Aqueous gel formation of a synthetic peptide derived from the β-sheet domain of platelet factor-4

Nathan A. Lockwood, Robert van Tankeren, Kevin H Mayo

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

We observed gelation of a 23-residue peptide derived from the β-sheet domain of platelet factor-4 (PF424-46). The gels were primarily heterogeneous mixtures of 50-200 μm spherical aggregates in a less-dense gel matrix. Infrared and circular dichroism spectroscopies showed gelation involving the conversion of PF424-46 from random coil to β-sheet. We used aggregation-induced NMR resonance broadening to show that temperature, pH, and ionic strength influenced PF424-46 gelation rates. Under identical solution conditions, gel formation took days at T ≤ 20 °C but only 30 min at T ≥ 50 °C. Gelation was most rapid at pH values near the pKa of the central His35 residue. Increases in solution ionic strength reduced the critical gelation concentration of PF424-46. Our results suggest that PF424-46 gels by a process combining aspects of both heat-set and β-fibril gelation mechanisms.

Original languageEnglish (US)
Pages (from-to)1225-1232
Number of pages8
JournalBiomacromolecules
Volume3
Issue number6
DOIs
StatePublished - Nov 1 2002

Fingerprint

Dive into the research topics of 'Aqueous gel formation of a synthetic peptide derived from the β-sheet domain of platelet factor-4'. Together they form a unique fingerprint.

Cite this