Mechanical characteristics of beta sheet-forming peptide hydrogels are dependent on peptide sequence, concentration and buffer composition. Issue 3 (14th March 2018)
- Record Type:
- Journal Article
- Title:
- Mechanical characteristics of beta sheet-forming peptide hydrogels are dependent on peptide sequence, concentration and buffer composition. Issue 3 (14th March 2018)
- Main Title:
- Mechanical characteristics of beta sheet-forming peptide hydrogels are dependent on peptide sequence, concentration and buffer composition
- Authors:
- Koch, Franziska
Müller, Michael
König, Finja
Meyer, Nina
Gattlen, Jasmin
Pieles, Uwe
Peters, Kirsten
Kreikemeyer, Bernd
Mathes, Stephanie
Saxer, Sina - Abstract:
- 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 regenerativeAbstract : 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. … (more)
- Is Part Of:
- Royal Society open science. Volume 5:Issue 3(2018)
- Journal:
- Royal Society open science
- Issue:
- Volume 5:Issue 3(2018)
- Issue Display:
- Volume 5, Issue 3 (2018)
- Year:
- 2018
- Volume:
- 5
- Issue:
- 3
- Issue Sort Value:
- 2018-0005-0003-0000
- Page Start:
- Page End:
- Publication Date:
- 2018-03-14
- Subjects:
- self-assembling peptides (SAP) -- SAP hydrogel stiffness -- nanofibrillar architecture -- SAP hydrogel degradability
Science -- Periodicals
500 - Journal URLs:
- https://royalsocietypublishing.org/journal/rsos ↗
- DOI:
- 10.1098/rsos.171562 ↗
- Languages:
- English
- ISSNs:
- 2054-5703
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library STI - ELD Digital store
- Ingest File:
- 25086.xml