Dresden 2006 – wissenschaftliches Programm
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AKB: Biologische Physik
AKB 40: Poster Session II
AKB 40.60: Poster
Mittwoch, 29. März 2006, 16:30–19:30, P3
Structure and Stability of Thiol Containing Collagen Peptides — •Christian Renner1,2, Ulrike Kusebauch1, Sergio Cadamuro1, and Luis Moroder1 — 1Max-Planck-Institut für Biochemie, D-82152 Martinsried — 2School of Biomedical and Natural Sciences, Nottingham Trent University, Nottingham NG11 8NS, UK
Collagen is the most abundant protein in mammals and as a natural biomaterial confers stability and strength to tissue. The dominant structural element is the right-handed triple helix that consists of three left-handed poly proline II-like helices formed by the single amino acid chains and coiled around each other. These trimeric super-helices build chemically cross-linked fibrils or networks that can associate to even larger structures. Cysteine residues are present in native collagens in non-triple helical portions where during maturation interchain disulfide knots are formed to crosslink the constituent three chains, but single cysteine residues of unknown structural and/or biological function are also found in triple-helical sequence portions. In the present study we have synthesized and analysed collagen peptides based on the regular structure (Gly-Pro-Hyp)n (Hyp is (4R)-hydroxyproline) where one or two amino acids were exchanged for cysteine. The reactivity of the thiol groups thus introduced allows to crosslink peptide chains within the triple helix or link different triple helices for forming a stable biomaterial. Moreover, selective 15N-labeling of individual glycine residues was expected to allow monitoring of thermal unfolding of the triple helix at defined sites and thus to analyze with spatial resolution the structural stability of the overall rod-like collagen triple helix.