The aim of this research is to investigate the hydrogelation of a peptide segment derived from the natural protein Semenogelin I, the main proteinaceous constituent in seminal plasma. The oligopeptide under investigation self-assembles to form fibrils consisting of an extended β-sheet. We are currently studying a series of truncated versions of the original oligopeptide sequence employing CD and FT IR spectroscopy in order to compare the length requirement for hydrogel formation and the properties of the hydrogels formed. We are also developing a method using Raman spectroscopy for determining the pKa value of a His residue present in the sequence. The deprotonation of this residue, as the pH is changed from acidic to neutral, is postulated to be the trigger for hydrogelation. We are also in the process of incorporating isotopically labeled residues into the sequence in order to determine structural details of the hydrogel. In addition, the kinetics of fibril formation is under investigation, employing a thioflavine-based assay, which is also used as a tool to assess the effects of external variables, such as pH, on aggregation.

Self-assembly and hydrogelation of a peptide derived from semenogelin I

253rd National Meeting (2017)

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