Antimicrobial and Cell-Penetrating Peptides: Structure, Assembly and Mechanisms of Membrane Lysis via Atomistic and Coarse-Grained Molecular Dynamic Simulations
Keywords: (CG-MD); (DMPC); (DOPC); (DPPC); (POPC); (POPG); 2,2,2-Trifluoroethanol (TFE); Antimicrobial peptides; Coarse-grained (CG) forcefields; Gramicidin A; MARTINI; MSI-78; NMR; X-ray crystallography; amphipathic; assembly; barrel-stave model; buforin II; carpet mechanism; cationic membrane proteins; cell penetrating peptides (CPPs); coarse grain; disor-dered toroidal pore; dynamics; lipid; lipid bilayer; lipid bilayers; lytic activity; magainins; melittin; melittins; membrane; membrane lysis; molecular dynamics simulation; self-assembly; sodiumdodecylsulfate (SDS); transmembrane (TM) peptides; viral RNA; zwitterionic diphosphocholine
Document Type: Research Article
Publication date: 01 November 2010
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.