1DUM

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

Summary for 1DUM

• Entry DOI: 10.2210/pdb1dum/pdb
• Descriptor: MAGAININ 2 (1 entity in total)
• Functional Keywords: antibiotic, magainin, dimer, amphipathic helix, membrane, vesicle, bilayer, antimicrobial protein
• Total number of polymer chains: 2
• Total formula weight: 5053.95

Authors

Takeda, A.,Wakamatsu, K.,Tachi, T.,Matsuzaki, K. (deposition date: 2000-01-18, release date: 2001-06-27, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR