CN115819498B - Antioxidant polypeptide penetrating blood brain barrier as well as preparation method and application thereof - Google Patents
Antioxidant polypeptide penetrating blood brain barrier as well as preparation method and application thereof Download PDFInfo
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- CN115819498B CN115819498B CN202211087558.9A CN202211087558A CN115819498B CN 115819498 B CN115819498 B CN 115819498B CN 202211087558 A CN202211087558 A CN 202211087558A CN 115819498 B CN115819498 B CN 115819498B
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Abstract
The invention discloses an antioxidant polypeptide penetrating through a blood brain barrier, and a preparation method and application thereof, and belongs to the technical field of preparation of functional active peptides. It comprises one or more of SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 or SEQ ID NO. 5. The antioxidant polypeptide obtained by fermenting yak milk by lactobacillus plantarum JLAU103 has high antioxidant activity, can penetrate through blood brain barrier and enter the brain to exert the functional activity of the antioxidant polypeptide, can be widely applied to the preparation of anti-aging functional foods, health-care products and skin-care cosmetics, can be obtained by solid-phase chemical synthesis, and has good application prospect.
Description
Technical Field
The invention relates to an antioxidant polypeptide penetrating through a blood brain barrier, and a preparation method and application thereof, and belongs to the technical field of preparation of functional active peptides.
Background
Oxidation causes rapid reaction of body functions, when oxidation and antioxidation in the body are unbalanced, neutrophil inflammatory infiltration is caused when oxidation is prone to occur, protease secretion is increased, a large amount of oxidation intermediates such as free radicals are generated, the original environment of normal metabolism of a human body is damaged, and the body is damaged, so that the microenvironment of the human body is changed. This change is considered to be an important factor for aging and disease, but brain tissue, which is the organ with the most active oxidative metabolism in the body, is more susceptible to attack by reactive oxygen species, causes imbalance of the oxidation-antioxidation system in cells, induces neuroinflammation and apoptosis, damages mitochondrial function, causes synaptic plasticity dysfunction, damages blood brain barrier integrity, neuron toxic edema, DNA oxidative damage, abnormal protein expression, etc., and further causes neuronal damage, decline of learning and memory capacity, and the serious person progresses to dementia. Under certain conditions, the peptide bonds of proteins break to form protein hydrolysates with antioxidant properties, which contain only a few hydrophobic or other types of amino acids, called antioxidant peptides, which regulate body availability, bind to free radicals and scavenge free radicals, protecting human tissues and organs from excess free radicals.
The Blood Brain Barrier (BBB) is a defence mechanism specific to the mammalian central nervous system that prevents pathogenic factors in the peripheral system, including bacterial and viral pathogens, from entering the brain tissue from the blood, maintains normal physiology of the brain, and selectively transports nutrients from the peripheral system to the central nervous system. Thus, the structure of the BBB is different from the surrounding vasculature. First, the tight junctions and adhesion junctions of the BBB confer megaohm (mΩ) resistance and prevent entry of molecules greater than 500Da, and the matrix proteins, pericytes and astrocyte ends further increase the resistance of the BBB. The selective transport of the blood brain barrier, while maintaining a relatively stable environment within the nervous system, also impedes the delivery of many neuroprotective factors within the brain. Almost all macromolecular substances and 98% of small molecular substances have difficulty crossing the blood brain barrier. To achieve protection of brain tissue using antioxidant peptides, the problem of its passage through the blood brain barrier is first addressed.
Disclosure of Invention
The invention aims to overcome the defects of the prior art and provides an antioxidant polypeptide penetrating through a blood brain barrier, and a preparation method and application thereof.
The aim of the invention is realized by the following technical scheme: an antioxidant polypeptide penetrating the blood brain barrier, comprising one or more of SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 or SEQ ID NO. 5.
It is another object of the present invention to provide a method for preparing the above antioxidant polypeptide penetrating the blood brain barrier, comprising the steps of:
s1, inoculating lactobacillus plantarum JLAU103 into yak milk, fermenting for 16-20 hours, and then performing solid-liquid separation to obtain supernatant;
s2, performing ultrafiltration treatment on the supernatant obtained in the step S1, and collecting fermentation supernatant with the molecular weight of less than 3 kDa;
s3, performing gel chromatography on the fermentation supernatant collected in the step S2, and collecting components with retention time of 17000-20000S; and (3) performing gel chromatography purification again on the collected components, wherein the gel particle size adopted in the purification is smaller than that adopted in the first gel chromatography, and collecting the components with retention time of 8000-9000 s to obtain the antioxidant polypeptide.
