TY - JOUR
T1 - Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy
AU - Naito, Akira
AU - Matsumori, Nobuaki
AU - Ramamoorthy, Ayyalusamy
N1 - Funding Information:
Researches in the Naito and Matsumori groups were supported by grants-in-aid for Scientific Research in an Innovative Area 16H00756 (AN) and 16H00773 (NM), and by grants-in-aid for Scientific Research (C) 15K06963 (AN) and (B) 15H03121 (NM) from the Ministry of Education, Culture, Sports, Science and Technology of Japan . Research in the Ramamoorthy laboratory has been supported by funds from the National Institutes of Health : for studies on antimicrobial peptides (AI054515), amyloid proteins ( AG048934 and Protein Folding Disease Center at the University of Michigan), and membrane proteins ( GM084018 ). NIH funding supports for the purchase a 600 MHz solid-state NMR spectrometer (to A.R.) and to upgrade a 400 MHz solid-state NMR spectrometer ( GM08401816-S1 to A.R.) at the University of Michigan are also acknowledged. A.R. thanks the past and present members of the “Ramyloid” subgroup in the Ramamoorthy laboratory and all the collaborators who have made contributions to overcome the numerous challenges in the exciting amyloid and antimicrobial projects.
Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2018/2
Y1 - 2018/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85020828329&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85020828329&partnerID=8YFLogxK
U2 - 10.1016/j.bbagen.2017.06.004
DO - 10.1016/j.bbagen.2017.06.004
M3 - Review article
C2 - 28599848
AN - SCOPUS:85020828329
VL - 1862
SP - 307
EP - 323
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 2
ER -