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Self-Assembling Peptide and Peptide Gel with High Strength

a peptide gel and self-assembling technology, applied in the direction of peptide/protein ingredients, spectral modifiers, macromolecular non-active ingredients, etc., can solve the problems of insufficient transparency of gel, scaffold may collapse when grasped with tweezers, and unknown infectious diseases, etc., to achieve the effect of practical mechanical strength

Inactive Publication Date: 2014-06-12
UNIV OKAYAMA +2
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The patent describes a specific peptide that can be assembled into a gel with good strength. This helps to create a practical material using the peptide.

Problems solved by technology

However, the collagen gel is derived from an animal and hence may cause an unknown infectious disease.
However, a scaffold (peptide gel) formed of the self-assembling peptide of Patent Document 1 or 2 is insufficient in mechanical strength and hence involves such a problem in handleability that the scaffold may collapse when grasped with tweezers, for example.
Further, the self-assembling peptide gel of Patent Document 1 involves such a problem that the gel is insufficient in transparency at neutral pH environment.

Method used

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  • Self-Assembling Peptide and Peptide Gel with High Strength
  • Self-Assembling Peptide and Peptide Gel with High Strength
  • Self-Assembling Peptide and Peptide Gel with High Strength

Examples

Experimental program
Comparison scheme
Effect test

example 1

[0101]A self-assembling peptide formed of an amino acid sequence of SEQ ID NO: 1 described in Table 1 was synthesized by an Fmoc solid-phase synthesis method. Next, the self-assembling peptide was acetylated at the N-terminus and amidated at the C-terminus by a conventional method to afford a modified peptide 1 ([CH3CO]-RLDLRLALRLDLR-[NH2]).

[0102]The resultant modified peptide 1 was dissolved in a 0.1 wt % sodium hydrogen carbonate solution at concentrations of 0.2, 0.4, and 0.6 w / v % to afford peptide solutions. The resultant peptide solutions were each measured for a pH value using pH test paper (trade name: pH Indicator Papers, manufactured by Whatman International Ltd., measurement range pH=6.0 to 8.1, Cat. No. 2629 990), and the pH was found to fall within the range of 6.9 to 7.8. 300 μl each of the peptide solutions were charged into a trade name “Nunc Tissue Culture Inserts” (membrane diameter: 10 mm, pore size: 8.0 μm membrane material: polycarbonate) (product number “Cat. N...

example 2

[0107]A modified peptide 2 ([CH3CO]-RLDLRLLLRLDLRe [NH2]) was obtained in the same manner as in Example 1 except that an amino acid sequence of SEQ ID NO: 2 was adopted in place of the amino acid sequence of SEQ ID NO: 1. Peptide gels 2 (liquid phase: MEN) at peptide concentrations of 0.2, 0.4, and 0.6 w / v % were formed in the same manner as in Example 1 except that the modified peptide 2 was used in place of the modified peptide 1.

[0108]The resultant peptide gels were each measured for mechanical strength in the same manner as in Example 1. FIG. 4 shows the results. As shown in FIG. 4, the peptide gel 2 at 0.4 w / v % had an absolute value L of an amount of change in load per unit time of 0.0423 g / s in the compression test.

[0109]The peptide gel 2 at 0.4 w / v % was grasped with tweezers and transported. As a result, as shown in FIG. 3(b), the peptide gel 2 had sufficient strength to grasp and was excellent in handleability.

example 3

[0110]A modified peptide 3 ([CH3CO]-RLDLRLALRLDLRL-[NH2]) was obtained in the same manner as in Example 1 except that an amino acid sequence of SEQ ID NO: 3 was adopted in place of the amino acid sequence of SEQ ID NO: 1. Peptide gels 3 (liquid phase: DMEM) at peptide concentrations of 0.2 and 0.4 w / v % were formed in the same manner as in Example 1 except that the modified peptide 3 was used in place of the modified peptide 1.

[0111]The resultant peptide gels were each measured for mechanical strength in the same manner as in Example 1. FIG. 5 shows the results. As shown in FIG. 5, the peptide gel 3 at 0.4 w / v % had an absolute value L of an amount of change in load per unit time of 0.0336 g / s in the compression test.

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Abstract

Provide are a peptide gel with practically sufficient mechanical strength and a self-assembling peptide capable of forming the peptide gel. The self-assembling peptide is formed of the following amino acid sequence: a1b1c1b2a2b3db4a3b5c2b6a4 where: a1 to a4 each represent a basic amino acid residue; b1 to b6 each represent an uncharged polar amino acid residue and / or a hydrophobic amino acid residue, provided that at least five thereof each represent a hydrophobic amino acid residue; c1 and c2 each represent an acidic amino acid residue; and d represents a hydrophobic amino acid residue.

Description

RELATED APPLICATIONS[0001]This application is a continuation of U.S. application Ser. No. 13 / 255,457, filed Sep. 8, 2011, which is a US National stage entry of International Application No PCT / JP2010 / 052047, which claims priority under 35 U.S.C. §119 or 365 to Japan, Application No 2009-054983, filed Mar. 9, 2009.TECHNICAL FIELD[0002]The present invention relates to a self-assembling peptide capable of forming a high-strength peptide gel, and a peptide gel, which is formed from the peptide.BACKGROUND ART[0003]A collagen gel is generally used as a scaffold (scaffold for cells) to be used in research and actual therapy in the regenerative medicine field. However, the collagen gel is derived from an animal and hence may cause an unknown infectious disease. As means for eliminating the concern about the unknown infectious disease, there exists a scaffold derived from a chemically synthesized material. Examples of such material include a self-assembling peptide disclosed in Patent Docume...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): C07K7/08C10M173/02A61K47/42
CPCC07K7/08C10M173/02A61K47/42A61K8/64A61K38/10A61L15/60A61L27/227A61L27/52A61L29/145A61L31/145A61P7/02A61Q19/00B01J20/28047C12N5/0068C12N2533/50A61K9/0048A61K9/06A61L31/10A61Q5/00C12N5/0656C12N5/0658
Inventor NAGAI, YUSUKEYOKOI, HIDENORIUESUGI, KOJINARUSE, KEIJIZHANG, SHUGUANG
Owner UNIV OKAYAMA
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