Mechanical Characteristics of Beta Sheet-forming Peptide Hydrogels Are Dependent on Peptide Sequence, Concentration and Buffer Composition

Overview

Journal R Soc Open Sci

Specialty Science

Date 2018 Apr 17

PMID 29657766

Citations 15

Authors

Franziska Koch

Michael Muller

Finja Konig

Nina Meyer

Jasmin Gattlen

Uwe Pieles

Kirsten Peters

Bernd Kreikemeyer

Stephanie Mathes

Sina Saxer

Affiliations

Soon will be listed here.

Abstract

Self-assembling peptide hydrogels can be modified regarding their biodegradability, their chemical and mechanical properties and their nanofibrillar structure. Thus, self-assembling peptide hydrogels might be suitable scaffolds for regenerative therapies and tissue engineering. Owing to the use of various peptide concentrations and buffer compositions, the self-assembling peptide hydrogels might be influenced regarding their mechanical characteristics. Therefore, the mechanical properties and stability of a set of self-assembling peptide hydrogels, consisting of 11 amino acids, made from four beta sheet self-assembling peptides in various peptide concentrations and buffer compositions were studied. The formed self-assembling peptide hydrogels exhibited stiffnesses ranging from 0.6 to 205 kPa. The hydrogel stiffness was mostly affected by peptide sequence followed by peptide concentration and buffer composition. All self-assembling peptide hydrogels examined provided a nanofibrillar network formation. A maximum self-assembling peptide hydrogel dissolution of 20% was observed for different buffer solutions after 7 days. The stability regarding enzymatic and bacterial digestion showed less degradation in comparison to the self-assembling peptide hydrogel dissolution rate in buffer. The tested set of self-assembling peptide hydrogels were able to form stable scaffolds and provided a broad spectrum of tissue-specific stiffnesses that are suitable for a regenerative therapy.

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