Further, lactobacillus plantarum JLAU103 inoculated in the S1 is obtained through inoculating and fermenting a yak seed culture medium, wherein the yak seed culture medium is an MRS culture medium added with fresh yak milk, the inoculation amount is 1-3%, and the volume ratio of the yak seed culture medium to the yak milk is 1:9 to 11.
Further, lactobacillus plantarum JLAU103 inoculated in the yak seed culture medium is subjected to recovery for 1-3 times, the recovery is carried out in the liquid MRS culture medium, and the recovery time is 20-28 hours.
Further, in S1, the solid-liquid separation adopts centrifugal treatment, the centrifugal rotation speed is 5000rpm/min, and the centrifugal time is 10-15 min.
Further, the first gel chromatography in S3 uses Sephadex G-25, and the purification uses Sephadex G-15.
Further, the first gel chromatography elution flow rate in S3 is 1.25mL/min, the detection wavelength is 280nm, and the peak component in the retention time is collected.
Further, the purification elution flow rate in S3 was 0.5mL/min, the detection wavelength was 280nm, and the peak component in the retention time was collected. And (3) identifying the optimal component from the components collected after purification by mass spectrum to obtain the amino acid sequence described in the invention.
The invention further provides a method for synthesizing the antioxidant polypeptide penetrating the blood brain barrier by adopting solid-phase chemistry according to the amino acid sequence.
The invention also provides application of the antioxidant polypeptide penetrating through the blood brain barrier in preparation of functional foods, health products and skin care cosmetics.
The beneficial effects of the invention are as follows:
the antioxidant polypeptide obtained by fermenting yak milk with lactobacillus plantarum has high antioxidant activity, can penetrate through blood brain barrier, enter the brain to exert the functional activity, improves the learning and memory capacity of a user, and protects neurons and synapses from damage. The antioxidant polypeptide can be widely applied to the preparation of anti-aging functional foods, health products and skin care cosmetics, can be obtained through solid-phase chemical synthesis, and has good application prospect.
Drawings
FIG. 1 shows the sequence information of an antioxidant polypeptide according to an embodiment of the present invention.
FIG. 2 shows the structure of an antioxidant polypeptide according to an embodiment of the present invention.
FIG. 3 is an elution diagram of the first chromatography in S3 of the second embodiment of the present invention.
FIG. 4 shows the antioxidant activity of the peak components of the first chromatography in example two S3 of the present invention.
FIG. 5 is an elution diagram of purification chromatography in S3 of the second embodiment of the present invention.
FIG. 6 shows the antioxidant activity of the peak components of the purification chromatography in example two S3 of the present invention.
FIG. 7 shows the antioxidant activity of the polypeptide prepared in example III of the present invention.
FIG. 8 shows the blood brain barrier penetrating ability of LYLKPR polypeptides prepared in accordance with example III of the present invention.
Detailed Description
The technical solutions of the present invention will be clearly and completely described below with reference to the embodiments, and it is apparent that the described embodiments are only some embodiments of the present invention, but not all embodiments. All other embodiments, which can be made by a person skilled in the art without any inventive effort, are intended to be within the scope of the present invention, based on the embodiments of the present invention.
Example 1
This example provides an antioxidant polypeptide penetrating the blood brain barrier, the amino acid sequence of which is SEQ ID NO.1 (Glu-Leu-Pro-Pro (ELPP), the sequence information and structure of which are shown as a in FIGS. 1 and 2), SEQ ID NO.2 (Phe-Asp-Gly-Asp-Phe (FDGDF), the sequence information and structure of which are shown as b in FIGS. 1 and 2), SEQ ID NO.3 (Leu-Tyr-Leu-Lys-Pro-Arg (LYLKPR), the sequence information and structure of which are shown as c in FIGS. 1 and 2), SEQ ID NO.4 (Leu-Gly-Asp-Lys-Leu-Phe (DKLF), the sequence information and structure of which are shown as d in FIGS. 1 and 2), SEQ ID NO.5 (Lys-Leu-Val-Ala-Trp-Val-Pro (KLLVAWVPP)), and the sequence information and structure of which are shown as e in FIGS. 1 and 2, respectively.
