CN111724841B - An information storage method based on biological protein - Google Patents

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

An information storage method based on biological protein

technical field

The invention relates to the field of information storage, in particular to an information storage method based on biological proteins.

Background technique

Over the past two decades, many strategies have been developed for information storage, including: deep-ultraviolet or far-ultraviolet light sources, dual-beam systems, and 3D storage architectures to increase optical storage densities to hundreds of Gb/inch2. However, in order to obtain high spatial resolution, many of these methods inevitably involve time- and cost-inefficient complex procedures. Furthermore, they use conventional optics, which are limited by the diffraction limit and cannot increase storage densities much higher than current industry standards.

Scattering-type scanning near-field optical microscopy was originally used to achieve super-resolution imaging beyond the diffraction limit, providing a promising alternative strategy to facilitate high-resolution nanofabrication. Harnessing the near-field electromagnetic interactions between optical media (e.g., photosensitive substrates or nanoparticles) and incident light at extreme subwavelength scales paves the way for nanofabrication and manipulation using photoinduced effects. For example, nonlinear optical phenomena can be induced by the high optical energy density of evanescent fields using optical fibers or scanning metal probes (or probe arrays) with ultra-sharp tips. Evanescent fields can be used to treat nanoscale regions of material surfaces, fabrication of optical nanodevices, and nanolithography.

In order to improve the efficiency of lithography, 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 taken into consideration in synergy. Specifically, the lithographic modes in the medium, including photo-induced, thermally-induced, electrical-induced and stress/strain-induced phase transitions, are actually material dependent. In this context, silk fibroin, a naturally occurring protein from the silkworm, is widely appreciated for its mechanical strength, optical transparency, biocompatibility, biodegradability, and tunable water solubility. Because the material can undergo radiation-induced nanoscale polymorphic transitions, it has been used as a resist-thin layer for transferring circuit patterns onto semiconductor substrates by electron beam, ion beam lithography. However, these existing lithography methods typically operate under high vacuum or rely on mask-based transfer methods.

In addition, in today's information age, the forms of information are various, and the way of recording and storing information is also constantly improving. However, limited by the information storage medium, the current information storage is mainly used to store physical information, and is not suitable for storing biological-based information with bio-active changes over time.

Silk fibroin is also a biomaterial with good biocompatibility, easy doping and functionalization, and easy nanofabrication. Using silk fibroin as a medium for information storage can not only achieve physical information storage (that is, storage through surface nanostructures). Encoded data); in the future, the information of living organisms can also be stored and analyzed through the interaction between living organisms and silk fibroin.

However, how to use silk fibroin to store information is an urgent need for those skilled in the art.

SUMMARY OF THE INVENTION

In view of the above problems of the prior art, the purpose of the present invention is to provide an information storage method based on biological proteins, which can store biological information, "write" and "read" digital information in situ, and realize the repetition of digital information. Write or erase, while being able to withstand harsh conditions such as high temperature, high humidity, radiation, and magnetic fields.

In order to solve the above problems, the present invention provides a biological protein-based information storage method, comprising the following steps:

S1. Preparation of biological protein membranes doped or undoped with functional groups;

S2. Encode the information to be stored;

S3. Store the encoded information and the information in the functional group in the biological protein membrane.

Further, step S1 includes the following steps:

S11. Evaporate a layer of metal material on the substrate;

S12. Spin coating a layer of biological protein solution on the substrate on which the metal material is evaporated to form a biological protein film.

Further, the substrate is one of Si, GaAs, AlN, Al2O3, ITO, SiO2, SiN, and glass materials;

The biological protein is one of silk fibroin, sericin, spider silk, staghorn, egg white and collagen.

Further, the biological protein solution can be pre-mixed with functional groups, and the functional groups are one or more of biomarkers, DNA, quantum dots, antibiotics, nanoparticles, growth factors, proteases, and antibodies. .

Further, after incorporating biomarkers and DNA into the biological protein membrane, biological-related information can be stored.

Further, after incorporating antibiotics into the biological protein membrane, it can be antibacterial.

