CN111724841A - Information storage method based on biological protein - Google Patents
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Abstract
The invention relates to the field of information storage, in particular to an information storage method based on biological protein, which comprises the following steps: s1, preparing a biological protein film doped or undoped with functional groups; s2, coding information to be stored; s3, storing the coded information and the information in the functional groups in the biological protein membrane; the invention can store biological information, can write in and read digital information in situ, can realize repeated writing or erasing of the digital information, and can resist severe conditions such as high temperature, high humidity, irradiation, magnetic field and the like.
Description
Technical Field
The invention relates to the field of information storage, in particular to an information storage method based on biological protein.
Background
Over the past two decades, information storage has developed a number of strategies including: deep or extreme ultraviolet light sources, dual beam systems and 3D storage architectures are used to increase the optical storage density to hundreds of Gb/inch 2. However, to achieve high spatial resolution, many of these methods inevitably involve complex processes that are time and cost inefficient. Furthermore, they use conventional optics that are limited by diffraction limits and do not improve storage density well above current industry standards.
Scattering-type scanning near-field optical microscopy, originally used to achieve super-resolution imaging beyond the diffraction limit, offers a promising alternative strategy for facilitating high-resolution nanofabrication. The use of near-field electromagnetic interactions between optical media (e.g., photosensitive substrates or nanoparticles) and extreme sub-wavelength scale incident light paves the way for nanofabrication and manipulation using photo-induced effects. For example, optical fibers or scanning metal probes (or probe arrays) with ultra-sharp tips can be used to induce nonlinear optical phenomena by high optical energy density of evanescent fields. The evanescent field can be used for processing a nanoscale region on the surface of a material, manufacturing an optical nanometer device and performing nanometer photoetching.
In order to increase the lithography efficiency and thus the efficiency of the information storage process, the dielectric material, the wavelength of the incident light and the tip size and material of the probe must be considered cooperatively. In particular, the lithographic modes in the medium (including light-induced, heat-induced, electrically-induced and stress/strain-induced phase transitions) are actually material dependent. In this case, silk fibroin, a naturally occurring protein from silkworms, is widely appreciated for its mechanical strength, optical transparency, biocompatibility, biodegradability and adjustable water solubility. Since this material can undergo radiation-induced nano-scale polymorphic transformations, it has been used as a resist-thin layer for transferring circuit patterns to semiconductor substrates by electron beam, ion beam lithography. However, these existing lithographic methods typically operate under high vacuum or rely on mask-based transfer methods.
In addition, in the information age of today, the forms of information are diversified, and the recording and storing methods of information are continuously improved. However, limited to information storage media, current information storages are mainly used to store physical information, and are not suitable for storing bio-based information with activity (bio-active) that varies with time.
Silk fibroin is also a biological material with good biocompatibility, easy doping and functionalization and easy nano processing, and the silk fibroin is used as a medium for information storage, so that the storage of physical information (namely, the coded data is stored through a surface nano structure) can be realized; in the future, the information of the living body can be stored and analyzed through the interaction between the living body and the silk fibroin.
However, how to utilize silk fibroin to store information is urgently needed to be solved by those skilled in the art.
Disclosure of Invention
In view of the above problems in the prior art, an object of the present invention is to provide an information storage method based on biological proteins, which can store biological information, can "write" and "read" digitized information in situ, can realize repeated writing or erasing of the digitized information, and can withstand severe conditions such as high temperature, high humidity, irradiation, and magnetic field.
In order to solve the above problems, the present invention provides a method for storing information based on bioprotein, comprising the steps of:
s1, preparing a biological protein film doped or undoped with functional groups;
s2, coding information to be stored;
and S3, storing the coded information and the information in the functional groups in the biological protein membrane.
Further, step S1 includes the steps of:
s11, evaporating a layer of metal material on a substrate;
s12, spin-coating a layer of biological protein solution on the substrate with the metal material evaporated to form a biological protein film.
Further, the substrate is Si, GaAs, AlN, Al2O3、ITO、SiO2SiN, glass material;
the biological protein is one of silk fibroin, sericin, spidroin, deer antler protein, egg white protein and collagen.