Example two
The present embodiment provides a method of preparing an antioxidant polypeptide that penetrates the blood brain barrier, comprising the steps of:
s1, placing lactobacillus plantarum JLAU103 in a liquid MRS culture medium for resuscitation for 24 hours, wherein the ratio of each inoculation is 1% after three times of resuscitations. Then adding the fresh milk of the yak into an MRS culture medium to prepare a yak seed culture medium (the volume ratio of the added fresh milk of the yak to the MRS culture medium is 10:1), and inoculating the recovered lactobacillus plantarum JLAU103 into the yak seed culture medium according to the inoculation amount of 1 percent for fermentation for 24 hours. Mixing the fermentation product with yak milk according to a weight ratio of 1:10, inoculating lactobacillus plantarum JLAU103 into the yak milk, fermenting for 18 hours, centrifuging at 5000rpm/min for 15min, and collecting the supernatant.
S2, carrying out ultrafiltration treatment on the supernatant obtained in the step S1 in an ice bath, adopting a tangential flow ultrafiltration system and a Biomax modified polyethersulfone composite membrane package, adopting an ultrafiltration membrane with a membrane molecular cut-off molecular weight of 3kDa to carry out separation, and collecting fermentation supernatant with a molecular weight of less than 3 kDa.
S3, performing gel chromatography on the fermentation supernatant collected in the step S2, wherein the chromatography adopts SephadexG-25, the mass concentration of a sample is 100mg/mL, the loading amount is 10mL, the elution flow rate is 1.25mL/min, the detection wavelength is 280nm, the elution diagram is shown in figure 3, wherein the component of F1 is not in the target retention time, and the component of F2 is in the retention time period of 17000-20000S. And (3) performing gel chromatography purification again on the collected components, wherein Sephadex G-15 is adopted for purification, the mass concentration of a sample is 50mg/mL, the loading amount is 2.5mL, the elution flow rate is 0.5mL/min, the detection wavelength is 280nm, the elution diagram is shown in figure 5, wherein the components of C1 and C2 are not in the target retention time, the component of C3 is in the retention time period of 8000-9000 s, the component of C3 is collected to be the antioxidant polypeptide, and the polypeptide screened by mass spectrum identification is consistent with the amino acid sequence in the first embodiment.
Example III
This example provides another method for preparing an antioxidant polypeptide that penetrates the blood brain barrier, wherein the antioxidant polypeptide is synthesized by solid phase chemistry according to the amino acid sequence of example one, the specific procedure of the synthesis being: fmoc solid phase synthesis was used and Gemini-NX 5. Mu.C 18110A, 4.6X250 mm liquid phase column was used for purification. Mobile phase a:0.1% trichloroacetic acid and 100% acetonitrile; mobile phase B:0.1% trichloroacetic acid and 100% water.
Example IV
This example provides an antioxidant activity assay for the antioxidant polypeptides prepared in examples two and three, the antioxidant activity assay comprising the following assay items:
abts radical scavenging Activity
ABTS +, was generated from 7mMABTS reaction with 2.49mM potassium persulfate in water, then stored at Room Temperature (RT) protected from light for 16 hours. The ABTS+ solution was diluted with ethanol to an absorbance of 0.70 at 734nm prior to use. A peptide sample solution (10. Mu.L, 1 mg/mL) was added to the 190 mLABST+ solution, and the mixture was incubated in the dark at room temperature for 5min. Absorbance of the mixed solution was measured at 734nm and ABTS radical scavenging activity was calculated by the following formula using Glutathione (GSH) as a positive control:
ABTS clearance (%) =1- (A1-A2)/(A0-A3) ×100
Wherein, A0: distilled water + ABTS, A1: peptide sample solution + ABTS, A2: peptide sample solution+pbs, A3: distilled water + PBS.
The peptide sample solution is the polypeptide prepared in the third embodiment, and the calculation result is shown in fig. 7, and the antioxidant polypeptides synthesized in the third embodiment have ABTS free radical scavenging capability, wherein the antioxidant effect of the polypeptide with LYLKPR (amino acid sequence of SEQ ID NO. 3) is particularly remarkable, the antioxidant effect of the polypeptide with KLLVAWVPP (amino acid sequence of SEQ ID NO. 5) is also excellent, and other polypeptides have a certain antioxidant capability.
