Logo image
Back
Anomalous Conformational Instability and Hydrogel Formation of a Cationic Class of Self-Assembling Oligopeptides
Journal article   Peer reviewed

Anomalous Conformational Instability and Hydrogel Formation of a Cationic Class of Self-Assembling Oligopeptides

Thomas J. Measey, Reinhard Schweitzer-Stenner, Vijoya Sa and Konstantin Kornev
Macromolecules, v 43(18), pp 7800-7806
28 Sep 2010
DOI: https://doi.org/10.1021/ma101450b
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Physical Sciences Polymer Science Science & Technology
A detailed understanding of the mechanistic principles which govern peptide and protein self-assembly is of considerable biomedical and biotechnological importance. Owing to the diversity of peptide and protein sequences which have been shown to aggregate into ordered structures, the ability to self-assemble is now recognized as an inherent feature of the polypeptide backbone. It is therefore of utmost importance to elucidate the rules governing the self-assembly process. De nova designed oligopeptides, based on sequences of alternating hydrophilic and hydrophobic residues and containing complementary charge distributions, have shown the potential to self-assemble into hydrogels rich in beta-sheet secondary structure. Here we present and characterize the unexpected self-assembly and hydrogel formation of AK-16, an alanine-rich oligopeptide, whose sequence does not abide by typical rules which allow for peptide self-organization. AK-16 spontaneously forms soluble, thermodynamically unstable/beta-sheet-rich aggregates, which can be stabilized by salt addition to yield a self-supporting macroscopic hydrogel. The AK-16 hydrogel exhibits the ability to encapsulate and slowly release a model protein. This one-charge-type system represents a novel class of self-assembling oligopeptides, in which the initial conformational instability can be exploited to tune the viscosity and physicochemical properties of the resultant hydrogel. This study provides insight for the future de nova design of self-assembling oligopeptides.

Metrics

6 Record Views
19 citations in Web of Science
23 citations in Scopus

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Collaboration types
Domestic collaboration
Web of Science research areas
Polymer Science
Logo image