to AU2002332942A priority Critical patent/AU2002332942A1/en
Publication of WO2003016903A2 publication Critical patent/WO2003016903A2/fr
Publication of WO2003016903A3 publication Critical patent/WO2003016903A3/fr
Publication of WO2003016903A8 publication Critical patent/WO2003016903A8/fr

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Classifications

    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
    • B01L3/00—Containers or dishes for laboratory use, e.g. laboratory glassware; Droppers
    • B01L3/50—Containers for the purpose of retaining a material to be analysed, e.g. test tubes
    • B01L3/502—Containers for the purpose of retaining a material to be analysed, e.g. test tubes with fluid transport, e.g. in multi-compartment structures
    • B01L3/5023—Containers for the purpose of retaining a material to be analysed, e.g. test tubes with fluid transport, e.g. in multi-compartment structures with a sample being transported to, and subsequently stored in an absorbent for analysis
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
    • G01N33/54366—Apparatus specially adapted for solid-phase testing
    • G01N33/54386—Analytical elements
    • G01N33/54387—Immunochromatographic test strips
    • G01N33/54388—Immunochromatographic test strips based on lateral flow
    • G01N33/54389—Immunochromatographic test strips based on lateral flow with bidirectional or multidirectional lateral flow, e.g. wherein the sample flows from a single, common sample application point into multiple strips, lanes or zones
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
    • G01N33/54366—Apparatus specially adapted for solid-phase testing
    • G01N33/54386—Analytical elements
    • G01N33/54387—Immunochromatographic test strips
    • G01N33/54388—Immunochromatographic test strips based on lateral flow
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/558—Immunoassay; Biospecific binding assay; Materials therefor using diffusion or migration of antigen or antibody
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
    • B01L2300/00—Additional constructional details
    • B01L2300/08—Geometry, shape and general structure
    • B01L2300/0809—Geometry, shape and general structure rectangular shaped
    • B01L2300/0825—Test strips
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
    • B01L2300/00—Additional constructional details
    • B01L2300/08—Geometry, shape and general structure
    • B01L2300/0848—Specific forms of parts of containers
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
    • B01L2300/00—Additional constructional details
    • B01L2300/08—Geometry, shape and general structure
    • B01L2300/0861—Configuration of multiple channels and/or chambers in a single devices
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
    • B01L2300/00—Additional constructional details
    • B01L2300/08—Geometry, shape and general structure
    • B01L2300/0887—Laminated structure
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01L—CHEMICAL OR PHYSICAL LABORATORY APPARATUS FOR GENERAL USE
    • B01L2400/00—Moving or stopping fluids
    • B01L2400/04—Moving fluids with specific forces or mechanical means
    • B01L2400/0403—Moving fluids with specific forces or mechanical means specific forces
    • B01L2400/0406—Moving fluids with specific forces or mechanical means specific forces capillary forces

Definitions

  • the invention relates to a method for the detection of at least one analyte from a sample by an immunochemical reaction with a device consisting of several zones. Furthermore, the invention relates to a device for the detection of at least one analyte from one or more capillary-capable materials, on which at least one starting zone and an adjacent zone consisting of one or more fields in which or at least one immobilized reagent is arranged. The invention further relates to a reagent for performing the method according to one of claims 1 to 17 and an analysis kit according to claim 57. The invention also relates to the use of the device, the reagent and the analysis kit according to claims 58 to 60.
  • DE 19622503 AI describes a method for the detection of analytes on surfaces which have come into contact with body fluids.
  • This document describes a test strip made of one or more capillary-active sheet-like materials capable of chromatography in fluid contact with one another with an eluent application zone at one end and a target zone at the other end.
  • the capture reagent can either bind the analyte, a specific analyte binding partner or a labeled binding partner.
  • the binding partner can specifically bind either the analyte or the specific analyte binding partner or the capture reagent, the binding of the labeled binding partner leading to a detectable signal in the capture zone or in the target zone. This signal indicates the presence of the analyte.
  • a wiping element is separated from the test strip surface and a pressing device which eliminates contact between the wiping element and the test strip surface between the eluent application zone and the conjugate zone. With the wiping element, body fluids are absorbed from a body region. Direct markings, such as metal markings, in particular the gold marking, are preferred as markings for detection, because the test result can be read directly from the eye.
  • Antibodies and antibody fragments can be considered as binding partners for the analyte. With this method, absolute amounts of up to 10 ng analyte, in particular drugs on surfaces, can be detected.
  • a disadvantage of this disclosure is that low concentrations of analytes cannot be detected.
  • US Pat. No. 6,248,598 B1 describes a method which, on the one hand, for the production of saliva and, on the other hand, for the detection of at least one analyte therein without any additional external
  • the US B1 describes a method for the detection of an analyte with a device which fluidly connects a first part with absorbent material, which absorbs saliva in the mouth, to a second part and then enables a visual detection of analytes. light.
  • a ligand that specifically binds an analyte, an indicator consisting of an analyte with a visually detectable label, an area on which the presence or absence of the analyte is indicated and possibly a control area.
  • a holder in which a window for visual detection is located is described.
  • One end of the device is for 10 to
  • WO 00/208 62 AI describes a method and an apparatus for the in vitro detection of many different analytes, from serum, plasma, blood, saliva or urine of human or animal origin.
  • the detection system consists of a plastic device with an absorbent pad with an affinity membrane.
  • the device has specific regions on the membrane in which antigens are immobilized.
  • Each device has a quality control substance to check that the device is working properly.
  • the control material is usually human IgG.
  • antigen detection the control material is a specific antigen. Any area can be used as a control area in a multi-analyte detection system.
  • the device consists of a microporous membrane with a first and a second surface, a liquid flowing from one side to the other.