Further, the biological protein solution may be doped with a functional group in advance, and the functional group is one or more of a biomarker, DNA, a quantum dot, an antibiotic, a nanoparticle, a growth factor, a protease, and an antibody.
Furthermore, after the biological protein membrane is doped with a biomarker and DNA, biologically relevant information can be stored.
Further, the biological protein film can be antibacterial after being doped with antibiotics.
Further, after protease is doped into the biological protein film, the stored information can be controllably degraded.
Further, step S2 includes:
and coding the information to be stored according to a preset coding form.
Further, step S3 includes the steps of:
s31, radiating a needle point of the atomic force microscope by adopting a laser source with preset power, wherein the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein film;
and S32, moving the biological protein film, and directly writing a dot matrix structure corresponding to the coded information on the biological protein film.
Further, after step S32, the method further includes:
decoding the information stored in the biological protein film, and reading the information stored in the biological protein film.
Further, the decoding the information stored in the bioprotein membrane, reading the information stored in the bioprotein membrane comprising:
and scanning the lattice structure by adopting an atomic force microscope, decoding the information in the lattice structure, and reading the information in the lattice structure.
Further, after step S32, the method further includes:
and erasing the information stored in the biological protein film, and rewriting the information stored in the biological protein film.
Further, the erasing the information stored in the bioprotein membrane, and the rewriting the information stored in the bioprotein membrane includes:
the needle point of the atomic force microscope is radiated by an infrared laser source with the power less than or greater than the preset power to eliminate the lattice structure,
and adopting the infrared laser source with the preset power to radiate the needle point of the atomic force microscope to rewrite the lattice structure.
Due to the technical scheme, the invention has the following beneficial effects:
the information storage method based on the bioprotein can store biological information, can write in and read digital information in situ, can realize repeated writing or erasing of the digital information, and can resist severe conditions such as high temperature, high humidity, irradiation, magnetic field and the like.
Drawings
In order to more clearly illustrate the technical solution of the present invention, the drawings used in the description of the embodiment or the prior art will be briefly described below. It is obvious that the drawings in the following description are only some embodiments of the invention, and that for a person skilled in the art, other drawings can be derived from them without inventive effort.
FIG. 1 is a flow chart of a method for storing information based on biological proteins according to an embodiment of the present invention;
fig. 2 is a flowchart of step S1 provided by the embodiment of the present invention;
fig. 3 is a flowchart of step S3 provided by the embodiment of the present invention;
FIG. 4 is a schematic diagram of a lattice structure according to an embodiment of the present invention;
FIG. 5 is a partial schematic view of a lattice structure according to an embodiment of the present invention;
FIG. 6 is a schematic diagram of a lattice structure provided in the second embodiment of the present invention;
fig. 7 is a schematic diagram of a lattice structure with elimination processing provided by the second embodiment of the present invention.
FIG. 8 is a graph comparing normalized activity of a biological protein membrane incorporating biomarkers and DNA provided by embodiments of the present invention;
FIG. 9 is a graph comparing the amount of information on a biological protein membrane incorporating a biomarker and DNA provided by an example of the present invention;
FIG. 10 is a graph comparing the antimicrobial properties of a bioprotein film incorporating antibiotics provided by examples of the present invention.
FIG. 11 is a graph comparing the degradation performance of protease-incorporated bioprotein films provided by examples of the present invention;
FIG. 12 is a graph comparing other properties of the bioprotein membranes provided by the examples of the present invention.
Detailed Description
The technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the drawings in the embodiments of the present invention, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all of the embodiments. All other embodiments, which can be obtained by a person skilled in the art without any inventive step based on the embodiments of the present invention, are within the scope of the present invention.
Reference herein to "one embodiment" or "an embodiment" means that a particular feature, structure, or characteristic may be included in at least one implementation of the invention. In the description of the present invention, it is to be understood that the terms "upper", "lower", and the like, indicate orientations or positional relationships based on those shown in the drawings, are merely for convenience in describing the present invention and simplifying the description, and do not indicate or imply that the referred device or element must have a specific orientation, be constructed in a specific orientation, and be operated, and thus, should not be construed as limiting the present invention.
Example one
This embodiment provides a method for storing information based on biological protein, which is shown in fig. 1, fig. 2 and fig. 3, and includes the following steps:
s1, preparing a biological protein film doped or undoped with functional groups;
s2, coding information to be stored;
and S3, storing the coded information and the information in the functional groups in the biological protein membrane.
