Conformational Studies of ε‐ CBz‐ L‐ Lysine and L‐ Valine Block Copolypeptides

Abstract

Conformational studies ofε-CBz-L-lysine andL-valine block copoylpeptides using x- ray diffraction and CD spectra are described. The block copolypeptides contain valine block in the center and on both side of the valine areε-CBz-L-lysine blocks. The conformation of the copolypeptides changes with increases in the chain length ofε- CBz-L- lysine blocks. When length ofε- CBZ-L- lysine blocks is 9, the block copolypeptide has exclusive beta sheet structure. With the increase in chain length ofε-CBz-L-lysine blocks from 9 to 14, the block copolypeptide shows presence of both alpha helix and beta sheet components. With further increase in chain length ofε- CBz-L- lysine blocks, the beta sheet component disappears and block copolypeptides exhibits exclusive α -helix conformation.

Copolymerization of N-Carboxyanhydrides of alpha - Amino Acids.

“…The copolypeptides from polymerization of amino acid N-carboxyanhydrides (NCA) have potential application in biomedical applications such as polypeptide adhesives for use as surgical sealant, antimicrobial polypeptides for the treatment of autoimmune disorders, polypeptide membranes for therapeutic delivery and polypeptide hydrogels for tissue engineering applications [39][40][41][42] . While these materials show great potential, much development is still required before they will be useful in some of these applications.…”