Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Amino acid pairing-based self assembling peptides and methods

An amino acid and self-assembly technology, which is applied in the preparation methods of peptides, chemical instruments and methods, pharmaceutical formulations, etc., and can solve the problems of inability to self-assemble molecules.

Inactive Publication Date: 2011-01-05
UNIVERSITY OF WATERLOO
View PDF9 Cites 21 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The second amino acid domain cannot carry out molecular self-assembly by itself

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Amino acid pairing-based self assembling peptides and methods
  • Amino acid pairing-based self assembling peptides and methods
  • Amino acid pairing-based self assembling peptides and methods

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0222] In one embodiment, the present invention provides a method for preparing self-assembled amino acid peptides with amino acid pairing properties for producing nanostructures. The method comprises the following steps: designing a β-chain peptide whose amino acids and their complementary amino acids can form at least one of the following interactions: hydrogen bonds, electrostatic interactions, hydrophobic interactions and van der Waals interactions; such polypeptide chains contain 2 Up to 40 amino acids, containing at least one amino acid pair capable of forming at least one of the following forces, hydrogen bonding, electrostatic interaction, hydrophobic interaction, and van der Waals interaction, and having complementary amino acid pairing and steric complementarity to a second polypeptide.

[0223] Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) and Thioflavin T (ThT) fluorescence spectroscopy can be used to analyze the secondary structure of pept...

Embodiment 1

[0263] Example 1: Hydrogen Bonded Amino Acid Pairing (AAP)

[0264] Table 1 lists amino acids that can form hydrogen bonds, and their atomic positions that can act as proton donors and proton acceptors. The amino acids that can be paired are listed in Table 2. Soluble and less soluble hydrogen bonded amino acid pairs are listed in Tables 3 and 4, respectively. When amino acids are charged, the presence of repulsive forces inhibits hydrogen bond pairing (see Table 3). Therefore, uncharged amino acid pairs capable of forming hydrogen bonds are of particular interest.

[0265] Table 1. Amino acids that form hydrogen bonds and the positions of atoms in the amino acids that can act as acceptors and donors.

[0266] amino acid

[0267] S

[0268] Table 2. Classification of amino acids forming hydrogen bonds according to their function (donor or acceptor) and the positions of atoms in the amino acid as proton donors and proton acceptors.

[0269] hyd...

Embodiment 2

[0287] Example 2: Amino Acid Pairing Peptides Based on Full Complementarity

[0288] A peptide is designed to contain hydrogen bonds, electrostatic and hydrophobic bonds for each of the amino acid pairings. The resulting peptide was called AC8. AC8 consists of 8 amino acids in sequence, including a typical hydrogen bond pairing (QN), a typical ion complementary pairing (EK), and 2 hydrophobic residue pairings (FF) ( Figure 13 A). The introduction of hydrophobic amino acids is to form a hydrophobic interior to encapsulate and stabilize hydrophobic substances ( Figure 13 B). These hydrophobic residues also strengthen the combination between polypeptides; the charged amino acid side chains improve the solubility of polypeptides and their polymers; hydrogen bond amino acid pairing can also stabilize these polypeptides and their polymers.

[0289] Concentration-dependent AC8 peptide assembly studies used the following method: surface tension measurements ( Figure 14A and ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
diameteraaaaaaaaaa
diameteraaaaaaaaaa
sizeaaaaaaaaaa
Login to View More

Abstract

The invention relates to self assembling beta-strand peptides for forming nanostructures, compositions containing the peptides, and methods of forming the peptides. The invention further relates to uses of these peptides in drug delivery and enhancement of drug solubility, biomolecule detection, and biocatalysis applications. The peptides of this invention are further useful in models of protein aggregation disease.

Description

technical field [0001] The present invention relates to self-assembling peptides forming nanostructures, methods of preparing polypeptides and uses of such peptides. Background technique [0002] The spontaneous assembly of molecules into well-ordered arrangements due to non-covalent interactions is called "molecular self-assembly." The resulting supramolecular structures often provide nanostructures with very well-defined macroscopic properties. (Whitesides et al., (1991), Science 254:1312-1319 "Whitesides et al. (1991)"). [0003] The ability of these entities to self-assemble has become a key factor in the development of these entities as novel materials. For example, research over the past decade has revealed that molecular self-assembly of biopolymers plays a key role in the discovery and design of biomaterials for applications in medical technology, and more specifically in regenerative medicine and drug delivery systems ( Langer and Vacanti (1993) Science 260:920-9...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): C07K7/06A61K38/02A61K45/08A61K47/18A61K47/42B82B1/00C07K1/00C07K5/06C07K5/072C07K5/113C11D1/88G01N33/50G01N33/569G01N33/66G01N33/68H01M8/22
CPCH01M4/8605C07K5/06113A61K47/42Y02E60/50C07K5/1021Y02E60/527A61K9/10G01N33/68C07K7/06C07K5/06104A61P35/00
Inventor 陈璞杨红冯善宇
Owner UNIVERSITY OF WATERLOO
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products