Specifically, step S1 includes the steps of:
s11, evaporating a layer of metal material on a substrate;
s12, spin-coating a layer of biological protein solution on the substrate with the metal material evaporated to form a biological protein film.
Further, in step S11, the metal material is one of Au, Ag, Al, Pt, Ti, Cu, Cr, and TiW.
Preferably, the metal material is Cr or Au, wherein the Cr and Au are both 10nm or 100nm thick.
Further, the concentration range of the bio-protein solution spin-coated in the step S12 is 1 wt% -30 wt%, and the rotation speed of the spin-coating is 500r/min-8000 r/min.
Preferably, the concentration of the biological protein solution is 7 wt%, and the rotation speed of the spin coating is 2500 r/min.
Further, the thickness of the bioprotein film in step S12 ranges from 10nm to 100 um.
Preferably, the thickness of the bioprotein film is 100 nm.
Specifically, the substrate is Si, GaAs, AlN, Al2O3、ITO、SiO2SiN, glass material;
the biological protein is one of silk fibroin, sericin, spidroin, deer antler protein, egg white protein and collagen.
Preferably, the substrate is a Si sheet, and the biological protein is silk fibroin.
In some embodiments, the bioprotein film can also be prepared without evaporating a layer of metal material on the substrate.
Further, the biological protein solution can be doped with a functional group in advance, the functional group is one or more of a biomarker, DNA, a quantum dot, an antibiotic, a nanoparticle, a growth factor, a protease and an antibody, wherein the mass-volume ratio of the functional group to the biological protein solution is 0.001mg/mL-1 g/mL.
As shown in fig. 8 and 9, after incorporation of a biomarker, DNA, into the bio-protein film, bio-related information comprising hemoglobin a1, albumin a2, and dextran headsugar A3, wherein the normalized activity is labeled S, it can be observed that the normalized activities of all three of hemoglobin a1, albumin a2, and dextran headsugar A3 are the same when 1 day passes; when 7 days pass, the normalized activity of the three is reduced, and the normalized activity of the albumin A2 is higher than that of the hemoglobin A1 and the glucan A3; when 14 days had elapsed, the normalized activity of the three decreased again, but the normalized activity of albumin a2 was still higher than the normalized activity of hemoglobin a1 and dextran A3.
As shown in FIG. 10, the biological protein film can resist bacteria after being doped with antibiotics, wherein a graph B1 shows that the biological protein film is doped with antibiotics, and a graph B2 shows that the biological protein film is not doped with antibiotics, and the antibacterial effect is obvious.
As shown in fig. 11, the stored information can be controllably degraded after the incorporation of protease into the bioprotein film, wherein, a graph D1 shows the bioprotein film without the incorporation of papain; FIG. D2 shows a papain-doped bioprotein film; FIG. D3 shows a papain-free bioprotein membrane after treatment in a 50 ℃ water bath; FIG. D4 shows a papain-doped bioprotein membrane after being treated in a water bath at 50 ℃; it can be observed that the information quantity of the biological protein film not doped with the papain is more than that of the biological protein film doped with the papain, and after the biological protein film is treated by water bath at 50 ℃, the information of the biological protein film not doped with the papain is retained, and the information of the biological protein film doped with the papain is eliminated.
Specifically, step S2 includes:
and coding the information to be stored according to a preset coding form, wherein the preset coding form is a binary form.
Further, a picture to be stored is selected, and binary storage information of the picture in the computer is obtained through Winhex software.
Specifically, step S3 includes the steps of:
s31, radiating a needle point of the atomic force microscope by adopting a laser source with preset power, wherein the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein film;
and S32, moving the biological protein film, and directly writing a dot matrix structure corresponding to the coded information on the biological protein film.
Further, the laser instantaneous power range radiated by the laser source in step S31 is 0.01mW to 100W.
Preferably, the laser instantaneous power radiated by the laser source is 300mW, while the laser wavelength radiated by the laser source is 6.06 μm.
Further, the laser source with preset power is adopted to radiate the needle tip of the atomic force microscope, and the laser source is mainly used for causing the biological protein morphology below the needle tip of the atomic force microscope to change, and the change trend is to change from flat to convex.
