Related ArticlesStable isotope-assisted NMR characterization of interaction between lipid A and sarcotoxin IA, a cecropin-type antibacterial peptide.
Biochem Biophys Res Commun. 2013 Feb 8;431(2):136-40
Authors: Yagi-Utsumi M, Yamaguchi Y, Boonsri P, Iguchi T, Okemoto K, Natori S, Kato K
Abstract
Sarcotoxin IA is a 39-residue cecropin-type peptide from Sarcophaga peregrina. This peptide exhibits antibacterial activity against Gram-negative bacteria through its interaction with lipid A, a core component of lipopolysaccharides. To acquire detailed structural information on this specific interaction, we performed NMR analysis using bacterially expressed sarcotoxin IA analogs with (13)C- and (15)N-labeling along with lipid A-embedding micelles composed of dodecylphosphocholine. By inspecting the stable isotope-assisted NMR data, we revealed that the N-terminal segment (Leu3-Arg18) of sarcotoxin IA formed an amphiphilic ?-helix upon its interaction with the aqueous micelles. Furthermore, chemical shift perturbation data indicated that the amino acid residues displayed on this ?-helix were involved in the specific interaction with lipid A. On the basis of these data, we successfully identified Lys4 and Lys5 as key residues in the interaction with lipid A and the consequent antibacterial activity. Therefore, these results provide unique information for designing chemotherapeutics based on antibacterial peptide structures.
NMR-based stable isotope resolved metabolomics in systems biochemistry
NMR-based stable isotope resolved metabolomics in systems biochemistry
Abstract An important goal of metabolomics is to characterize the changes in metabolic networks in cells or various tissues of an organism in response to external perturbations or pathologies. The profiling of metabolites and their steady state concentrations does not directly provide information regarding the architecture and fluxes through metabolic networks. This requires tracer approaches. NMR is especially powerful as it can be used not only to identify and quantify metabolites in an unfractionated mixture such...
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03-03-2011 02:06 AM
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
J Phys Chem B. 2011 Feb 10;
Authors: Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, Vosegaard T, Nielsen NC
Recently, ether lipids have been introduced as long-term stable alternatives to the more natural,...
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02-12-2011 05:26 PM
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Methods Enzymol. 2010;478:305-22
Authors: Yamaguchi Y, Kato K
Unique advantages offered by nuclear magnetic resonance (NMR) spectroscopy provide high-resolution information not only on structures but also on dynamics and interactions of glycoconjugates in solution. These benefits are further enhanced by applying stable-isotope-labeling techniques, which we...
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12-31-2010 07:03 PM
[NMR paper] Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st
Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Related Articles Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Chem Phys Lipids. 2004 Nov;132(1):65-77
Authors: Grage SL, Afonin S, Grüne M, Ulrich AS
The interaction of the fusogenic polypeptide segment "B18" from the fertilization protein binding with lipid membranes was investigated by solid state 2H and 31P NMR, and by differential scanning calorimetry. B18 is known...
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11-24-2010 10:03 PM
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Related Articles Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Prog Nucl Magn Reson Spectrosc. 2010 May;56(4):346-59
Authors: Kato K, Yamaguchi Y, Arata Y
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10-19-2010 04:51 PM
[NMR paper] Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o
Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
Related Articles Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
J Biol Chem. 1994 Jan 21;269(3):1785-93
Authors: Draeger LJ, Mullen GP
The carboxyl-terminal 92 residues of c-Myc-92 display site-specific DNA binding specificity for the consensus sequence 5'-CACCACGTGGTG-3' (Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., and...
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08-22-2010 03:33 AM
[NMR paper] Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o
Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
Related Articles Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
J Biol Chem. 1994 Jan 21;269(3):1785-93
Authors: Draeger LJ, Mullen GP
The carboxyl-terminal 92 residues of c-Myc-92 display site-specific DNA binding specificity for the consensus sequence 5'-CACCACGTGGTG-3' (Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., and...
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08-22-2010 03:33 AM
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 19 March 2010</br>
Koichi, Kato , Yoshiki, Yamaguchi , Yoji, Arata</br>
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Stable isotope-assisted NMR characterization of interaction between lipid A and sarcotoxin IA, a cecropin-type antibacterial peptide.
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