The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation-Reference-Cited by-同舟云学术

The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation

Published:2020 Issue:17 Volume:16 Page:4110-4114
ISSN:1744-683X
Container-title:Soft Matter
language:en
Short-container-title:Soft Matter

Author:

Hesser Morgan¹²³⁴,Thursch Lavenia⁵²³⁴,Lewis Todd⁵²³⁴,DiGuiseppi David¹²³⁴^ORCID,Alvarez Nicolas J.⁵²³⁴^ORCID,Schweitzer-Stenner Reinhard¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. Drexel University

3. Philadelphia

4. USA

5. Department of Chemical and Biological Engineering

Abstract

The tripeptide glycyl-histidyl-glycine (GHG) self-assembles into long, crystalline fibrils forming a strong hydrogel (G′ ∼ 50 kPa) above a critical concentration of 40 mM upon the deprotonation of its imidazole group.

Funder

National Science Foundation

Drexel University

Publisher

Royal Society of Chemistry (RSC)

Subject

Condensed Matter Physics,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/SM/D0SM00224K

Reference38 articles.

1. Self Assembly of Short Aromatic Peptides into Amyloid Fibrils and Related Nanostructures

2. The physical properties of supramolecular peptide assemblies: from building block association to technological applications

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4. Exploring the sequence space for (tri-)peptide self-assembly to design and discover new hydrogels

5. Peptide Fibrillization

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