  • Membrane has a multiplicity of readable regions which are arranged spaced apart from one another over the entire membrane, an antigen, antibody or hapten being immobilized on each region. Furthermore, the device has a cover for the first side of the membrane with a recess for receiving liquids, whereby a region of the membrane is visible. Finally, the device consists of an absorbent
  • the object of the invention is therefore possibilities for the detection of low concentrations to provide different analytes. It is also a sub-object of the invention to increase the specificity for the detection of drugs and drug substitutes.
  • the object of the invention is achieved by the method according to the features in the characterizing part of claim 1.
  • the advantage of this method is that very low concentrations of an analyte are sufficient to be able to be detected using the method according to the invention.
  • This method therefore offers a highly sensitive method to detect analytes from a sample. Simple detection methods for the determination of analytes allow them to be carried out outside of laboratories, e.g. on the street, in police stations, in prisons, in factories or other workplaces, at home, practically anywhere. This detection method eliminates the need for costly laboratory analysis and thus enables cost savings.
  • Free biotin binding sites are then saturated with a biotin-labeled enzyme, eg alkaline phosphatase.
  • a biotin-labeled enzyme eg alkaline phosphatase.
  • the addition of chromogenic substrates causes a color mixture to precipitate, which enables the binding to be detected.
  • the biotin-binding proteins contain four biotin binding sites and the enzymes used also carry several biotin groups, complexes with many protein-enzyme-biotin molecules can form, which significantly increases the sensitivity of detection.
  • Alkaline phosphatase is used as a marker enzyme, since a sensitive, histochemical color reagent and signal amplifier system develops in conjunction with suitable substrates.
  • the enzyme ß-galactosidase cleaves natural and artificial ß-D-galactosides into galactose and the corresponding residues (mostly alcohol compounds).
  • unphysiological Substrates for the enzyme such as ONPG or X-gal, produce colored reaction products after hydrolysis and oxidation and thus allow visual and spectrophotometric detection.
  • an embodiment according to claim 4 is advantageous, wherein by separating the analyte in the many zones, a reaction with a dye component or its precursor as well as with a conjugated antibody can take place and these can then be detected in an analysis field.
  • Another advantage is that, regardless of the presence of an analyte in the sample, a marking in the zone of the control field can be detected in order to control the functionality of the analysis method.
  • a further advantage is the temporary immobilization of the reagents in the dye field and in the conjugate field, because this eliminates the need to add these reagents during the analysis, thus simplifying the process and preventing confusion of the reagents.
  • the arrangement of running fields enables the analytes to be freed from particulate contaminants during the passage of the capillary-capable material.
  • An embodiment according to claim 5 proves to be advantageous, according to which a multiplicity of analytes can be detected by this method. It has also proven to be advantageous that such a large number of analytes can be detected using the same method without having to adapt the method. Another advantage is that, due to the diversity of this method, no special training of the personnel to be carried out is required for the various analytes, and thus a large number of analytes can be evaluated by only one person. It has also proven to be advantageous that several analytes can be evaluated simultaneously using one method and on one device.
  • a further development of the method according to claim 10 is also advantageous, according to which the risk of contamination for the personnel who carries out the analysis can be minimized by the rapid detection of antibodies against infections. On the one hand, it can be decided by the detection of a viral infection that special caution should prevail for the further examination measures. On the other hand, due to the rapid analysis results, intensive treatment of supposedly infected people or even their quarantine can be dispensed with.
  • the method enables the detection of different hormones, e.g. of HCG, which is only detectable during pregnancy. This method also makes it easy to quickly prove pregnancy.
  • a further development of the method according to claim 12 has also proven to be advantageous, according to which, in the event of a conspicuous medical history, a first statement about the presence of tumor markers can be made quickly, and thus the time period until the result of the finding and thus the uncertainty for the patient is minimized.
  • the embodiment of the method according to claim 13 proves to be advantageous, wherein the correct treatment of the intoxication can be started immediately by detecting the toxin and, for example, the appropriate antidote can be administered immediately.
  • a further development according to claims 14, 15 and 16 is advantageous, according to which the analyte comes from a sample of any origin and can be used for the method.
  • a particular advantage of this method is that, despite the variety of samples, regardless of their origin, a reliable, reproducible result is always achieved. It has proven to be particularly advantageous that the method has a high tolerance limit for contamination and that the samples therefore do not have to be cleaned before the analysis.
  • the object of the invention is independently achieved by a device according to the features in the characterizing part of claim 18.
  • This device provides a very sensitive possibility for the detection of at least one analyte.
  • the simple structure of the device enables it to be operated and evaluated by chemically and medically untrained personnel, and the analyte can thus be detected independently of a specific location.
  • a further development according to claim 19 proves to be advantageous because it can prevent non-specific bindings and therefore only specific bindings can take place and can also be detected. It is also advantageous that during the detection no signals which result from unspecific binding influence the readability of the device.
  • the sensitivity of the device for detecting the analyte is increased.
  • the dye components and their precursors act as part of an amplifier system.
  • the attachment of a dye field enables only the analyte to be applied to the device and not the dye components to be added to the reagent first. This again simplifies the handling of the device.
  • Embodiments of the device according to one of claims 23 and 24 are also advantageous, the dye component or its precursors serving as an enhancer system and the sensitivity of the analysis thus being increased.
  • X-gal has the advantage over ONPG that the blue oxidigo dye formed as a reaction product after hydrolysis and oxidation is sparingly soluble and therefore does not diffuse.
  • Embodiments according to claims 25 and 26 also prove to be advantageous, according to which the addition of these substances results in better solubility of the dye components and their precursors and thus in turn improves the sensitivity of the analysis.
  • the refinements according to claim 30 also prove to be advantageous, the same analyte being arranged in the analysis field or a specific binding partner for the analyte to be detected and thus cross-reactions and false positive results can be excluded by unspecific binding.
  • An embodiment according to claim 31 is also advantageous in that a variety of analytes can be detected and the device can not only be used for the detection of a single analyte and production costs for the different designs of the devices can thereby be minimized. It also proves advantageous that the same method can be used for the detection of all analytes.
