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US-20260125492-A1 - ENZYMATIC GRAPHENE-PEPTIDE DISPERSION

US20260125492A1US 20260125492 A1US20260125492 A1US 20260125492A1US-20260125492-A1

Abstract

A method for forming an aqueous graphene-peptide dispersion. Graphene, a peptide, water and a tyrosinase enzyme are mixed. The resulting suspension is sonicated or vortexed until an aqueous graphene-peptide dispersion forms.

Inventors

  • Kenny Barriales
  • Shadman Kandaker
  • Ankit Jain
  • Rein Ulijn

Assignees

  • RESEARCH FOUNDATION OF THE CITY UNIVERSITY OF NEW YORK

Dates

Publication Date
20260507
Application Date
20241025

Claims (20)

  1. 1 . A method for forming an aqueous graphene-peptide dispersion, the method comprising: mixing graphene, a peptide having from two to four residues, water and an oxidant, the peptide having a first residue that is Y, a second residue that is H, Y, W, F, A, V, L, I, P or M, optionally a third residue that is K, H, R, D or E and optionally a fourth residue that is an amino acid, the peptide having an N-terminus that is optionally acetylated and a C-terminus that is optionally amidated, thereby forming a suspension; and sonicating or vortexing the suspension until an aqueous graphene-peptide dispersion forms.
  2. 2 . The method as recited in claim 1 , wherein the peptide is a tripeptide consisting of the first residue, the second residue and the third residue.
  3. 3 . The method as recited in claim 2 , wherein the tripeptide is KYF.
  4. 4 . The method as recited in claim 2 , wherein the tripeptide is HYF.
  5. 5 . The method as recited in claim 2 , wherein the tripeptide is Ac-KYF.
  6. 6 . The method as recited in claim 2 , wherein the second residue is A, V, L, I, P or M.
  7. 7 . The method as recited in claim 2 , wherein the second residue is H, Y, W or F.
  8. 8 . The method as recited in claim 2 , wherein the third residue is D or E.
  9. 9 . The method as recited in claim 2 , wherein the tripeptide is selected from the group consisting of KYF, HYF, KYY, HYY, DYF, EYF and Ac-KYF.
  10. 10 . The method as recited in claim 2 , wherein the tripeptide is selected from the group consisting of KYF and Ac-KYF.
  11. 11 . An aqueous graphene-peptide dispersion formed according to the method of claim 1 .
  12. 12 . An aqueous graphene-peptide dispersion formed according to the method of claim 2 .
  13. 13 . The method as recited in claim 1 , wherein the peptide is a dipeptide consisting of the first residue and the second residue.
  14. 14 . The method as recited in claim 13 , wherein the second residue is A, V, L, I, P or M.
  15. 15 . The method as recited in claim 13 , wherein the second residue is H, Y, W or F.
  16. 16 . The method as recited in claim 13 , wherein the dipeptide is selected from the group consisting of YR, WY, FY, and LY.
  17. 17 . An aqueous graphene-peptide dispersion formed according to the method of claim 13 .
  18. 18 . The method as recited in claim 1 , wherein the peptide is a tetrapeptide consisting of the first residue, the second residue, the third residue and the fourth residue.
  19. 19 . The method as recited in claim 1 , wherein the oxidant is a tyrosinase enzyme.
  20. 20 . A method for forming an aqueous graphene-peptide dispersion, the method comprising: mixing graphene, a tripeptide, water and an oxidizing enzyme, the tripeptide having a first residue that is Y, a second residue that is H, Y, W, F, A, V, L, I, P or M, and a third residue that is K, H, R, D or E, the tripeptide having an N-terminus that is optionally acetylated and a C-terminus that is optionally amidated, thereby forming a suspension; and sonicating or vortexing the suspension until an aqueous graphene-peptide dispersion forms.