Title : Electrostatics and flexibility drive membrane recognition and early penetration by the antimicrobial peptide dendrimer bH1.

Pub. Date : 2013 Oct 9

PMID : 23959139






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Molecular dynamics simulations of the polycationic antimicrobial peptide dendrimer (Leu)8(DapLeu)4(DapPhe)2DapLys-NH2 binding to membranes suggest that electrostatic interactions with the polyanionic lipopolysaccharide (LPS) and conformational flexibility of the 2,3-diaminopropanoic acid (Dap) branching units drive its selective insertion into microbial membranes. 2,3-diaminopropionic acid selectin L Homo sapiens
2 Molecular dynamics simulations of the polycationic antimicrobial peptide dendrimer (Leu)8(DapLeu)4(DapPhe)2DapLys-NH2 binding to membranes suggest that electrostatic interactions with the polyanionic lipopolysaccharide (LPS) and conformational flexibility of the 2,3-diaminopropanoic acid (Dap) branching units drive its selective insertion into microbial membranes. 2,3-diaminopropionic acid selectin L Homo sapiens