Berlin 2018 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 20: Poster Session I
CPP 20.11: Poster
Montag, 12. März 2018, 17:30–19:30, Poster A
Simulations of linear and cyclic RGD peptides at a free surface of the polymer brushes — •Olga Guskova1,2, Ulla König1, Petra Uhlmann1, and Jens-Uwe Sommer1,2 — 1IPF Dresden — 2DCMS, TU Dresden
Motivated by recent experiments [1,2] aiming at biomimetic design of new polymeric surfaces relevant for the biotechnological applications, the behaviour of short peptides with the RGD motif, mimicking the cell adhesion proteins, is simulated using DFT/MD combination. Three peptides are modeled: linear GRGDS, linear GRGDSPK and cyclic cRGDyK in aqueous solutions and being chemically attached to the PAA brush surface. For free peptides, the net charge and the charge pattern are characterized and the most reactive amino-groups are predicted based on the ESP charges. The free energy of hydration calculated by thermodynamic integration shows the negative values and changes in the row GRGDS>GRGDSPK>cRGDyK. Secondary structures of linear peptides have ''normally allowed'' β-regions, β-turns and coil-like structures, whereas the cyclic chain is sterically restraint. The secondary structures and the radial distribution functions of water around the charged peptide groups are calculated for the chains attached to PAA backbone. We compare the shielding and exposure of bound GRGDS, GRGDSPK and cRGDyK peptides and the availability of the RGD sequence and R-side chain at the brush surface.
[1] E. Psarra et al. ACS Omega, 2017, 2, 946.
[2] U. König et al. Biointerphases 2017 (submitted).