Further, after the protease is incorporated into the biological protein membrane, the stored information can be degraded in a controllable manner.

Further, step S2 includes:

The information to be stored is encoded according to the preset encoding form.

Further, step S3 includes the following steps:

S31. Use a laser source of preset power to irradiate the needle tip of an atomic force microscope, and the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein membrane;

S32. Move the biological protein membrane, and directly write the lattice structure corresponding to the encoded information on the biological protein membrane.

Further, after step S32, the method further includes:

Decoding the information stored in the biological protein membrane, and reading the information stored in the biological protein membrane.

Further, decoding the information stored in the biological protein membrane, and reading the information stored in the biological protein membrane includes:

The lattice structure is scanned by an atomic force microscope, the information in the lattice structure is decoded, and the information in the lattice structure is read.

Further, after step S32, the method further includes:

The information stored in the biological protein membrane is erased, and the information stored in the biological protein membrane is rewritten.

Further, erasing the information stored in the biological protein membrane, and rewriting the information stored in the biological protein membrane includes:

Using an infrared laser source with a power smaller than or greater than the preset power to irradiate the tip of the atomic force microscope to eliminate the lattice structure,

Using the infrared laser source with the preset power to irradiate the tip of an atomic force microscope, the lattice structure is rewritten.

Due to the above-mentioned technical scheme, the present invention has the following beneficial effects:

The biological protein-based information storage method of the present invention can store biological information, "write" and "read" digital information in situ, realize repeated writing or erasing of digital information, and can withstand high temperature at the same time. , high humidity, radiation, magnetic fields and other harsh conditions.

Description of drawings

In order to illustrate the technical solutions of the present invention more clearly, the following will briefly introduce the accompanying drawings that are required to be used in the description of the embodiments or the prior art. Obviously, the drawings in the following description are only some embodiments of the present invention, and for those of ordinary skill in the art, other drawings can also be obtained from these drawings without creative effort.

1 is a flowchart of a biological protein-based information storage method provided in an embodiment of the present invention;

2 is a flowchart of step S1 provided by an embodiment of the present invention;

3 is a flowchart of step S3 provided by an embodiment of the present invention;

4 is a schematic diagram of a lattice structure provided in Embodiment 1 of the present invention;

5 is a partial schematic diagram of a lattice structure provided in Embodiment 1 of the present invention;

6 is a schematic diagram of a lattice structure provided by Embodiment 2 of the present invention;

FIG. 7 is a schematic diagram of a lattice structure that has been eliminated and processed according to Embodiment 2 of the present invention.

Figure 8 is a comparison diagram of the normalization activity of biological protein membranes incorporating biomarkers and DNA provided by the embodiment of the present invention;

Figure 9 is a comparison diagram of the amount of biological protein membrane information incorporated into biomarkers and DNA provided in an embodiment of the present invention;

FIG. 10 is a comparison diagram of the antibacterial performance of the biological protein membrane incorporating antibiotics provided in the embodiment of the present invention.

Figure 11 is a comparison diagram of the degradation performance of the biological protein membrane incorporating protease provided in the embodiment of the present invention;

FIG. 12 is a comparison diagram of other properties of the biological protein membrane provided in the embodiment of the present invention.

Detailed ways

The technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the accompanying drawings in the embodiments of the present invention. Obviously, the described embodiments are only a part of the embodiments of the present invention, but not all of the embodiments. Based on the embodiments of the present invention, all other embodiments obtained by those of ordinary skill in the art without creative work fall within the protection scope of the present invention.

Reference herein to "one embodiment" or "an embodiment" refers to a particular feature, structure, or characteristic that may be included in at least one implementation of the present invention. In the description of the present invention, it should be understood that the orientation or positional relationship indicated by the terms "upper", "lower", etc. is based on the orientation or positional relationship shown in the accompanying drawings, and is only for the convenience of describing the present invention and simplifying the description, It is not intended to indicate or imply that the device or element referred to must have a particular orientation, be constructed and operate in a particular orientation, and therefore should not be construed as limiting the invention.

