Berlin 2005 – wissenschaftliches Programm
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AKB: Biologische Physik
AKB 30: Biomaterials
AKB 30.1: Vortrag
Freitag, 4. März 2005, 17:30–17:45, TU H2013
Proteoglycan conformation and mechanical properties: A molecular modeling investigation — •Mark Bathe1, Gregory C. Rutledge2, Alan J. Grodzinsky2, and Bruce Tidor2 — 1HMI Berlin, Germany — 2MIT Cambridge MA, USA
Proteoglycans (PGs) play a central role in determining the structural and biomechanical properties of tissues ranging from articular cartilage to the central nervous system. They are high molecular weight comb biopolymers consisting of anywhere from one to one hundred glycosaminoglycans (GAGs) (anionic polysaccharides) grafted to a linear protein backbone. PG chemical composition varies considerably with the disease state of tissues, making it of fundamental importance to biology to understand their composition-function relationship.
Towards this aim, we simulate PG conformation and osmotic pressure using a coarse-grained molecular model. GAG molecular weight, degree of sulfation, and grafting density affect significantly the apparent persistence length of PGs, whereas GAG sulfation type (4 vs. 6) and pattern do not. Similarly, GAG osmotic pressure is influenced primarily by its sulfation density. Our results reaffirm that variations in PG composition may be used to alter significantly the structural and biomechanical properties of a variety of tissues, and provide quantitative new insight into the structure-function relationship of this important class of biomolecules.