  • an embodiment according to claim 32 proves to be advantageous, according to which only a small amount of the analyte has to be applied to the device and thereby the costs for the material expenditure of the device are minimized.
  • the analyte can already be bound in the reagent and is detected in the analysis method by a specific binding partner for the binding partner of the analyte. This enables indirect detection of the analyte.
  • components of the dye system or their precursors can already be added to the reagent and, for example, this can shorten the running distance of the analyte on the device and thus minimize the size of the device overall.
  • the object of the invention is also achieved independently by an analysis kit according to the features in the characterizing part of claim 57.
  • the advantage of this is that all the necessary devices and reagents for carrying out the analysis are made available.
  • Another advantage is that the simple way of storing the analysis kit at room temperature makes it possible to store it regardless of the location.
  • the object of the invention is also achieved independently by using the device according to the features in the characterizing part of claim 58. It has been shown to be advantageous that the device provides a reliable means for analyzing at least one analyte in a sample.
  • the object of the invention is also achieved independently by the use of the reagent according to the features in the characterizing part of claim 59. It has proven to be advantageous that the use of the reagent provides an inexpensive means with enhancement potential.
  • the object of the invention is also achieved independently by using the analysis kit in accordance with the features in the characterizing part of claim 60. It proves to be advantageous that the analysis kit enables rapid and uncomplicated determination of the analyte regardless of the location.
  • Figure 1 shows a square device from the start zone and analysis field.
  • Figure 2 shows a square device from the start zone, zone and target zone.
  • 3 shows a quadrangular device consisting of the start zone, zone and target zone
  • 5 shows a round device comprising the start zone, zone and target zone
  • FIG. 6 shows a star-shaped device consisting of a starting zone and an analysis field
  • FIG. 7 shows a star-shaped device comprising the start zone, zone and target zone
  • FIG. 8 shows a hexagonal device consisting of a start zone and an analysis field
  • Fig. 9 shows a hexagonal device from the start zone, zone and target zone.
  • Fig. 1 shows a side view of a device 1 on a carrier material 2, wherein the at least one capillary material 3 by means of a connecting layer 4, such as. B. one Double adhesive film, is connected to the carrier material 2. It is also possible to apply the capillary-capable material to a one-sided adhesive carrier material (laminating). A starting zone 5 and a further zone 6, which is formed from at least one capillary-capable material 3, are arranged on the device 1.
  • FIG. 2 shows a further embodiment of the device 1, it being noted at this point that the invention is not restricted to the specially shown embodiment variants of the device, but rather that various combinations of the individual embodiment variants with one another are possible and this variation possibility is due to this the teaching of technical action through objective invention lies in the ability of the specialist working in this technical field.
  • the scope of protection also includes all conceivable design variants which are possible by combining individual details of the design variant illustrated and described.
  • FIG. 2 shows a side view of a device 1 on a carrier material 2, the
  • Carrier material 2 is connected to at least one capillary-capable material 3 via a connecting layer 4.
  • a starting zone 5, a zone 6 and a target zone 7 are arranged on the capillary-capable material 3.
  • Zone 6 consists of several fields, e.g. a conjugate field 8 with specific binding partners to which at least one substance is conjugated, at least one running field 9, an analysis field 10 and / or control field 11 and a dye id 12.
  • FIG. 3 shows a square device 1, with several analysis fields 10 being arranged in zone 6. A different analyte 13 can be bound to each of these analysis fields 10 and thus the device 1 for the detection of several different analytes
  • start zone 5 can also be arranged centrally on the device 1, the analysis fields 10 being able to be located on all sides of the start zone 5.
  • a plurality of target zones 7 can also be arranged on the device 1.
  • FIG. 4 shows a round embodiment of the device 1 as described in FIG. 1. Adjacent to the starting zone 5 there is another zone 6 in which the detection of the at least one analyte 13 takes place.
  • Fig. 5 shows a round embodiment of the device 1, being adjacent to the Starting zone 5 are a conjugate field 8, a dye id 12, several running fields 9, at least one analysis field 10 and / or a control field 11 and a target zone 7.
  • FIG. 6 and 7 show star-shaped designs of the device 1, the device 1 in FIG. 6 being formed only by a start zone 5 and an adjacent zone 6 and in FIG. 7 comprising a start zone 5, a target zone 7 and a zone 6 from a conjugate field 8, a dye id 12, several running fields 9, at least one analysis field 10 and / or a control field 11 are shown.
  • the different zones 6 are arranged in a circle on the device 1.
  • FIG. 8 and 9 show octagonal embodiments of the device 1, the device 1 in FIG. 8 being formed only by a start zone 5 and an adjacent zone 6 and in FIG. 9 comprising a start zone 5, a target zone 7 and a zone 6 from a conjugate field 8, a dye id 12, several running fields 9, at least one analysis field 10 and / or a control field 11 are shown.
  • the different zones 6 or fields can have different forms, e.g. linear, circular, triangular, quadrangular, hexagonal, pentagonal, heptagonal, octagonal, trapezoidal, rhomboid, etc., can be arranged on the device 1.
  • the capillary-capable material which constitutes a filter, consists of cellulose and / or its derivatives, of organic polymers and their derivatives, in particular of materials that adsorb little protein on their surface, such as e.g. Glass fiber, ceramic, polytetrafluoroethylene (PTFE), nylon, polyvinylidene fluoride (PVDF), materials based on silicon, materials of biological origin, acetates or from mixtures or modifications thereof
  • the filters are of a pore size selected from a range with an upper limit of 50 ⁇ m, preferably 40 ⁇ m, in particular 35 ⁇ m and a lower limit of 0.20 ⁇ m, preferably 5 ⁇ m and in particular 10 ⁇ m. Filters with a pore size have also been selected particularly advantageously from a range with an upper limit of 30 ⁇ m, preferably 25 ⁇ m, in particular 20 ⁇ m and a lower limit of 12 ⁇ m, preferably 15 ⁇ m, in particular 17 ⁇ m. Pre-filters with an undefined pore size can also be used.
