Structure and orientation of the antibiotic peptide magainin in membranes by solid‐state nuclear magnetic resonance spectroscopy

Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One‐ and two‐dimensional solid‐state 15N NMR spectra of specifically 15N‐labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is α‐helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.

[1]  S. Opella,et al.  fd coat protein structure in membrane environments. , 1993, Journal of molecular biology.

[2]  J Skolnick,et al.  Insertion of peptide chains into lipid membranes: An off‐lattice Monte Carlo dynamics model , 1993, Proteins.

[3]  H. Guy,et al.  Modeling the ion channel structure of cecropin. , 1992, Biophysical journal.

[4]  J. H. Spencer,et al.  Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy. , 1992, Biochemistry.

[5]  C. J. Salter,et al.  An electrophysiological and spectroscopic study of the properties and structure of biological calcium channels. Investigations of a model ion channel. , 1992, Biochimica et biophysica acta.

[6]  S. Opella,et al.  Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation. , 1992, Biophysical journal.

[7]  S. O. Smith,et al.  Solid-state NMR approaches for studying membrane protein structure. , 1992, Annual review of biophysics and biomolecular structure.

[8]  S. Opella,et al.  Flat-coil probe for NMR spectroscopy of oriented membrane samples , 1991 .

[9]  J. Gesell,et al.  Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy , 1991, Journal of biomolecular NMR.

[10]  S. Opella,et al.  NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein. , 1991, Science.

[11]  J. Barker,et al.  Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[12]  H. G. Boman,et al.  Antibacterial peptides: Key components needed in immunity , 1991, Cell.

[13]  N. Fujii,et al.  Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. , 1991, Biochimica et biophysica acta.

[14]  S. Opella,et al.  NMR-Structural Studies of Membrane Bound Peptides and Proteins , 1991 .

[15]  I. Shalit,et al.  All‐D‐magainin: chirality, antimicrobial activity and proteolytic resistance , 1990, FEBS letters.

[16]  R. B. Merrifield,et al.  All-D amino acid-containing channel-forming antibiotic peptides. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[17]  K. Gable,et al.  Raman spectroscopy of synthetic antimicrobial frog peptides magainin 2a and PGLa. , 1990, Biochemistry.

[18]  S. Opella,et al.  Improvements in determining structural information from solid-state NMR spectra , 1990 .

[19]  M. Zasloff,et al.  Peptides from frog skin. , 1990, Annual review of biochemistry.

[20]  Q. Teng,et al.  The in situ determination of the 15N chemical-shift tensor orientation in a polypeptide , 1989 .

[21]  Isao Ando,et al.  Nitrogen-15 NMR chemical shift tensors and conformation of some nitrogen-15-labeled polypeptides in the solid state , 1989 .

[22]  G. Molle,et al.  Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. , 1989, Biophysical journal.

[23]  R. Cooke,et al.  High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein , 1989, FEBS letters.

[24]  H V Westerhoff,et al.  Magainins and the disruption of membrane-linked free-energy transduction. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[25]  N. Fujii,et al.  Magainin 1-induced leakage of entrapped calcein out of negatively-charged lipid vesicles. , 1989, Biochimica et biophysica acta.

[26]  B. Kachar,et al.  Spontaneous polymerization of the antibiotic peptide magainin 2 , 1989, FEBS letters.

[27]  P. Stewart,et al.  Solid-state nuclear magnetic resonance structural studies of proteins. , 1989, Methods in enzymology.

[28]  Hao‐Chia Chen,et al.  Synthetic magainin analogues with improved antimicrobial activity , 1988, FEBS letters.

[29]  R. B. Merrifield,et al.  Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[30]  W. DeGrado,et al.  Synthetic amphiphilic peptide models for protein ion channels. , 1988, Science.

[31]  S. Oiki,et al.  Channel protein engineering: synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[32]  M. Zasloff,et al.  Antimicrobial activity of synthetic magainin peptides and several analogues. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[33]  A. Bax,et al.  A two‐dimensional NMR study of the antimicrobial peptide magainin 2 , 1988, FEBS letters.

[34]  Structural Models for Membrane Insertion and Channel Formation by Antiparallel Alpha Helical Membrane Peptides , 1988 .

[35]  S. O. Smith,et al.  High-resolution solid-state NMR of proteins. , 1988, Annual review of physical chemistry.

[36]  M. Zasloff,et al.  Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[37]  T. Oas,et al.  Determination of the nitrogen-15 and carbon-13 chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patterns , 1987 .

[38]  F. Dahlquist,et al.  The Amide 15N Chemical Shift Tensors of Four Peptides Determined from 13C Dipole-Coupled Chemical Shift Powder Patterns , 1987 .

[39]  P. Stewart,et al.  Protein structure by solid-state NMR spectroscopy , 1987, Quarterly Reviews of Biophysics.

[40]  Kaiser Et,et al.  Peptides with affinity for membranes. , 1987 .

[41]  E. Kaiser,et al.  Peptides with affinity for membranes. , 1987, Annual review of biophysics and biophysical chemistry.

[42]  D. Suter,et al.  Spin dynamics and thermodynamics in solid‐state NMR cross polarization , 1986 .

[43]  D. Torchia,et al.  15N chemical shift and 15N-13C dipolar tensors for the peptide bond in [1-13C]glycyl[15N]glycine hydrochloride monohydrate , 1984 .

[44]  J. Waugh.  Uncoupling of local field spectra in nuclear magnetic resonance: determination of atomic positions in solids. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[45]  Alexander Pines,et al.  Proton‐enhanced NMR of dilute spins in solids , 1973 .

[46]  M. Schiffer,et al.  Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. , 1967, Biophysical journal.