Design and characterization of functional novel oligopeptides

Abstract

The present study focus on the design, synthesis and functional role of a few oligopeptides. Towards this, we designed four peptides with primary sequence of alternating hydrophobic and hydrophilic amino acid residues incorporating calcium binding functional groups and motifs. As a preliminary step towards the development of peptide-based materials, we studied the self-assembly of these peptides under various conditions. In addition to these, the peptides were used as model system for understanding the protein-mineral interaction in biomineralization. Among the four peptides synthesized, two of them (P3 and P4) gave fiber-like structures on mica substrate, whereas spherical particles were observed for the peptides (P1 and P2). In the mineralization studies, all four peptides did not show significant effect on aggregation or polymorph selectivity in the calcium carbonate crystallization.