  • the capillary-capable material can be formed by a filter with an arbitrarily defined pore size.
  • the capillary-capable material 3 of the device 1 has a thickness selected from an area with a lower limit of 0.05 mm, preferably 0.08 mm, in particular 0.15 mm and an upper limit of 2 mm, preferably 1.5 mm. in particular 1 mm.
  • a thickness has been selected from a range with a lower limit of 0.1 mm, preferably 0.15 mm, in particular 0.2 mm and an upper limit of 0.9 mm, preferably 0.8 mm, in particular 0, 5 mm.
  • the thickness of the capillary material 3 can vary in the different zones 6 or the different fields; ie that the device 1 does not have to have a uniform thickness over its entire extent.
  • the different zones 6 of the device 1 can consist of the same capillary material 3 or of different capillary materials 3. As shown in FIG. 2, the device 1 in the start and target zone 7 can be made of a different material than in the zone 6 consisting of fields. The thickness and the pore size of the capillary material 3 can also be different in the different zones 6.
  • the capillary material is treated with solutions containing proteins such as BSA, milk powder, casein, gelatin, fat-free milk powder, calf serum, etc. and / or with commercial blocking reagents, e.g. Blotto or Superblock (from Pierce) in a concentration of 0.1-10 mg / ml and / or detergents, e.g. Tween, Triton, Nonidet P-40, Chaps, etc. in a concentration of 0.005 to
  • a predeterminable amount of the at least one analyte 13 is selected in a concentration from a range with a lower limit of 0.5 ng / ml, in particular 1 ng / ml, preferably 2 ng / ml, and an upper limit of 5 mg / ml, in particular
  • the at least one analyte 13 can be detected both directly and indirectly, for example by the analyte 13 itself, a specific analyte binding partner or a labeled binding partner. Indirect detection is carried out by binding analyte 13 to a first specific binding partner, eg primary antibody. In the analysis field either this or the analyte (at another location) is then recognized and bound by a second specific binding partner, for example secondary antibody, which is immobilized in the analysis field 10.
  • a first specific binding partner eg primary antibody
  • a second specific binding partner for example secondary antibody
  • the presence of the analyte in the analysis field 10 is finally linked to a further specific binding partner, which is conjugated to a substance, which either binds the analyte itself (at another location) or the analyte to the first specific binding partner or recognizes the second specific binding partner.
  • At least one analyte 13 is immobilized in the analysis field 10.
  • an analyte-specific binding partner can also be immobilized in analysis field 10.
  • the specific binding partner which is conjugated with a substance must be specific for the analyte and bind it to another location.
  • a large number of different analytes 13 can be detected.
  • the at least one analyte 13 can be selected from a group comprising drugs or drug substitutes including cannabis products, e.g. Marijuana, hashish and / or cannabinol, cocaine, e.g. Benzoylecgonine, crack and / or crystal, opiates, such as e.g. Morphine,
  • MDA dimethoxybromamphetamine
  • methamphetamines such as e.g. ecstasy, MDMA
  • phencyclidine angel dust
  • ⁇ -hydroxybutyric acid liquid ec
  • Doping agents from a group comprising anabolics such as testosterone and its derivatives, somatotropin, ephedrine derivatives, analeptics, such as strychnine, amphetamine derivatives, analgesics, antitussives, agents for increasing the oxygen transport capacity and the oxygen availability for the skeletal muscles, such as eg erythropoietin and / or diuretics, drugs, analgesics or psychopharmaceuticals from a group comprising, neuroleptics such as phenothiazine, butyrophenones and / or thioxanthenes, antidepressants such as MAO (monoamine oxidase) inhibitors, imipramine, desipramine, amitriptyline, etc., tranquilizers, such as.
  • anabolics such as testosterone and its derivatives, somatotropin, ephedrine derivatives, analeptics, such as strychnine, amphetamine derivatives, an
  • B. benzodiazepines diazepam
  • barbiturates and or psychoanaleptics
  • stimulants such as phenylethylamine, antiepileptics and / or hypnotics
  • antibodies formed as a reaction to viral, viroid, bacterial, mycotic, parasitic or prion-based infections and / or formed as a result of immunizations (vaccination in humans or animals or polyclonal antibody production in animals) and / or formed as a result of autoimmune diseases or allergic reactions
  • hormones such as, for example, HCG (human chorion gonadotropin), proteins as tumor markers from a group comprising squamous cell carcinoma antigen (SCC), thyroglobin (Tg), steroid hormone receptors, prostate-specific antigen (PSA), neuron-specific enolase (NSE), carcinoembryonic antigen (CEA), alpha-fetoprotein (AFP), CYFRA 21-1, CA 125, 19-9,
  • allergens such as. e.g. pollen, dust mite droppings, histamine, etc.
  • the detection of prions from the nervous system of various mammals as well as from feed or food is of increasing importance in order to prevent the spread of Creutzfeldt-Jakob disease.
  • Markers or species-specific proteins which are used in genetic engineering to identify genetically modified foods, seeds, etc. can also be detected as analyte 13.
  • Various antibody (sub) types can also be detected.
  • concentration of the at least one analyte 13 in the dilution series decreases with a factor selected from a range with a lower limit of 1, in particular 2, preferably 3 and an upper limit of 100, in particular 10, preferably with a factor 5.
  • the analyte 13 can be obtained from a sample of biological origin, such as body fluids from humans and animals, e.g. Blood, plasma, serum, urine, saliva, sweat, sperm, etc. and / or of vegetable origin, e.g. Leaf, fruit, seeds, etc. and / or microbiological
  • the analyte 13 can also be detected from the soil or from water.