Example 1

The first embodiment provides a biological protein-based information storage method, which is shown in FIG. 1 , FIG. 2 and FIG. 3 , and includes the following steps:

S1. Preparation of biological protein membranes doped or undoped with functional groups;

S2. Encode the information to be stored;

S3. Store the encoded information and the information in the functional group in the biological protein membrane.

Specifically, step S1 includes the following steps:

S11. Evaporate a layer of metal material on the substrate;

S12. Spin coating a layer of biological protein solution on the substrate on which the metal material is evaporated to form a biological protein film.

Further, the metal material in step S11 is one of Au, Ag, Al, Pt, Ti, Cu, Cr, and TiW.

Preferably, the metal material is Cr or Au, wherein the thickness of both Cr and Au is 10 nm or 100 nm.

Further, the concentration range of the biological protein solution spin-coated in step S12 is 1wt%-30wt%, and the rotation speed of the spin-coating is 500r/min-8000r/min.

Preferably, the concentration of the biological protein solution is 7wt%, and the rotation speed of the spin coating is 2500r/min.

Further, the thickness of the biological protein membrane in step S12 ranges from 10 nm to 100 um.

Preferably, the thickness of the biological protein membrane is 100 nm.

Specifically, the substrate is one of Si, GaAs, AlN, Al ₂ O ₃ , ITO, SiO ₂ , SiN, and glass materials;

The biological protein is one of silk fibroin, sericin, spider silk, staghorn, egg white and collagen.

Preferably, the substrate is a Si sheet, and the biological protein is silk fibroin.

In some embodiments, a biological protein film can also be prepared without evaporating a layer of metal material on the substrate.

Further, the biological protein solution can be pre-mixed with functional groups, and the functional groups are one or more of biomarkers, DNA, quantum dots, antibiotics, nanoparticles, growth factors, proteases, and antibodies. , wherein the mass-volume ratio of the functional group to the biological protein solution is 0.001 mg/mL-1 g/mL.

As shown in Figures 8 and 9, after incorporating biomarkers and DNA into the biological protein membrane, biologically relevant information can be stored, and the biologically relevant information includes hemoglobin A1, albumin A2 and glucose A3, where normalized It can be observed that the normalized activities of hemoglobin A1, albumin A2 and glucose A3 are the same after 1 day; after 7 days, the normalized activities of the three decrease, and the The normalized activity of albumin A2 was higher than that of hemoglobin A1 and glucosinolate A3; after 14 days, the normalized activity of the three decreased again, but the normalized activity of albumin A2 was still higher than Normalized activity of hemoglobin A1 and glucosinolate A3.

As shown in Figure 10, the biological protein film can be antibacterial after incorporating antibiotics, wherein, Figure B1 is the biological protein film after incorporating antibiotics, and Figure B2 is the biological protein film without incorporating antibiotics, it can be seen that Antibacterial effect is obvious.

As shown in Figure 11, after incorporating protease into the biological protein membrane, the stored information can be degraded in a controllable manner, wherein, Figure D1 is the biological protein membrane without papain; Figure D2 is the biological protein membrane doped with papain; Figure D3, after being treated in a 50°C water bath, the bioprotein film without papain; Figure D4, after being treated in a 50°C water bath, the bioprotein film with papain; it can be observed that the information quantity of the bioprotein film without papain Compared with the papain-doped biological protein membrane, the information quantity is more. After being treated in a 50 ℃ water bath, the information of the papain-free biological protein membrane is retained, while the information of the papain-doped biological protein membrane is eliminated.

Specifically, step S2 includes:

The information to be stored is encoded according to a preset encoding form, wherein the preset encoding form is a binary form.

Further, select a picture to be stored, and obtain its binary storage information in the computer through Winhex software.

Specifically, step S3 includes the following steps:

S31. Use a laser source of preset power to irradiate the needle tip of an atomic force microscope, and the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein membrane;

S32. Move the biological protein membrane, and directly write the lattice structure corresponding to the encoded information on the biological protein membrane.

Further, the instantaneous laser power radiated by the laser source in step S31 ranges from 0.01mW to 100W.

Preferably, the instantaneous laser power radiated by the laser source is 300 mW, and the laser wavelength radiated by the laser source is 6.06 μm.

