Search

The article summarizes our research devoted to the development of functionalizable collagen using azidoproline-containing model peptides. 'Click chemistry' or Staudinger reduction followed by acylation provided facile access to a range of differently functionalized collagen model peptides bearing e.g. carbohydrates. The research provided not only insight into the factors that are responsible for the high conformational stability of collagen but also a guide in which positions functional moieties are tolerated without or by deliberately disturbing the supramolecular assembly of collagen. The presented research will be useful for the development of collagen-based materials.

An 'azido gauche effect' determines the conformation of (4S)- and (4R)-azidoproline (Azp) derivatives and affects the s-cis:s-trans conformer ratio of Xaa-Azp bonds. The article summarizes our research on the conformational analysis of monomers as well as oligomers derived from (4S)Azp and (4R)Azp. We show that (4S)Azp and (4R)Azp can be used to tune the stability of the polyproline II (PPII) helix. In addition we demonstrate that Azpcontaining oligoprolines are attractive molecular scaffolds with a well-defined helical conformation that can be readily further functionalized using e.g. click chemistry.