2. Hydroxyl radical scavenging Activity
Hydroxyl radical scavenging activity: 1mL of peptide sample solution (8 mg/mL), 1.0mL of salicylic acid (0.435 mM), 2.0mL of LFASO 4 (0.5 mM) and 1.5mLH 2 O 2 (3.0%, w/v) was added to the tube and mixed to start the reaction. The tubes were incubated at 37℃for 30 minutes. Then, absorbance was measured at 510nm, and hydroxyl radical scavenging activity was calculated by the following formula with GSH as a positive control:
hydroxyl radical scavenging Activity (%) = [1- (A1-A2)/A0 ]. Times.100
Wherein, A0: h 2 O 2 +FeSO 4 +distilled water+salicylic acid, A1: h 2 O 2 +FeSO 4 + peptide sample solution + salicylic acid, A2: h 2 O 2 +FeSO 4 + peptide sample solution + ethanol. Spectrophotometer adjusts component 0: h 2 O 2 +FeSO 4 + distilled water + ethanol.
The peptide samples used in this test were all peak fractions collected by two gel chromatographies in preparation procedure S3 of example two, and the calculation results are shown in fig. 4 and 6. As can be seen from FIG. 4, the peak fraction (F2) having a retention time of 17000 to 20000S has a higher hydroxyl radical scavenging activity among the peak fractions collected by the first gel chromatography in S3 of example II. FIG. 6 shows that the peak fractions with different retention times have higher hydroxyl radical scavenging activity among the peak fractions collected by the purification gel chromatography in S3 of example two.
3. Oxygen radical absorption Capacity determination (ORAC)
To each well of 96 Kong Yingguang plate, 25. Mu.L of a sample to be measured (peptide sample to be measured was dissolved in 75mmol/LPBS buffer at a sample concentration of 100 mmol/L), 25. Mu.L of 75mmol/L PBS buffer and 150. Mu.L of 63mmol/L sodium Fluorescein (FL) were added, 10s were shaken, pre-heated at 37℃for 20min, 25. Mu.L of 6mmol/L azobisisobutyrimidine hydrochloride (AAPH, as-prepared) was rapidly added to each well with a multi-well pipette, and 96 Kong Yingguang plates were placed in a fluorescent microplate analyzer pre-heated in advance (37 ℃) and the fluorescent intensity of each well was measured once every 4min at an excitation wavelength of 485nm and the measurement was terminated when the fluorescent intensity was 5% of the initial fluorescent intensity. The area under the fluorescence decay curve (AUC) was calculated using the approximate integration method with respect to the fluorescence intensity:
AUC＝2×[(f0+f1+……+fn-1+fn)-f0-fn]/2×Δt
wherein fn is the relative fluorescence intensity of the nth measurement point; Δt is the interval time between adjacent time points of 4min. The measurement results are expressed as ORAC values, and the ORAC values of the samples to be measured are expressed as umol/Trolox/g.
ORAC value= (AUC Sample of -AUC Blank space )/(AUC trolox -AUC Blank space )×C sample/Ctrolox
Wherein AUC Sample of : area under fluorescence decay curve, AUC of sample Blank space : area under fluorescence decay curve without sample, AUC trolox : area under the fluorescence decay curve of the trolox standard.
The peptide samples used in this assay were all peak fractions collected by two gel chromatographies in preparation process S3 of example two and the polypeptides prepared in example three, and the calculated results are shown in FIGS. 4, 6 and 7. As can be seen from FIG. 4, the peak component (F2) having a retention time of 17000 to 20000S has a higher oxygen radical absorption capacity among the peak components collected by the first gel chromatography in S3 of example II. FIG. 6 shows that, of the peak components collected by the purification gel chromatography in S3 of example II, the peak component (C3) having a retention time of 8000 to 9000S has a stronger oxygen radical absorption capacity. As shown in the calculation results of FIG. 7, LYLKPR (amino acid sequence of SEQ ID NO. 3) has optimal oxygen radical absorption capacity, KLLVAWVPP (amino acid sequence of SEQ ID NO. 5) times, and other polypeptides have better oxygen radical absorption capacity and antioxidant capacity.
