Eigenschaften late-stage-modifizierter Kollagen-Modellpeptide

Natural collagen is a posttranslational highly modified Scleroprotein. The influece of specific modification on the triplehelical structure was investigated with collagen model peptides. This model peptides were synthesized using an optimized solid phase peptide synthesis protocol and dihydroxylated diastereoselectivly, similar to a posttranslational modification. A correlation between Hydroxylation pattern, conformarmation of the pyrrolidine and stability of the triple helical structure, determined with NMR-spectroscopical methods, was observed. A 1,2-diol, able to bind boronic acid or benzoboroxoles reversibly, was used to link the three single strands of a benzoboroxole modified collagen model peptide. This ist he first example of a covalent reversible capped collagen triple helix. Different cap-structures led to a stabilization oft he triple helical structure in all cases. A variation of the charge pattern led to the formation of different supramolecular aggregates.Soluble aggregates with broad or narrow size distribution as well as unsoluble aggregates were observed. The ability of precipitating silica of collagen model peptids is only little investigated. In this work, a link between aggregation or charge pattern and the ability of silica precipitation was observed. This is a significant progress in the synthesis of organic-inorganic-hybrid material based on collagens.