Further, using a laser source with preset power to irradiate the tip of the atomic force microscope is mainly used to cause the topography of the biological protein under the tip of the atomic force microscope to change, and the change trend is from flat to raised point.

Further, the absorption spectrum of the biological protein membrane in step S31 contains two absorption peaks, one absorption peak is the uncrosslinked silk fibroin absorption peak, which is at 1650 cm ⁻¹ ; the other absorption peak is the crosslinking peak. The absorption peak of silk fibroin is at 1625cm ^-1 .

Further, the radiation frequency of the laser source may or may not correspond to the absorption spectrum of the biological protein film.

Further, the atomic force microscope in step S31 is in a tapping mode.

Further, the speed of moving the biological protein membrane in step S32 is 10 nm/ms-10 μm/ms.

As shown in FIG. 4 and FIG. 5 , in step S32, the raised points on the biological protein membrane are specified as "1" and the non-raised points as "0" in the lattice structure, which is the same as the preset in step S2. Corresponding to the encoding form.

Preferably, the raised points and the non-raised points on the biological protein membrane in the lattice structure are arranged at intervals of 100 nm.

Specifically, after step S32, the method further includes:

Decoding the information stored in the biological protein membrane, and reading the information stored in the biological protein membrane.

Further, decoding the information stored in the biological protein membrane, and reading the information stored in the biological protein membrane includes:

The lattice structure is scanned by an atomic force microscope, the information in the lattice structure is decoded, and the information in the lattice structure is read. The raised dots and non-raised dots on the biological protein membrane in the lattice structure are set, and then the information in the lattice structure is read.

As shown in Figure 12, it can be observed that the information storage method based on biological protein can withstand harsh conditions such as high temperature, high humidity, irradiation, magnetic field, etc., where BP is the curve before processing, and AP is the curve after processing.

The first embodiment provides an information storage method based on biological proteins, which can store biological information, and can "write" and "read" digital information in situ.

Embodiment 2

The second embodiment provides a biological protein-based information storage method, which is shown in FIG. 1 , FIG. 2 and FIG. 3 , and includes the following steps:

S1. Preparation of biological protein membranes doped or undoped with functional groups;

S2. Encode the information to be stored;

S3. Store the encoded information and the information in the functional group in the biological protein membrane.

Specifically, step S1 includes the following steps:

S11. Evaporate a layer of metal material on the substrate;

S12. Spin coating a layer of biological protein solution on the substrate on which the metal material is evaporated to form a biological protein film.

Further, the metal material in step S11 is one of Au, Ag, Al, Pt, Ti, Cu, Cr, and TiW.

Preferably, the metal material is Cr or Au, wherein the thickness of both Cr and Au is 10 nm or 100 nm.

Further, the concentration range of the biological protein solution spin-coated in step S12 is 1wt%-30wt%, and the rotation speed of the spin-coating is 500r/min-8000r/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 biological protein membrane in step S12 ranges from 10 nm to 100 um.

Preferably, the thickness of the biological protein membrane is 100 nm.

Specifically, the substrate is one of Si, GaAs, AlN, Al ₂ O ₃ , ITO, SiO ₂ , SiN, and glass materials;

The biological protein is one of silk fibroin, sericin, spider silk, staghorn, egg white and collagen.

Preferably, the substrate is a Si sheet, and the biological protein is silk fibroin.

In some embodiments, a biological protein film can also be prepared without evaporating a layer of metal material on the substrate.

Further, the biological protein solution can be pre-mixed with functional groups, and the functional groups are one or more of biomarkers, DNA, quantum dots, antibiotics, nanoparticles, growth factors, proteases, and antibodies. , wherein the mass-volume ratio of the functional group to the biological protein solution is 0.001 mg/mL-1 g/mL.