  • the analyte 13 has to be concentrated, e.g. by sucking in larger air volumes by means of a pump, it being possible for the analyte 13 to be enriched directly on the material of the starting zone 5.
  • One or more dye components or their precursors are temporarily immobilized in the dye id 12.
  • the dye components do not necessarily have to be located in a zone 6, but can also be divided into several zones 6, such as, for example, the start zone 5, the dye id 12, the conjugate field 8 and the running field 9.
  • the dye components are in undissolved form in front.
  • the dye components or their precursors used are: tyramine and its derivatives, X-gal (5-bromo-4-chloro-3-indolyl-ß-D-galactoside), S-gal (3,4 cyclohexenoesculetin-ß-D- Galactopyranoside), ONPG (o-nitrophenyl-ß-D-galactopyranoside), CPRG (chlorophenol red-ß-D-galactopyranoside), bluogal (5-bromo-3-indolyl-ß-D-galactoside), MUGal (4-methylumbelüferyl -beta-D-galacto- pyranoside), NBT (nitroblue tetrazolium chloride), BCIP (5-bromo-4-chloro-3-indolyl phosphate), PNPP (p-nitrophenyl phosphate), OPD (o-phenylenediamine), ABTS (2,2'-azin
  • conjugate field 8 there are in particular specific binding partners such as e.g. Antibodies against analyte 13, which are combined with a catalyst, e.g. an organic or inorganic catalyst or enzymes or proteins, e.g. ⁇ -galactosidase, peroxidase, alkaline phosphatase, streptavidin / avidin, protein A or similar molecules capable of high-affinity specific bonds, etc., are conjugated.
  • a catalyst e.g. an organic or inorganic catalyst or enzymes or proteins, e.g. ⁇ -galactosidase, peroxidase, alkaline phosphatase, streptavidin / avidin, protein A or similar molecules capable of high-affinity specific bonds, etc.
  • a catalyst e.g. an organic or inorganic catalyst or enzymes or proteins, e.g. ⁇ -galactosidase, peroxidase, alkaline phosphatase, streptavidin /
  • the concentration of the specific binding partner to which the substance is conjugated is selected from a range with a lower limit of 0.5 ng / ml, in particular 1 ng / ml, preferably 2 ng / ml, and an upper limit of 5 mg / ml, in particular 2 mg / ml, preferably 1 mg / ml. Concentrations have also been selected particularly advantageously from a range with a lower limit of 0.1 mg / ml, preferably 0.2 mg / ml, in particular 0.3 mg / ml, and an upper limit of 2 mg / ml, preferably 1 mg / ml, especially 0.5 mg / ml.
  • an immobilized specific binding partner for example a Antibodies for at least one substance, such as, for example, ⁇ -galactosidase, alkaline phosphatase, peroxidase, streptavidin / avidin, protein A or similar molecules capable of high-affinity specific bonds, etc., in a concentration selected from a range with a lower limit of 0.5 ng / ml, in particular 1 ng / ml, preferably 2 ng / ml, and an upper limit of 5 mg / ml, in particular 3 mg / ml, preferably 1 mg / ml.
  • a concentration selected from a range with a lower limit of 0.5 ng / ml, in particular 1 ng / ml, preferably 2 ng / ml, and an upper limit of 5 mg / ml, in particular 3 mg / ml, preferably 1 mg / ml.
  • a small amount of a sample with an absorbent material such as e.g. collected a cotton swab.
  • the analyte 13 adhering to the absorbent material is taken up in a reagent, in particular an organic reagent.
  • a reagent in particular an organic reagent.
  • Three to seven drops of this reagent provided with analyte 13 are applied to the device 1.
  • the reagent with the analyte 13 migrates in the capillary-capable material 3 of the device 1 at a speed of 1 to 12 cm / minute from the starting zone 5, for example through the zone 6 consisting of at least one conjugate field 8, dye id 12,
  • the first marking resulting from the binding of the analyte-specific and / or substance-conjugated analyte-specific binding partner in the analysis field 10 results and the second label results from the binding of the immobilized binding partner specifically for the substance, such as ⁇ -galactosidase in reaction with a dye component or its precursor.
  • the analyte-specific binding partner in analysis field 10 and the analyte-specific binding partner to which at least one substance is conjugated reacts with the passing dye component or its precursors in such a way that the dye or dye complex formed is either insoluble or poorly soluble on Analysis field 10 remains and / or can be detected by antibodies against the dye complex formed.
  • the specific binding partner, to which at least one substance is conjugated can carry several binding sites for dyes or dye complex molecules that produce a clearly visible label.
  • analyte 13 If a sufficient amount of the analyte 13 is present, it binds to the analyte-specific binding partners which are conjugated with a substance, and these binding partners can therefore no longer bind to the immobilized analyte 13 in the analysis field 10 and run into the target zone 7 without formation of a visible marking of the device 1.
  • the substance thus bound also react the passing dye components or their precursors in such a way that the dye formed remains complex insoluble or poorly soluble in place and / or by an antibody against the dye complex formed, which is immobilized in the control field 11, with the
  • the detection of an analyte 13 with the enzyme ß-galactosidase as an enhancer system is carried out by the cleavage of natural or artificial ß-D-galactosides in galactose and the corresponding residual compounds.
  • Unphysiological substrates for the enzyme such as ONPG or X-gal, give colored reaction products after hydrolysis and oxidation and allow visual and spectrophotometric detection.
  • streptavidin and avidin proteins with multiple Binding sites for biotin are used.
  • a specific binding partner can be labeled with biotin.
  • Proteins such as streptavidin and avidin bind to one of their four binding sites in a highly specific manner to ' biotin. Free biotin binding sites are then saturated with biofin-labeled enzyme, eg alkaline phosphatase. Due to the addition of chromogenic substrates, a color mixture precipitates, so that the binding can be demonstrated.