Further, the absorption spectrum of the bioprotein film in step S31 includes two absorption peaks, one absorption peak being an uncrosslinked silk fibroin absorption peak at 1650cm-1At least one of (1) and (b); another absorption peak is cross-linked silk fibroin absorption peak at 1625cm-1To (3).
Further, the radiation frequency of the laser source may or may not correspond to the absorption spectrum of the bioprotein film.
Further, the atomic force microscope is in the tapping mode in step S31.
Further, the rate of moving the bio-protein film in step S32 is 10nm/ms to 10 μm/ms.
Referring to FIGS. 4 and 5, the protruding sites on the bioprotein film are defined as "1" and the non-protruding sites are defined as "0" in the lattice structure in step S32, corresponding to the predetermined coding pattern in step S2.
Preferably, the convex points and the non-convex points on the bioprotein film in the lattice structure are arranged at an interval period of 100 nm.
Specifically, after step S32, the method further includes:
decoding the information stored in the biological protein film, and reading the information stored in the biological protein film.
Further, the decoding the information stored in the bioprotein membrane, reading the information stored in the bioprotein membrane comprising:
scanning the lattice structure by adopting an atomic force microscope, decoding information in the lattice structure, reading the information in the lattice structure, wherein convex points and non-convex points on the biological protein film in the lattice structure after the atomic force microscope is scanned are set by taking 100nm as an interval period, and then the information in the lattice structure is read.
As shown in fig. 12, it was observed that the bioprotein-based information storage method can withstand severe conditions such as high temperature, high humidity, irradiation, and magnetic field, where BP is a curve before processing and AP is a curve after processing.
The embodiment one provides an information storage method based on biological protein, which can store biological information and can write and read digital information in situ.
Example two
The second embodiment provides a method for storing information based on biological protein, which is shown in fig. 1, fig. 2 and fig. 3, and includes the following steps:
s1, preparing a biological protein film doped or undoped with functional groups;
s2, coding information to be stored;
and S3, storing the coded information and the information in the functional groups in the biological protein membrane.
Specifically, step S1 includes the steps of:
s11, evaporating a layer of metal material on a substrate;
s12, spin-coating a layer of biological protein solution on the substrate with the metal material evaporated to form a biological protein film.
Further, in step S11, the metal material is one of Au, Ag, Al, Pt, Ti, Cu, Cr, and TiW.
Preferably, the metal material is Cr or Au, wherein the Cr and Au are both 10nm or 100nm thick.
Further, the concentration range of the bio-protein solution spin-coated in the step S12 is 1 wt% -30 wt%, and the rotation speed of the spin-coating is 500r/min-8000 r/min.
Preferably, the concentration of the biological protein solution is 7 wt%, and the rotation speed of the spin coating is 2500 r/min.
Further, the thickness of the bioprotein film in step S12 ranges from 10nm to 100 um.
Preferably, the thickness of the bioprotein film is 100 nm.
Specifically, the substrate is Si, GaAs, AlN, Al2O3、ITO、SiO2SiN, glass material;
the biological protein is one of silk fibroin, sericin, spidroin, deer antler protein, egg white protein and collagen.
Preferably, the substrate is a Si sheet, and the biological protein is silk fibroin.
In some embodiments, the bioprotein film can also be prepared without evaporating a layer of metal material on the substrate.
Further, the biological protein solution can be doped with a functional group in advance, the functional group is one or more of a biomarker, DNA, a quantum dot, an antibiotic, a nanoparticle, a growth factor, a protease and an antibody, wherein the mass-volume ratio of the functional group to the biological protein solution is 0.001mg/mL-1 g/mL.
As shown in fig. 8 and 9, after incorporation of a biomarker, DNA, into the bio-protein film, bio-related information comprising hemoglobin a1, albumin a2, and dextran headsugar A3, wherein the normalized activity is labeled S, it can be observed that the normalized activities of all three of hemoglobin a1, albumin a2, and dextran headsugar A3 are the same when 1 day passes; when 7 days pass, the normalized activity of the three is reduced, and the normalized activity of the albumin A2 is higher than that of the hemoglobin A1 and the glucan A3; when 14 days had elapsed, the normalized activity of the three decreased again, but the normalized activity of albumin a2 was still higher than the normalized activity of hemoglobin a1 and dextran A3.
