Comparative studies of adhesion peptides based on l ‐ or d‐amino acids

Detailed studies comparing solid‐supported l‐ or d‐amino acid adhesion peptides based on the sequence KLHRIRA were performed. Stability towards proteases and levels of cellular adhesion to the otherwise inert surface of PEGA resin were compared by using fluorescently labelled peptides. A clear difference in the peptide stability towards cleavage by subtilisin, trypsin, or papain was observed. However, all of the on‐bead peptides provided an optimal surface for cell adhesion and proliferation. In long‐term experiments, these properties were still found to be similar on the resins modified either with l‐ or with d‐amino acids and unaffected by the nature of their fluorescence labelling at either terminus. These results support that the more accessible l‐amino acids can be utilized for cell adhesion experiments and confirm the nonspecific interaction mechanism of cell binding to these peptides on the bead surface. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.

On‐bead studies of adhesion peptides based on the sequence KLHRIRA have revealed both differences and similarities. All the peptides displayed excellent cell adhesion ability demonstrating the broad scope of this type. The peptides were generated from either L‐ or d‐amino acids, but no direct correlation between proteolytic stability and cell adhesion properties was found.

Source: Journal of Peptide Science - August 31, 2016 Category: Biochemistry Authors: Sergey Nikitin, Daniel Palmer, Morten Meldal, Frederik Diness Tags: Research Article Source Type: research