[HTML][HTML] Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR …

RM Verly, CM De Moraes, JM Resende, C Aisenbrey… - Biophysical journal, 2009 - cell.com
DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has
been prepared by solid-phase chemical peptide synthesis and its conformation was studied …

Consequences of N-acylation on structure and membrane binding properties of dermaseptin derivative K4-S4-(1-13)

DE Shalev, S Rotem, A Fish, A Mor - Journal of Biological Chemistry, 2006 - ASBMB
Acyl conjugation to antimicrobial peptides is known to enhance antimicrobial properties.
Here, we investigated the consequences of aminolauryl (NC 12) conjugation to the …

[HTML][HTML] The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy

B Bechinger - Biochimica et Biophysica Acta (BBA)-Biomembranes, 1999 - Elsevier
Linear peptide antibiotics have been isolated from amphibians, insects and humans and
used as templates to design cheaper and more potent analogues for medical applications …

Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy

JM Resende, CM Moraes… - Proceedings of the …, 2009 - National Acad Sciences
The heterodimeric antimicrobial peptide distinctin is composed of 2 linear peptide chains of
22-and 25-aa residues that are connected by a single intermolecular SS bond. This …

Conformation–activity relationship of a novel peptide antibiotic: structural characterization of dermaseptin DS 01 in media that mimic the membrane environment

MA Castiglione‐Morelli, P Cristinziano… - Peptide Science …, 2005 - Wiley Online Library
Dermaseptins, small polycationic peptides synthesized by amphibians, exert a lytic action on
bacteria, protozoa, yeast, and filamentous fungi at micromolar concentrations, but unlike …

Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin

A Ramamoorthy, S Thennarasu, DK Lee, A Tan… - Biophysical journal, 2006 - cell.com
The mechanism of membrane interaction of two amphipathic antimicrobial peptides, MSI-78
and MSI-594, derived from magainin-2 and melittin, is presented. Both the peptides show …

The membrane interactions of antimicrobial peptides revealed by solid-state NMR spectroscopy

B Bechinger, ES Salnikov - Chemistry and physics of lipids, 2012 - Elsevier
Solid-state NMR spectroscopic techniques provide valuable information about the structure,
dynamics and topology of membrane-inserted polypeptides. In particular antimicrobial …

Solution and solid-state nuclear magnetic resonance structural investigations of the antimicrobial designer peptide GL13K in membranes

N Harmouche, C Aisenbrey, F Porcelli, Y Xia… - Biochemistry, 2017 - ACS Publications
The antimicrobial peptide GL13K encompasses 13 amino acid residues and has been
designed and optimized from the salivary protein BPIFA2 to exhibit potent bacteriocidal and …

Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR

RW Glaser, C Sachse, UHN Dürr, P Wadhwani… - Biophysical journal, 2005 - cell.com
The membrane-disruptive antimicrobial peptide PGLa is found to change its orientation in a
dimyristoyl-phosphatidylcholine bilayer when its concentration is increased to biologically …

Solid-state NMR investigations of peptide− lipid interaction and orientation of a β-sheet antimicrobial peptide, protegrin

S Yamaguchi, T Hong, A Waring, RI Lehrer… - Biochemistry, 2002 - ACS Publications
Protegrin-1 (PG-1) is a broad-spectrum β-sheet antimicrobial peptide found in porcine
leukocytes. The mechanism of action and the orientation of PG-1 in lipid bilayers are here …