As shown in FIG. 10, the biological protein film can resist bacteria after being doped with antibiotics, wherein a graph B1 shows that the biological protein film is doped with antibiotics, and a graph B2 shows that the biological protein film is not doped with antibiotics, and the antibacterial effect is obvious.
As shown in fig. 11, the stored information can be controllably degraded after the incorporation of protease into the bioprotein film, wherein, a graph D1 shows the bioprotein film without the incorporation of papain; FIG. D2 shows a papain-doped bioprotein film; FIG. D3 shows a papain-free bioprotein membrane after treatment in a 50 ℃ water bath; FIG. D4 shows a papain-doped bioprotein membrane after being treated in a water bath at 50 ℃; it can be observed that the information quantity of the biological protein film not doped with the papain is more than that of the biological protein film doped with the papain, and after the biological protein film is treated by water bath at 50 ℃, the information of the biological protein film not doped with the papain is retained, and the information of the biological protein film doped with the papain is eliminated.
Specifically, step S2 includes:
and coding the information to be stored according to a preset coding form, wherein the preset coding form is a binary form.
Further, a picture to be stored is selected, and binary storage information of the picture in the computer is obtained through Winhex software.
Specifically, step S3 includes the steps of:
s31, radiating a needle point of the atomic force microscope by adopting a laser source with preset power, wherein the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein film;
and S32, moving the biological protein film, and directly writing a dot matrix structure corresponding to the coded information on the biological protein film.
Further, the laser instantaneous power range radiated by the laser source in step S31 is 0.01mW to 100W.
Preferably, the laser instantaneous power radiated by the laser source is 300mW, while the laser wavelength radiated by the laser source is 6.06 μm.
Further, the laser source with preset power is adopted to radiate the needle tip of the atomic force microscope, and the laser source is mainly used for causing the biological protein morphology below the needle tip of the atomic force microscope to change, and the change trend is to change from flat to convex.
Further, the absorption spectrum of the bioprotein film in step S31 includes two absorption peaks, one absorption peak being an uncrosslinked silk fibroin absorption peak at 1650cm-1At least one of (1) and (b); another absorption peak is cross-linked silk fibroin absorption peak at 1625cm-1To (3).
Further, the radiation frequency of the laser source may or may not correspond to the absorption spectrum of the bioprotein film.
Further, the atomic force microscope is in the tapping mode in step S31.
Further, the rate of moving the bio-protein film in step S32 is 10nm/ms to 10 μm/ms.
Further, step S32 specifies the salient points on the bioprotein film as "1" and the non-salient points as "0" within the lattice structure, corresponding to the predetermined coding pattern in step S2.
Preferably, the protruding points and the non-protruding points on the bio-protein film in the lattice structure are arranged at intervals of 100nm, and as shown in fig. 6, 16 points are written in two rows, and the codes are "11111111" and "11111111111", respectively.
Specifically, after step S32, the method further includes:
and erasing the information stored in the biological protein film, and rewriting the information stored in the biological protein film.
Further, the erasing the information stored in the bioprotein membrane, and the rewriting the information stored in the bioprotein membrane includes:
the needle point of the atomic force microscope is radiated by an infrared laser source with the power less than or greater than the preset power to eliminate the lattice structure,
and adopting the infrared laser source with the preset power to radiate the needle point of the atomic force microscope to rewrite the lattice structure.
Further, when the preset power is changed from small to large, the dot matrix structure is changed from convex points to concave points, and vice versa.
Preferably, as shown in FIG. 7, the query results in ASCII encodings for the letters "U" and "T" of "01010101" and "01010100", respectively. Increasing the instantaneous power of the laser source radiation to 1W, and erasing the dot in the corresponding position of the lattice structure, namely changing 1 into 0, to obtain the ASCII codes '01010101' and '01010100' of U and T, so as to realize the erasing.
Further, convex points and non-convex points on the bioprotein film in the lattice structure after atomic force microscope scanning are set at intervals of 100nm of the lattice structure which is eliminated, and information in the lattice structure is read.
