title: The role of tryptophan spatial arrangement for antimicrobial-derived, membrane-active peptides adsorption and activity.
abstract: Herein we explored the role of topological distribution of aromatic amino acids in peptide-membrane interfacial interactions. The membrane activity of closely related peptides and their binding energy is sensitive to the positioning of minimum two tryptophans, and by the degree of flanking at the membrane interface mediated by aromatic amino acids.
authors.affiliation: Department of Physics, Laboratory of Molecular Biophysics and Medical Physics, Alexandru I. Cuza University, Iasi 700506, Romania.
authors.forename: Irina
authors.initials: I
authors.lastname: Schiopu
authors.forename: Loredana
authors.initials: L
authors.lastname: Mereuta
authors.forename: Aurelia
authors.initials: A
authors.lastname: Apetrei
authors.forename: Yoonkyung
authors.initials: Y
authors.lastname: Park
authors.forename: Kyung-Soo
authors.initials: KS
authors.lastname: Hahm
authors.forename: Tudor
authors.initials: T
authors.lastname: Luchian
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D000890:Anti-Infective Agents; D010455:Peptides; D014364:Tryptophan