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to, and is a continuation-in-part of, U.S. patent application Ser. No. 18/805,215 (filed Aug. 14, 2024) which is a non-provisional of, U.S. Patent Application 63/519,402 (filed Aug. 14, 2023), the entirety of which are incorporated herein by reference. STATEMENT OF FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT This invention was made with government support under grant number FA9550-21-1-0091 awarded by the Air Force Office of Scientific Research. The government has certain rights in the invention. BACKGROUND OF THE INVENTION Graphene, a two-dimensional carbon material, possesses extraordinary mechanical, electrical, and thermal properties, making it highly attractive for various biological applications such as biosensing, biotherapeutics and tissue engineering. However, the tendency of graphene sheets to aggregate and restack hinders its dispersion in water, limiting its potential applications. An improved method for dispersing graphene in water is therefore desired. The discussion above is merely provided for general background information and is not intended to be used as an aid in determining the scope of the claimed subject matter. SUMMARY This disclosure provides a method for forming an aqueous graphene-peptide dispersion. In a first embodiment, a method for forming an aqueous graphene-peptide dispersion is provided. The method comprising: mixing graphene, a peptide having from two to four residues, water and an oxidant, the peptide having a first residue that is Y, a second residue that is H, Y, W, F, A, V, L, I, P or M, optionally a third residue that is K, H, R, D or E and optionally a fourth residue that is an amino acid, the peptide having an N-terminus that is optionally acetylated and a C-terminus that is optionally amidated, thereby forming a suspension; and sonicating or vortexing the suspension until an aqueous graphene-peptide dispersion forms. In a second embodiment, a method for forming an aqueous graphene-peptide dispersion is provided. The method comprising: mixing graphene, a tripeptide, water and an oxidizing enzyme, the tripeptide having a first residue that is Y, a second residue that is H, Y, W, F, A, V, L, I, P or M, and a third residue that is K, H, R, D or E, the tripeptide having an N-terminus that is optionally acetylated and a C-terminus that is optionally amidated, thereby forming a suspension; and sonicating or vortexing the suspension until an aqueous graphene-peptide dispersion forms. This brief description of the invention is intended only to provide a brief overview of subject matter disclosed herein according to one or more illustrative embodiments, and does not serve as a guide to interpreting the claims or to define or limit the scope of the invention, which is defined only by the appended claims. This brief description is provided to introduce an illustrative selection of concepts in a simplified form that are further described below in the detailed description. This brief description is not intended to identify key features or essential features of the claimed subject matter, nor is it intended to be used as an aid in determining the scope of the claimed subject matter. The claimed subject matter is not limited to implementations that solve any or all disadvantages noted in the background. BRIEF DESCRIPTION OF THE DRAWINGS So that the manner in which the features of the invention can be understood, a detailed description of the invention may be had by reference to certain embodiments, some of which are illustrated in the accompanying drawings. It is to be noted, however, that the drawings illustrate only certain embodiments of this invention and are therefore not to be considered limiting of its scope, for the scope of the invention encompasses other equally effective embodiments. The drawings are not necessarily to scale, emphasis generally being placed upon illustrating the features of certain embodiments of the invention. In the drawings, like numerals are used to indicate like parts throughout the various views. Thus, for further understanding of the invention, reference can be made to the following detailed description, read in connection with the drawings in which: FIG. 1A is a schematic representation of KYF dispersing graphene sheets and further dispersion through enzymatic oxidation. FIG. 1B illustrates a molecular structure of KYF and radical formation structure after tyrosinase is introduced. FIG. 1C shows illustrations of the peptide structure covalently bound onto the graphene surface with corresponding covalent and non-covalent interactions (top) top-down view to emphasize x-stacking (bottom). Hydrogens were removed for clarification. FIG. 1D depicts macroscopic and Cryo-TEM images of 1G, 2G and 3G respectively. Scale bar=500 nm. Inset Scale bar=200 nm FIG. 2A show optical Images of 1G, 2G and 3G. Scale bar=200 μm. FIG. 2B depicts a zeta potential analysis of 1G, 2G and 3G (n=3). F