4.Fe 2+ Chelating activity
2.75mL of water, 1mL of peptide sample solution (8 mg/mL), 0.2mL of ferrozine solution (5 mM), and 0.05mL of FeCl 2 The solution (4 mM) was mixed and shaken vigorously and incubated at room temperature for 10 minutes. The absorbance of the reaction mixture was measured at 562 nm. Fe (Fe) 2+ The chelating activity is calculated from the following formula:
Fe 2+ chelating activity (%) = [ A0- (A1-Ai)/A0 ]]×100
Wherein A0 is the absorbance of the mixed solution containing no peptide sample, A1 is the absorbance of the mixed solution containing all the above components, and Ai is the absorbance of the mixed solution containing no FeCl 2 Absorbance of the mixed solution of (a) and (b).
The peptide samples used in this test were all peak fractions collected by two gel chromatographies in preparation procedure S3 of example two, and the calculation results are shown in fig. 4 and 6. As can be seen from FIG. 4, the peak component (F2) having a retention time of 17000 to 20000S among the peak components collected by the first gel chromatography in S3 of example II has higher Fe 2+ Chelating activity. FIG. 6 also shows that, of the peak components collected by the purification gel chromatography in S3 of example II, the peak component (C3) having a retention time of 8000 to 9000S has stronger Fe 2+ Chelating activity.
Example five
This example provides the antioxidant polypeptide LYLKPR (amino acid) prepared in example threeThe blood brain barrier penetrating ability of the sequence SEQ ID NO. 3) is measured by the following specific measuring method: using transwell plates, 0.5ml of cultured BEND3 cells (5X 10) were added to each upper well 4 Well), 1.5ml of cell-free complete medium was added to the lower macropores. The culture medium is replaced every two days until the resistance reaches 180Ω·cm 2 Indicating that the blood brain barrier reaches a stable state, and establishing a blood brain barrier model. 200. Mu.M peptide LYLKPR 2h was added to the upper wells, and the medium was removed from the small and large wells and the reverse phase high performance liquid chromatography (RP-HPLC) was used to calculate whether the peptide could cross the blood brain barrier.
As a result, as shown in FIG. 8, most LYLKPR polypeptides are able to cross the blood brain barrier and enter the central nervous system of the brain to exert their antioxidant activity.
From the fourth and fifth embodiments, the antioxidant polypeptide of the present invention can be widely used for preparing functional food and health care products for resisting aging and improving memory, and can also be used for preparing skin care cosmetics for resisting aging
The foregoing is merely a preferred embodiment of the invention, and it is to be understood that the invention is not limited to the form disclosed herein but is not to be construed as excluding other embodiments, but is capable of numerous other combinations, modifications and environments and is capable of modifications within the scope of the inventive concept, either as taught or as a matter of routine skill or knowledge in the relevant art. And that modifications and variations which do not depart from the spirit and scope of the invention are intended to be within the scope of the appended claims.
Claims (3)
1. An antioxidant polypeptide that penetrates the blood brain barrier, characterized in that: the amino acid sequence of the polypeptide is shown as SEQ ID NO. 3.
2. A method of preparing the blood-brain barrier penetrating antioxidant polypeptide of claim 1, wherein: the amino acid sequence of claim 1 is synthesized using solid phase chemistry.
3. The use of the antioxidant polypeptide penetrating the blood brain barrier of claim 1 for the preparation of functional foods, health products and skin care cosmetics.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109666973A (en) * | 2018-11-21 | 2019-04-23 | 北京大学 | It is a kind of across the peptide library of blood-brain barrier and its screening technique |
| CN114288414A (en) * | 2021-12-07 | 2022-04-08 | 深圳先进技术研究院 | Polypeptide crossing blood brain barrier, derivative and application thereof |
| CN114751957A (en) * | 2022-03-15 | 2022-07-15 | 吉林农业大学 | Memory-improving derived peptide with high oxidation resistance and capability of penetrating blood brain barrier and application thereof |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109666973A (en) * | 2018-11-21 | 2019-04-23 | 北京大学 | It is a kind of across the peptide library of blood-brain barrier and its screening technique |
| CN114288414A (en) * | 2021-12-07 | 2022-04-08 | 深圳先进技术研究院 | Polypeptide crossing blood brain barrier, derivative and application thereof |
| CN114751957A (en) * | 2022-03-15 | 2022-07-15 | 吉林农业大学 | Memory-improving derived peptide with high oxidation resistance and capability of penetrating blood brain barrier and application thereof |
Non-Patent Citations (2)
| Title |
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| 治疗性多肽靶向中枢神经系统给药的研究进展;吴庆建;《中华神经医学杂志》;全文 * |
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