As shown in Figures 8 and 9, after incorporating biomarkers and DNA into the biological protein membrane, biologically relevant information can be stored, and the biologically relevant information includes hemoglobin A1, albumin A2 and glucose A3, where normalized It can be observed that the normalized activities of hemoglobin A1, albumin A2 and glucose A3 are the same after 1 day; after 7 days, the normalized activities of the three decrease, and the The normalized activity of albumin A2 was higher than that of hemoglobin A1 and glucosinolate A3; after 14 days, the normalized activity of the three decreased again, but the normalized activity of albumin A2 was still higher than Normalized activity of hemoglobin A1 and glucosinolate A3.

As shown in Figure 10, the biological protein film can be antibacterial after incorporating antibiotics, wherein, Figure B1 is the biological protein film after incorporating antibiotics, and Figure B2 is the biological protein film without incorporating antibiotics, it can be seen that Antibacterial effect is obvious.

As shown in Figure 11, after incorporating protease into the biological protein membrane, the stored information can be degraded in a controllable manner, wherein, Figure D1 is the biological protein membrane without papain; Figure D2 is the biological protein membrane doped with papain; Figure D3, after being treated in a 50°C water bath, the bioprotein film without papain; Figure D4, after being treated in a 50°C water bath, the bioprotein film with papain; it can be observed that the information quantity of the bioprotein film without papain Compared with the papain-doped biological protein membrane, the information quantity is more. After being treated in a 50 ℃ water bath, the information of the papain-free biological protein membrane is retained, while the information of the papain-doped biological protein membrane is eliminated.

Specifically, step S2 includes:

The information to be stored is encoded according to a preset encoding form, wherein the preset encoding form is a binary form.

Further, select a picture to be stored, and obtain its binary storage information in the computer through Winhex software.

Specifically, step S3 includes the following steps:

S31. Use a laser source of preset power to irradiate the needle tip of an atomic force microscope, and the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein membrane;

S32. Move the biological protein membrane, and directly write the lattice structure corresponding to the encoded information on the biological protein membrane.

Further, the instantaneous laser power radiated by the laser source in step S31 ranges from 0.01mW to 100W.

Preferably, the instantaneous laser power radiated by the laser source is 300 mW, and the laser wavelength radiated by the laser source is 6.06 μm.

Further, using a laser source with a preset power to irradiate the tip of the atomic force microscope is mainly used to cause the topography of the biological protein below the tip of the atomic force microscope to change, and the change trend is from flat to raised point.

Further, the absorption spectrum of the biological protein membrane in step S31 contains two absorption peaks, one absorption peak is the uncrosslinked silk fibroin absorption peak, which is at 1650 cm ⁻¹ ; the other absorption peak is the crosslinking peak. The absorption peak of silk fibroin is at 1625cm ^-1 .

Further, the radiation frequency of the laser source may or may not correspond to the absorption spectrum of the biological protein film.

Further, the atomic force microscope in step S31 is in a tapping mode.

Further, the speed of moving the biological protein membrane in step S32 is 10 nm/ms-10 μm/ms.

Further, in the step S32, the raised dots on the biological protein membrane are specified as "1" and the non-raised dots are defined as "0" in the lattice structure, which corresponds to the preset encoding form in the step S2.

Preferably, with an interval of 100 nm, set the raised points and non-raised points on the biological protein membrane in the lattice structure, as shown in Figure 6, write 16 points in two rows, the codes are "" 11111111" and "11111111".

Specifically, after step S32, the method further includes:

The information stored in the biological protein membrane is erased, and the information stored in the biological protein membrane is rewritten.

Further, erasing the information stored in the biological protein membrane, and rewriting the information stored in the biological protein membrane includes:

Using an infrared laser source with a power smaller than or greater than the preset power to irradiate the tip of the atomic force microscope to eliminate the lattice structure,

Using the infrared laser source with the preset power to irradiate the tip of an atomic force microscope, the lattice structure is rewritten.

Further, when the preset power changes from low to high, the dot matrix structure changes from raised points to pits, and vice versa.

Preferably, as shown in FIG. 7 , the ASCII codes of the letters "U" and "T" obtained from the query are "01010101" and "01010100", respectively. Increase the instantaneous power of the laser source radiation to 1W, the dot matrix structure will be erased to eliminate the corresponding position, that is, from "1" to "0", the ASCII codes of "U" and "T" are obtained" 01010101" and "01010100" to achieve elimination.

