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dc.contributor.authorKoch, Franziska
dc.contributor.authorKönig, Finja
dc.contributor.authorMeyer, Nina
dc.contributor.authorGattlen, Jasmin
dc.contributor.authorPieles, Uwe
dc.contributor.authorPeters, Kirsten
dc.contributor.authorKreikemeyer, Bernd
dc.contributor.authorMathes, Stephanie
dc.contributor.authorSaxer, Sina
dc.contributor.authorMüller, Michael
dc.date.accessioned2018-12-13T09:51:36Z
dc.date.available2018-12-13T09:51:36Z
dc.date.issued2018-03
dc.identifier.doi10.1098/rsos.171562
dc.identifier.urihttp://hdl.handle.net/11654/26948
dc.description.abstractSelf-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.
dc.description.urihttp://rsos.royalsocietypublishing.org/content/5/3/171562
dc.language.isoen_US
dc.relation.ispartofRoyal Society Open Science
dc.accessRightsAnonymous
dc.subjectself-assembling peptides (SAP)
dc.subjectSAP hydrogel stiffness
dc.subjectnanofibrillar architectur
dc.subjectSAP hydrogel degrability
dc.titleMechanical characteristics of beta sheet-forming peptide hydrogels are dependent on peptide sequence, concentration and buffer composition
dc.type01 - Zeitschriftenartikel, Journalartikel oder Magazin
dc.audienceScience
fhnw.publicationStatePublished
fhnw.ReviewTypeAnonymous ex ante peer review of a complete publication
fhnw.InventedHereYes
fhnw.PublishedSwitzerlandNo
fhnw.IsStudentsWorkno
fhnw.publicationOnlineJa


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