Binding of antimicrobial peptides (latarcins, Ltcs) to the sodiumdodecyl sulfate micelle (SDS, 60 detergent molecules) as revealed by molecular dynamics (MD) simulations. Final MD-structures of Ltcs are the result of their fine-tuned interactions with the heterogeneous water-detergent interface. Thus, rigid amphipatic helix of Ltc1 retains rod-like conformation in the micelle, whereas flexible Ltc2a forms kinked conformation adapting to polar/hydrophobic properties of the micelle surface. Cationic, hydrophobic and polar residues are shown in stick representation. Solvent accessible surface of SDS micelle is colored as follows: polar heads red, acyl chains gray (Polyansky et al., JBCB, 2007).
Our main interests include computer simulations of membrane and membrane-active peptides and proteins, especially development of protein solvation models for membrane-mimic media. Among the objects we are working on: cardiotoxins, fusion peptides, seven-helix receptors of the GPCR family, glycophorin A and its dimers, signal peptides.
Among our objectives is understanding of spatial structure-function relationships for membrane proteins via molecular modeling techniques.
For more information see our projects.
Find out how to contact us.
Address: 117997 Russia, Moscow, ul. Miklukho-Maklaya 16/10.