Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
A variety of biomolecules acting on the cell membrane folds into a biologically active structure in the membrane environment. It is, therefore, important to determine the structures and dynamics of such biomolecules in a membrane environment. While several biophysical techniques are used to obtain low-resolution information, solid-state NMR spectroscopy is one of the most powerful means for determining the structure and dynamics of membrane bound biomolecules such as antibacterial biomolecules and amyloidogenic proteins; unlike X-ray crystallography and solution NMR spectroscopy, applications of solid-state NMR spectroscopy are not limited by non-crystalline, non-soluble nature or molecular size of membrane-associated biomolecules. This review article focuses on the applications of solid-state NMR techniques to study a few selected antibacterial and amyloid peptides. Solid-state NMR studies revealing the membrane inserted bent α-helical structure associated with the hemolytic activity of bee venom melittin and the chemical shift oscillation analysis used to determine the transmembrane structure (with α-helix and 310-helix in the N- and C-termini, respectively) of antibiotic peptide alamethicin are discussed in detail. Oligomerization of an amyloidogenic islet amyloid polypeptide (IAPP, or also known as amylin) resulting from its aggregation in a membrane environment, molecular interactions of the antifungal natural product amphotericin B with ergosterol in lipid bilayers, and the mechanism of lipid raft formation by sphingomyelin studied using solid state NMR methods are also discussed in this review article. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
['Naito|Akira|A|', 'Matsumori|Nobuaki|N|', 'Ramamoorthy|Ayyalusamy|A|']
D058227:Amyloidogenic Proteins D000818:Animals D000900:Anti-Bacterial Agents D000935:Antifungal Agents D019295:Computational Biology D006801:Humans D007700:Kinetics D008024:Ligands D008563:Membrane Lipids D021962:Membrane Microdomains D008565:Membrane Proteins D008567:Membranes, Artificial D008954:Models, Biological D056004:Molecular Dynamics Simulation D019906:Nuclear Magnetic Resonance, Biomolecular D011485:Protein Binding D011487:Protein Conformation D013329:Structure-Activity Relationship
Solid-state NMR Membrane environment IAPP Antifungal natural product Lipid raft Amyloidogenic peptide Antibacterial peptide