  • biofin-labeled enzyme eg alkaline phosphatase. Due to the addition of chromogenic substrates, a color mixture precipitates, so that the binding can be demonstrated.
  • biotin-binding proteins contain four biotin binding sites and the enzymes used can also carry several biotin groups, complexes can form with many protein-enzyme-biotin molecules, which significantly increases the sensitivity of detection.
  • Alkaline phosphatase is used as a marker enzyme, since a sensitive, histochemical one is found in connection with suitable substrates
  • Color reagent and signal amplifier system can be developed.
  • BCEP is usually used together with nitro blue tetrazolium (NBT) as a color enhancer.
  • the enzyme peroxidase (HRP) with derivatized tyramine can be used as a further alternative amplification system (Super-CARD, Catalytic deposition of derivatized tyramine, Bhattacharya, R., Bhattacharya, D., and Dhar, TK (1999) Journal of Immunological Method 227, 31-39).
  • HRP enzyme peroxidase
  • the specific binding partner is coupled to the enzyme peroxidase (HRP) and catalyzes the covalent binding of the derivatized tyramine to the analysis field (specifically to specially modified proteins for this purpose) using H2O2 (which is present in the reagent or is formed directly by a chemical reaction).
  • p-OH-PPA-casein p-OH-PPA-gelatin or p-OH-PPA-BSA
  • p-OH-PPA 3- (p-hydroxyphenyl) propionic acid) which are immobilized on the analysis field).
  • a dye gold particles (NanoGold) or a catalyst is considered.
  • a histochemical color reagent gives a signal that is amplified many times over.
  • the reagent used to take up the sample consists of monohydric alcohol with 1 to 5 carbon atoms, ketones with 3 to 8 carbon atoms, polyhydric alcohols, especially ethylene glycol and polyethylene glycol.
  • concentrations of these chemical compounds are from a range with a lower limit of 0.1%, in particular 5%, preferably 10%, and an upper limit of 40%, in particular 30%, preferably 20% selected.
  • the reagent can additionally be a detergent, in particular (octylphenoxyl) polyethoxyethanol, alkylphenol polyglycol ether, Tween 20, sodium deoxycholate, Nonidet P-40 (Igepal CA-630), Triton X-100, cholic acid, deoxycholic acid and / or Zwittergent® in a concentration selected from a range with a lower limit of 0.001%, in particular 0.005%, preferably 0.01%, and an upper limit of 1%, in particular 0.5%, preferably 0.2%, as a solubilizer.
  • a detergent in particular (octylphenoxyl) polyethoxyethanol, alkylphenol polyglycol ether, Tween 20, sodium deoxycholate, Nonidet P-40 (Igepal CA-630), Triton X-100, cholic acid, deoxycholic acid and / or Zwittergent® in a concentration selected from a range with a lower limit of 0.001%, in particular 0.00
  • a buffer can also be added to the reagent, which keeps the reagent constant in a pH range.
  • Buffer solutions such as e.g. Citrate buffer, acetate buffer, maleate buffer, phosphate buffer, collidine buffer, triethanolamine-HCl-EDTA buffer, tris buffer, ammediol buffer, glycine buffer, diethanolamine buffer or tris-boric acid-EDTA buffer, or buffer according to Good, N.E. et al. (1966) Biochemistry 5, 467.
  • the concentration of the buffer solutions is in one percent by weight
  • the buffer solution has a pH value selected from a range with a lower limit of 5.5, in particular 6.0, preferably 6.5, and an upper limit of 9.5, in particular 9.0, preferably 8.5. Buffer solutions with a pH
  • At least one dye component or its precursor can be added to the reagent, the dye components being selected from a group comprising tyramine and its derivatives, X-Gal (5-bromo-4-chloro-3-indolyl- ⁇ -D- Galactoside), S-Gal (3,4 cyclohexenoesculetin-ß-D-galactopyranoside), ONPG (o-nitrophenyl-ß-D-galactopyranoside), CPRG (chlorophenol red-ß-D-galactopyranoside), Bluogal (5- Bromine-3-indolyl- ⁇ -D-galactoside), MUGal (4-methylumbelliferyl- ⁇ -D-galactopyranoside), NBT (Nitroblue Tetrazolium chloride), BCE?
  • X-Gal (5-bromo-4-chloro-3-indolyl- ⁇ -D- Galactoside)
  • S-Gal (3,4
  • LuciGLOTM LuciGLOTM, DuoLuXTM, Lumigen PS-3, chemiluminescent HRP (horseradishperoxidase) substrate, 2 Component System from BioFXTM, and / or Lumi-Gal 530 and / or fluorescent dyes, e.g. 3-carboxyumbelliferyl- ⁇ -D-galactopyranoside (CUG) and / or MUP (4-methylumbelliferyl phosphate).
  • concentration of the dye components is selected from a range with a lower limit of 1 ⁇ M, in particular 10 ⁇ M, preferably 50 ⁇ M, and an upper limit of 300 mM, in particular 150 mM, preferably 100 mM.
  • the dye components and / or their precursors are dissolved in the reagent and are dissolved there by adding the components of the reagent, BSA, maltodextrin, milk powder, calf serum, casein and / or gelatin, or are transported via the device 1 by the capillary action ,
  • sodium salts, potassium salts, phosphate salts, magnesium and / or manganese salts, BSA, maltodextrin (maltrin) or milk powder in a concentration from a range with a lower limit of 0.001%, in particular
  • 0.1%, preferably 1%, and an upper limit of 30%, in particular 20%, preferably 10%, can be added.
  • a preservative in particular sodium azide, sodium benzoate, sorbic acid, pentachlorophenol, sorbate and / or preservative based on mercury, can be added to the reagent in a concentration from a range with a lower limit of 0.01%, in particular 0.05%, preferably 0.1%, and an upper limit of 5%, in particular 3%, preferably 1%, in order to extend the shelf life of the reagent.
