Monitoring the early stage self-assembly of enzyme-assisted peptide hydrogels

Richard J Williams, James Gardiner, Anders B Sorensen, Silvia Marchesan, Roger J. Mulder, Keith M. McLean, Patrick Gordon Hartley

Research output: Contribution to journalArticleResearchpeer-review

9 Citations (Scopus)

Abstract

The early stages of the self-assembly of peptide hydrogels largely determine their final material properties. Here we discuss experimental methodologies for monitoring the self-assembly kinetics which underpin peptide hydrogel formation. The early stage assembly of an enzyme-catalysed Fmoc-trileucine based self-assembled hydrogel was examined using spectroscopic techniques (circular dichroism, CD, and solution NMR) as well as chromatographic (HPLC) and mechanical (rheology) techniques. Optimal conditions for enzyme-assisted hydrogel formation were identified and the kinetics examined. A lag time associated with the formation and accumulation of the self-assembling peptide monomer was observed and a minimum hydrogelator concentration required for gelation was identified. Subsequent formation of well defined nano-and microscale structures lead to self-supporting hydrogels at a range of substrate and enzyme concentrations. 1H NMR monitoring of the early self-assembly process revealed trends that were well in agreement with those identified using traditional methods (i.e. HPLC, CD, rheology) demonstrating 1H NMR spectroscopy can be used to non-invasively monitor the self-assembly of peptide hydrogels without damaging or perturbing the system.

Original languageEnglish
Pages (from-to)572-578
Number of pages7
JournalAustralian Journal of Chemistry
Volume66
Issue number5
DOIs
Publication statusPublished - 2013
Externally publishedYes

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