Peptide derivatives, and their use for the synthesis of silicon-based composite materials
Abstract
Methods for forming peptide derivatives using functional moieties and peptide derivatives are provided. Further, methods for using peptide derivatives to form silicon-based composite materials and silicon-based composite materials formed thereby are provided. The silicon-based composite materials may have features on the nanoscale, and the materials may exhibit characteristics derived from the functional moieties on the peptide derivatives. It is emphasized that this abstract is provided to comply with the rules requiring an abstract which will allow a searcher or other reader to quickly ascertain the subject matter of the technical disclosure. It is submitted with the understanding that is will not be used to interpret or limit the scope or meaning of the claims. 37 CFR 1.72(b).
Claims
exact text as granted — not AI-modified1 . A method of forming a composite material comprising:
providing a substantially pure peptide having at least two amino acids and less than about 45 amino acids, wherein: at least one amino acid has a polar functionality; modifying said peptide with a first functional moiety selected from the group consisting of 1-pyreneacetic acid, 1-pyrenemethylamine, 5(6)-carboxyfluorescein, EDTA, cyclam tetraacetic acid, lauric acid, cholesterol, D-biotin, carboxymethyl-β-cyclodextrin, and cysteine to form a peptide derivative; and exposing said peptide derivative to a precursor containing a silicon species such that a composite material forms, wherein said peptide derivative and said silicon species are incorporated into said composite material.
2 . (canceled)
3 . The method of claim 1 wherein said peptide has between about 7 to about 30 amino acids.
4 . The method of claim 1 wherein said peptide is polybasic.
5 . The method of claim 1 wherein said peptide has a pI of greater than about 6.5.
6 . The method of claim 1 wherein said peptide has a pI of between about 7 to about 12.
7 . The method of claim 1 wherein said peptide has a pI of between about 8 to about 12.
8 .- 11 . (canceled)
12 . The method of claim 1 wherein said peptide derivative has characteristics derived from said first functional moiety
13 . The method of claim 1 wherein said polar functional amino acid is selected from lysine, histidine, arginine, serine, tyrosine, threonine, asparagine, glutamine and cysteine, and combinations thereof.
14 . The method of claim 1 wherein said polar functional amino acid is selected from lysine, histidine, and arginine, and combinations thereof.
15 . The method of claim 1 wherein said peptide has at least one motif comprising SGS wherein said motif is flanked by an amino acid selected from a basic amino acid and an aromatic amino acid.
16 . The method of claim 1 wherein said peptide has at least one incidence of two or more tandem repeat polar functional amino acids.
17 . The method of claim 1 wherein said peptide is modified with a plurality of functional moieties to form said peptide derivative.
18 . The method of claim 17 wherein said peptide is modified with between 1 to 3 functional moieties.
19 . The method of claim 1 wherein said first functional moiety is selected from dyes, tracers, chemical indicators, fluorophores, luminophores, biomolecules, biologically active compounds, enzymes, liquid crystals, enzyme inhibitors, metal chelators, metal complexes, nanoparticles, quantum dots, radioisotopes, cysteine or drugs.
20 . The method of claim 1 wherein said first functional moiety is selected from 1-pyreneacetic acid and 1-pyrenemethylamine.
21 . The method of claim 1 wherein said first functional moiety comprises 5(6)-carboxyfluorescein.
22 . The method of claim 1 wherein said first functional moiety comprises EDTA.
23 . The method of claim 1 wherein said first functional moiety comprises cyclam tetraacetic acid.
24 . The method of claim 1 wherein said first functional moiety comprises lauric acid.
25 . The method of claim 1 wherein said first functional moiety comprises cholesterol.
26 . The method of claim 1 wherein said first functional moiety comprises D-biotin.
27 . The method of claim 1 wherein said first functional moiety comprises carboxymethyl-y-cyclodextrin.
28 . The method of claim 1 wherein said first functional moiety comprises cysteine.
29 .- 36 . (canceled)
37 . The method of claim 1 wherein said silicon containing species is selected from Q-unit silanes, T-unit silanes, D-unit silanes, and M-unit silanes.
38 . The method of claim 1 wherein said silicon containing species is selected from orthosilicic acid, tetramethoxysilane, and tetraethoxysilane.
39 . The method of claim 1 wherein said silicon containing species is selected from phenyltriethoxysilane, phenyltrichlorosilane, 3-aminopropyltriethoxysilane, and methyltriemethoxysilane.
40 . The method of claim 1 wherein said silicon containing species is selected from phenylmethyldichlorosilane and dimethyldimethoxysilane.
41 . The method of claim 1 wherein said silicon containing species comprises trimethylchlorosilane.
42 . The method of claim 1 wherein said silicon containing species is treated prior to exposing said peptide derivative to said precursor containing said silicon species such that the silanol content of said silicon species is maximized.
43 . The method of claim 1 wherein said peptide derivative is exposed to said precursor containing said silicon species occurs in solution at a pH of about 5 to about 10.
44 . The method of claim 43 wherein said solution has a pH of about 6 to about 9.
45 . The method of claim 43 wherein said solution has a pH of about 7 to about 8.
46 . The method of claim 1 further comprising forming an ordered pattern on a substrate with said peptide derivative prior to exposing said peptide derivative to said precursor containing said silicon species.
47 . The method of claim 46 wherein said ordered pattern is formed by soft lithography.
48 . The method of claim 46 wherein said ordered pattern is formed by ink jet modified printing.
49 . The method of claim 1 further comprising treating said composite such that an organic portion of said composite is altered.
50 . The method of claim 1 wherein said composite material has features on the nanoscale.
51 . The method of claim 1 wherein said peptide derivative is exposed to said precursor in the presence of an electric field.
52 . The method of claim 1 wherein said peptide derivative is exposed to said precursor in the presence of a magnetic field.
53 . The method of claim 1 wherein said peptide derivative is provided in a porous matrix, and wherein said peptide derivative is exposed to said precursor in said porous matrix.
54 . The method of claim 53 wherein said peptide derivative is exposed to said precursor in the presence of an electric field.
55 . The method of claim 53 wherein said peptide derivative is exposed to said precursor in the presence of a magnetic field.
56 .- 96 . (canceled)Join the waitlist — get patent alerts
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