  • the dye components and / or their precursors are in the reagent or partially in the reagent or are completely or partially in the dye id 12 or completely or partially in the starting zone 5 of the device 1 in undissolved form.
  • the analysis kit comprises a device 1 for detecting at least one analyte 13, the reagent an absorbent substance, such as a cotton swab or the like.
  • the analysis kit also contain other aids, such as gloves, stopwatch, pipettes, etc.
  • the start 5 and finish zone 7 are made of cellulose absorbent paper (Pall Corporation, type 165 for the start zone 5 (BSP165PK) and type 197 for the target zone 7 (BSP197PK)).
  • the format of start 5 and finish zone 7 is 25 x 80 mm.
  • the filter paper is used without further impregnation to produce the device 1.
  • the dye id 12 is made from glass fiber microfilter type GF / D (Whatman).
  • the format of the dye field 12 is 5 x 80 mm and is evenly charged with 80 ⁇ l of the dye solution. This is followed by drying at 20 ° C in the absence of light.
  • the dye solution consists of: X-Gal (100 mM), NBT (50 mM), Phenazine Methosulfate (1 mM), BSA (4%), Maltrin (1) in PBS (5 mM KH 2 PO 4 , 15 mM Na 2 HPO 4 , 120 mM NaCl, 2.3 mM KC1, 2 mM MgCl 2 , 0.05% NaN 3 , 5% ethanol, 0.1% Triton X-100).
  • the starting reagents are manufactured by SIGMA-Aldrich.
  • the conjugate field 8 consists of blocked Accuwick® membrane (Pall. AW 14-20-10).
  • the membrane is blocked with 1% BSA in PBS solution for 1 hour at room temperature, then drying at 20 ° C.
  • the format is again 5 x 80 mm. 80 ⁇ l of the antibody solution are pipetted on evenly and then drying is carried out at 20 ° C.
  • the antibody solution consists of: primary monoclonal antibodies (host mouse) against benzodiazepines (25 nM), (Fitzgerald, cat.
  • the strips are placed in a 1% BSA-containing PBS solution (5 mM KH 2 PO 4 , 15 mM Na 2 HPO 4 , 120 mM NaCl, 2.3 mM KC1, 2 mM MgCl 2 , 0.05 % NaN 3 , 0.1% Titron X-100) incubated for 30 minutes at room temperature with stirring.
  • a 1% BSA-containing PBS solution 5 mM KH 2 PO 4 , 15 mM Na 2 HPO 4 , 120 mM NaCl, 2.3 mM KC1, 2 mM MgCl 2 , 0.05 % NaN 3 , 0.1% Titron X-100
  • a BS A-benzodiazepine conjugate (from Fitzgerald) is immobilized in the test field before binding sites are blocked.
  • the cellulose acetate filter (AcetatePlus) is incubated in 100 mM sodium periodate (SIGMA-Aldrich) for 20 min, then washed with H2O and with a 0.5 ⁇ M BSA-benzodiazepine solution in 0.1 M borate buffer (pH 9.0 ) incubated for 10 minutes. Then 4 mg sodium cyanoborohydride (SIGMA-Aldrich) are added per ml and incubated for 2 h at room temperature. Unbound BSA benzodiazepine is washed away using H2O.
  • control field 11 a specific polyclonal antibody against the enzyme ⁇ -galactosidase (Fitzgerald, host: Rabbit) is immobilized before the binding sites are blocked. 0.25 ⁇ M specific polyclonal antibody is immobilized using the same method as in the test field.
  • the reagent used, in which the sample is taken up consists of PBS (5 mM
  • the starting zone 5, the fields of zone 6 and the target zone 7 are cut according to the specifications described and by means of double-sided adhesive film (from Tesa AG)
  • Carrier films Xeroperm (Rank Xerox Limited) attached. Of these, strips of 4 mm are cut with a roll cutter. The strips are stored at room temperature in the absence of light and moisture.
  • the start 5 and finish zone 7 are made of cellulose absorbent paper (Pall Corporation, type 165 for the application cushion (BSP165PK) and type 197 for the absorption cushion (BSP197PK)) manufactured. Strips of 25 x 80 mm are cut to size, which are used to produce the device 1 without further impregnation or pretreatment.
  • BSP165PK type 165 for the application cushion
  • BSP197PK type 197 for the absorption cushion
  • Dye 12 is made from 'Glass Fiber Media' (Pall, A / D Glass). Strips in the format of 5 x 80 mm are cut and evenly charged with 80 ⁇ l of the dye solution. The drying is then carried out at 20 ° C in the absence of light.
  • the dye solution consists of: X-Gal (100 mM), NBT (50 mM), phenazine methosulfate (1 mM), BSA (4%), maltrine (1%) in PBS (5 mM KH 2 PO 4 , 15 mM Na 2 HPO 4 , 120 mM NaCl, 2.3 mM KC1, 2 mM MgCl 2 , 0.05% NaN 3 , 5% ethanol, 0.1% Triton X-100) (all solutions are from SIGMA -Aldrich).
  • the running field 9, analysis field 10 and control field 11 consist of a 5 ⁇ m Immunodyne® ABC membrane in the format 20 x 80 mm (Pall., BC500H5R).
  • a 0.5 ⁇ M testosterone-3-CMO-BSA solution (from Fitzgerald, 80-IT49) is placed on the device 1 at the location of the analysis field 10 and a 0.25 ⁇ M biotin-BSA at the location of the control field 11 solution
  • Biotinylated anti-mouse IgG antibodies (host: Pferd, Vector Laboratories: BA-2080) and 100 nM of an avidin-beta-galactosidase conjugate (SIGMA-Aldrich) applied directly to the blocked Immunodyne® ABC membrane between start zone 5 and analysis field 10.