Further, in the above-mentioned lattice structure that has been eliminated, with an interval of 100 nm, the raised points and non-raised points on the biological protein film in the lattice structure after the atomic force microscope scanning are set, and then read. Take the information in the lattice structure.

As shown in Figure 12, it can be observed that the biological protein-based information storage method can withstand harsh conditions such as high temperature, high humidity, irradiation, and magnetic fields, where BP is the curve before processing, and AP is the curve after processing.

The second embodiment provides an information storage method based on biological proteins, which can realize repeated writing or erasing of digital information.

The foregoing description has fully disclosed specific embodiments of the present invention. It should be pointed out that any changes made by those skilled in the art to the specific embodiments of the present invention will not depart from the scope of the claims of the present invention. Accordingly, the scope of the claims of the present invention is not limited to the foregoing specific embodiments.

Claims (13)

1. an information storage method based on biological protein, is characterized in that, comprises the following steps: S1. Preparation of biological protein membranes doped or undoped with functional groups; S2. Encode the information to be stored; S3. Store the encoded information and the information in the functional group in the biological protein membrane; wherein, only the encoded information is stored in the biological protein membrane not doped with the functional group. 2. biological protein-based information storage method according to claim 1, is characterized in that, step S1 comprises the following steps: S11. Evaporate a layer of metal material on the substrate; S12. Spin coating a layer of biological protein solution on the substrate on which the metal material is evaporated to form a biological protein film. 3. the information storage method based on biological protein according to claim 2, is characterized in that, The substrate is one of Si, GaAs, AlN, Al ₂ O ₃ , ITO, SiO ₂ , SiN, and glass materials; the biological protein is silk fibroin, sericin, spider silk, keratin, egg white One of protein and collagen. 4. The biological protein-based information storage method according to claim 2, wherein the biological protein solution can be pre-doped with functional groups, and the functional groups are biomarkers, DNA, quantum dots, One or more of antibiotics, nanoparticles, growth factors, proteases, and antibodies. 5 . The biological protein-based information storage method according to claim 4 , wherein the biological protein membrane can store biological-related information after incorporating biomarkers and DNA into the biological protein membrane. 6 . 6. The biological protein-based information storage method according to claim 4, wherein the biological protein membrane can be antibacterial after incorporating antibiotics. 7 . The biological protein-based information storage method according to claim 4 , wherein after the biological protein membrane is incorporated with protease, the stored information can be degraded in a controllable manner. 8 . 8. The biological protein-based information storage method according to claim 1, wherein step S2 comprises: The information to be stored is encoded according to the preset encoding form. 9. biological protein-based information storage method according to claim 1, is characterized in that, step S3 comprises the following steps: S31. Use a laser source of preset power to irradiate the needle tip of an atomic force microscope, and the radiation frequency of the laser source corresponds to the absorption spectrum of the biological protein membrane; S32. Move the biological protein membrane, and directly write the lattice structure corresponding to the encoded information on the biological protein membrane. 10. The biological protein-based information storage method according to claim 9, wherein after step S32, the method further comprises: Decoding the information stored in the biological protein membrane, and reading the information stored in the biological protein membrane. 11. The information storage method based on biological protein according to claim 10, characterized in that, The decoding of the information stored in the biological protein membrane, and the reading of the information stored in the biological protein membrane includes: The lattice structure is scanned by an atomic force microscope, the information in the lattice structure is decoded, and the information in the lattice structure is read. 12. The biological protein-based information storage method according to claim 9, wherein after step S32, the method further comprises: The information stored in the biological protein membrane is erased, and the information stored in the biological protein membrane is rewritten. 13. The biological protein-based information storage method according to claim 12, characterized in that, The erasing of the information stored in the biological protein membrane, and the rewriting of the information stored in the biological protein membrane include: Using an infrared laser source with a power smaller than or greater than the preset power to irradiate the tip of the atomic force microscope to eliminate the lattice structure, Using the infrared laser source with the preset power to irradiate the tip of an atomic force microscope, the lattice structure is rewritten.

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