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Interaction of Peptides with Pollen Camodulin and Their Effects on Cellular Functions

The interaction between dansyl-labeled pollen calmodulin(D-pCaM) and buckwheat pollen peptide analogs was studied in the presence of Ca 2+ . Most peptides in our research can associate with D-pCaM and form peptide-pCaM complexes, which changed the fluorescence spectra of D-pCaM. The dissociation constants K d for these complexes were determined using fluorescence titration. Peptide BP-13, AMALALKKTGNH 2, had the smallest K d value 4.0 nmol/L, demonstrating the highest affinity for pCaM. In addition to studying the influence of hydrophobicity, propensity of secondary structure and chain length on these peptides abilities to bind pCaM, we have also found that Gly/L-Ala→D-Ala substitution in peptide chains caused great changes in their affinity for pCaM. These results suggest a potentially useful approach to improving the binding ability of peptidic antagonist to CaM. Furthermore, our data provided evidence on the dissimilarity of different CaMs although they have highly-conserved structures. A primary study was carried out on the effects of CaM-binding peptides on cellular signal transduction, cell proliferation and growth, showing the participation of CaM in this important cellular life process.