  • SIGMA-Aldrich an avidin-beta-galactosidase conjugate
  • the reagent used, in which the sample is taken up consists of PBS (5 mM
  • Carrier material (film Xeroperm type 003R96094 from Rank Xerox Limited) attached. Of these, strips of 4 mm are cut with a roll cutter. The strips are stored at room temperature in the absence of light and moisture.
  • FIGS. 1 to 9 For the sake of order, it should finally be pointed out that, for a better understanding of the structure of FIGS. 1 to 9, these or their components have been partially shown to scale and / or enlarged and / or reduced.
  • FIGS. 1 to 9 can form the subject of independent solutions according to the invention.
  • the relevant tasks and solutions according to the invention can be found in the detailed descriptions of these figures.

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Abstract

L'invention concerne un procédé permettant de déterminer au moins une substance à analyser, à partir d'un prélèvement, par une réaction immunochimique à l'aide d'un dispositif composé de plusieurs zones. Cette substance à analyser est appliquée sur une zone de départ dans un réactif, en particulier un réactif organique, et s'écoule dans au moins une autre zone présentant un ou plusieurs champs sous l'effet de forces capillaires. Selon cette invention, au moins un partenaire de liaison spécifique, auquel au moins une substance est conjuguée, est temporairement immobilisé dans un champ.
PCT/AT2002/000246 2001-08-20 2002-08-16 Dispositif et procede permettant de determiner une substance a analyser WO2003016903A2 (fr)

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EP1566640A1 (fr) * 2004-02-18 2005-08-24 Ani Biotech Oy Dispositif d' échantillonnage, méthode et leur utilisation
EP1970706A1 (fr) * 2005-12-14 2008-09-17 DENKA SEIKEN Co., Ltd. Procédé de détection immunochromatographique pour staphylocoque présentant une multirésistance aux médicaments, et kit de diagnostic
CN105973632A (zh) * 2016-05-05 2016-09-28 中国农业科学院烟草研究所 植物根系分泌物发生及收集装置及其收集方法
EP3408672A4 (fr) * 2016-01-27 2019-10-23 Undercover Colors, Inc. Procédés et appareil pour détecter des composés dans des liquides
US10519175B2 (en) 2017-10-09 2019-12-31 Compass Pathways Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
CN110987548A (zh) * 2019-10-11 2020-04-10 广州万孚生物技术股份有限公司 毛发中毒品检测方法、前处理试剂与试剂盒
US11564935B2 (en) 2019-04-17 2023-01-31 Compass Pathfinder Limited Method for treating anxiety disorders, headache disorders, and eating disorders with psilocybin
US11724985B2 (en) 2020-05-19 2023-08-15 Cybin Irl Limited Deuterated tryptamine derivatives and methods of use

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EP0699906A2 (fr) * 1994-07-25 1996-03-06 Roche Diagnostics GmbH Méthode de détecter la contamination d'une surface avec une analyte
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Cited By (25)

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EP1566640A1 (fr) * 2004-02-18 2005-08-24 Ani Biotech Oy Dispositif d' échantillonnage, méthode et leur utilisation
WO2005078441A1 (fr) * 2004-02-18 2005-08-25 Ani Biotech Oy Dispositif d'echantillonnage et son procede d'utilisation
EP1970706A1 (fr) * 2005-12-14 2008-09-17 DENKA SEIKEN Co., Ltd. Procédé de détection immunochromatographique pour staphylocoque présentant une multirésistance aux médicaments, et kit de diagnostic
EP1970706A4 (fr) * 2005-12-14 2009-08-19 Denka Seiken Kk Procédé de détection immunochromatographique pour staphylocoque présentant une multirésistance aux médicaments, et kit de diagnostic
US8431351B2 (en) 2005-12-14 2013-04-30 Denka Seiken Co., Ltd. Immunochromatography detection of multidrug-resistant Staphylococcus and diagnostic kit
EP3408672A4 (fr) * 2016-01-27 2019-10-23 Undercover Colors, Inc. Procédés et appareil pour détecter des composés dans des liquides
CN105973632A (zh) * 2016-05-05 2016-09-28 中国农业科学院烟草研究所 植物根系分泌物发生及收集装置及其收集方法
CN105973632B (zh) * 2016-05-05 2019-01-25 中国农业科学院烟草研究所 植物根系分泌物发生及收集装置及其收集方法
US11149044B2 (en) 2017-10-09 2021-10-19 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11629159B2 (en) 2017-10-09 2023-04-18 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US10947257B2 (en) 2017-10-09 2021-03-16 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US10954259B1 (en) 2017-10-09 2021-03-23 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US10519175B2 (en) 2017-10-09 2019-12-31 Compass Pathways Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11180517B2 (en) 2017-10-09 2021-11-23 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11447510B2 (en) 2017-10-09 2022-09-20 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11505564B2 (en) 2017-10-09 2022-11-22 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11939346B2 (en) 2017-10-09 2024-03-26 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11851451B2 (en) 2017-10-09 2023-12-26 Compass Pathfinder Limited Preparation of psilocybin, different polymorphic forms, intermediates, formulations and their use
US11738035B2 (en) 2019-04-17 2023-08-29 Compass Pathfinder Limited Method for treating anxiety disorders, headache disorders, and eating disorders with psilocybin
US11564935B2 (en) 2019-04-17 2023-01-31 Compass Pathfinder Limited Method for treating anxiety disorders, headache disorders, and eating disorders with psilocybin
CN110987548A (zh) * 2019-10-11 2020-04-10 广州万孚生物技术股份有限公司 毛发中毒品检测方法、前处理试剂与试剂盒
US11724985B2 (en) 2020-05-19 2023-08-15 Cybin Irl Limited Deuterated tryptamine derivatives and methods of use
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US11834410B2 (en) 2020-05-19 2023-12-05 Cybin Irl Limited Deuterated tryptamine derivatives and methods of use
US11958807B2 (en) 2020-05-19 2024-04-16 Cybin Irl Limited Deuterated tryptamine derivatives and methods of use

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