As shown in fig. 12, it was observed that the bioprotein-based information storage method can withstand severe conditions such as high temperature, high humidity, irradiation, and magnetic field, where BP is a curve before processing and AP is a curve after processing.
The second embodiment provides an information storage method based on biological protein, which can realize repeated writing or erasing of digital information.
The foregoing description has disclosed fully preferred embodiments of the present invention. It should be noted that those skilled in the art can make modifications to the embodiments of the present invention without departing from the scope of the appended claims. Accordingly, the scope of the appended claims is not to be limited to the specific embodiments described above.
Claims (13)
1. A method for storing information based on biological protein is characterized by comprising the following steps:
s1, preparing a biological protein film doped or undoped with functional groups;
s2, coding information to be stored;
and S3, storing the coded information and the information in the functional groups in the biological protein membrane.
2. The bioprotein-based information storage method of claim 1, wherein the step S1 comprises the steps of:
s11, evaporating a layer of metal material on a substrate;
s12, spin-coating a layer of biological protein solution on the substrate with the metal material evaporated to form a biological protein film.
3. The bioprotein-based information storage method of claim 2,
the substrate is Si, GaAs, AlN or Al2O3、ITO、SiO2SiN, glass material; the biological protein is one of silk fibroin, sericin, spidroin, deer antler protein, egg white protein and collagen.
4. The method for storing information based on biological protein as claimed in claim 2, wherein the biological protein solution can be doped with functional groups in advance, and the functional groups are one or more of biomarkers, DNA, quantum dots, antibiotics, nanoparticles, growth factors, proteases and antibodies.
5. The method for storing information based on biological protein as claimed in claim 4, wherein the biological protein film is incorporated with biomarker and DNA to store biologically relevant information.
6. The method for storing information based on bioprotein of claim 4, wherein said bioprotein membrane is antibacterial after being incorporated with antibiotics.
7. The method for storing biological protein-based information according to claim 4, wherein the stored information can be controllably degraded after the incorporation of protease into the biological protein film.
8. The bioprotein-based information storage method of claim 1, wherein step S2 comprises:
and coding the information to be stored according to a preset coding form.
9. The bioprotein-based information storage method of claim 1, wherein the step S3 comprises the steps of:
s31, radiating a needle point of the atomic force microscope by adopting a laser source with preset power, wherein the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein film;
and S32, moving the biological protein film, and directly writing a dot matrix structure corresponding to the coded information on the biological protein film.
10. The bioprotein-based information storage method of claim 9, wherein after step S32, the method further comprises:
decoding the information stored in the biological protein film, and reading the information stored in the biological protein film.
11. The bioprotein-based information storage method of claim 10,
the decoding information stored in the bioprotein membrane, reading information stored in the bioprotein membrane comprising:
and scanning the lattice structure by adopting an atomic force microscope, decoding the information in the lattice structure, and reading the information in the lattice structure.
12. The bioprotein-based information storage method of claim 9, wherein after step S32, the method further comprises:
and erasing the information stored in the biological protein film, and rewriting the information stored in the biological protein film.
13. The bioprotein-based information storage method of claim 12,
the erasing the information stored in the bioprotein membrane, and the rewriting the information stored in the bioprotein membrane includes:
the needle point of the atomic force microscope is radiated by an infrared laser source with the power less than or greater than the preset power to eliminate the lattice structure,
and adopting the infrared laser source with the preset power to radiate the needle point of the atomic force microscope to rewrite the lattice structure.
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| CN105633112A (en) * | 2015-12-30 | 2016-06-01 | 西安电子科技大学 | Super-light resistive random access memory and preparation method thereof |
| CN110431148A (en) * | 2017-01-10 | 2019-11-08 | 罗斯威尔生命技术公司 | Method and system for the storage of DNA data |
| CN106527045A (en) * | 2017-01-20 | 2017-03-22 | 中国科学院上海微系统与信息技术研究所 | Optical component-based method for information hiding and reproduction |
| CN110892485A (en) * | 2017-02-22 | 2020-03-17 | 特韦斯特生物科学公司 | Nucleic acid based data storage |
| CN107331773A (en) * | 2017-06-28 | 2017-11-07 | 深圳大学 | A kind of degradable albumen based transistor type memory and preparation method thereof |
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