1DUM

NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES

1DUM の概要

• エントリーDOI: 10.2210/pdb1dum/pdb
• 分子名称: MAGAININ 2 (1 entity in total)
• 機能のキーワード: antibiotic, magainin, dimer, amphipathic helix, membrane, vesicle, bilayer, antimicrobial protein
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 5053.95

構造登録者

Takeda, A.,Wakamatsu, K.,Tachi, T.,Matsuzaki, K. (登録日: 2000-01-18, 公開日: 2001-06-27, 最終更新日: 2024-05-22)

主引用文献

Hara, T.,Kodama, H.,Kondo, M.,Wakamatsu, K.,Takeda, A.,Tachi, T.,Matsuzaki, K.
Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue.
Biopolymers, 58:437-446, 2001

PubMed Abstract: To elucidate the effects of peptide dimerization on pore formation by magainin 2 (MG2), a covalently linked antiparallel dimer of the MG2 analogue [(F5Y, L6C, F16W, I20C-MG2)(2): II] was synthesized based on the dimer structure revealed by our NMR study. The interactions of the dimer with lipid bilayers were investigated by CD and fluorescence in comparison with a monomer analogue (F5Y, F16W-MG2: I). Similar to I, II was found to form a peptide-lipid supramolecular complex pore accompanied with lipid flip-flop and peptide translocation. The pore formed by II was characterized by a slightly larger pore diameter and a threefold longer lifetime than that of I, although the pore formation rate of the dimer was lower than that of the monomer. The coexistence of the dimer and the monomer exhibited slight but significant synergism in membrane permeabilization, which was maximal at a monomer/dimer ratio of 3. Therefore, we concluded that a pentameric pore composed of one pore-stabilizing dimer and three monomers maximized the overall leakage activity in keeping with our kinetic prediction.

PubMed: 11180056
DOI: 10.1002/1097-0282(20010405)58:4<437::AID-BIP1019>3.3.CO;2-9

実験手法

SOLUTION NMR