Regensburg 2004 – wissenschaftliches Programm
CPP 13: SYMPOSIUM: Understanding and Controlling Complex Structures: From Synthetic Polymers to Biomaterials I
CPP 13.8: Vortrag
Dienstag, 9. März 2004, 12:00–12:15, H 37
Synthetic collagen peptides give clues to triple helix stability — •Christian Renner, Dirk Barth, Alexander Milbradt, Barbara Sacca, Hans-Juergen Musiol, and Luis Moroder — MPI fuer Biochemie, 82152 Martinsried
Collagen is the most abundant protein in mammals. It gives mechanical strength to tissue through its unique molecular structure: In the collagen triple helix three protein strands that each form a left-handed helix pack together resulting in a right-handed super helix. Although collagens have been investigated by biologists, chemists and physicists for many decades, the rules governing triple helix stability and thus collagen function have not yet been fully elucidated. Surprisingly, repetition of the simple amino acid triplet (Gly-Pro-Pro/Hyp) is sufficient for generating the supramolecular organisation of the collagen helix with high stability. We have used synthetic collagen peptides, where one hydrogen atom of each triplet is substituted by fluorine, to study the influence of the fluorinated position on structure and stability (1). We found that current explanations of triple helix stability are inadequately simple and have to be replaced by a detailed and quantitative view of the combination of interactions involved. Additional means for investigation and stabilisation of triple helices are natural (2) or synthetic cystine knots (3).
(1) Barth, D., Milbradt, A. G., Renner, C. and Moroder, L. (2003) ChemBioChem, in press. (2) Barth, D., Kyrieleis, O., Renner, C. and Moroder L. (2003) Chem. Eur. J. 9, 3703-3714. (3) Renner, C., Sacca, B. and Moroder, L. (2003) Biopolymers, in press.