[NMR paper] Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
Related ArticlesStructural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
ACS Chem Biol. 2015 Apr 17;10(4):965-9
Authors: Malgieri G, Avitabile C, Palmieri M, D'Andrea LD, Isernia C, Romanelli A, Fattorusso R
Abstract
We here report an original approach to elucidate mechanisms of action of antimicrobial peptides and derive crucial structural requirements for the design of novel therapeutic agents. The high resolution structure of TB_KKG6A, an antimicrobial peptide designed to amplify the spectrum of action of Temporin B, bound to E. coli is here determined by means of CD and NMR methodologies. We have also defined, through STD analysis, the residues in closer proximity to the bacterial membrane.
[NMR paper] Synthesis, spectroscopic investigations (X-ray, NMR and TD-DFT), antimicrobial activity and molecular docking of 2,6-bis(hydroxy(phenyl)methyl)cyclohexanone.
Synthesis, spectroscopic investigations (X-ray, NMR and TD-DFT), antimicrobial activity and molecular docking of 2,6-bis(hydroxy(phenyl)methyl)cyclohexanone.
Related Articles Synthesis, spectroscopic investigations (X-ray, NMR and TD-DFT), antimicrobial activity and molecular docking of 2,6-bis(hydroxy(phenyl)methyl)cyclohexanone.
Molecules. 2015;20(7):13240-63
Authors: Barakat A, Ghabbour HA, Al-Majid AM, Soliman SM, Ali M, Mabkhot YN, Shaik MR, Fun HK
Abstract
The synthesis of 2,6-bis(hydroxy(phenyl)methyl)cyclohexanone 1...
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[NMR paper] Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.
Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.
Biochim Biophys Acta. 2015 Jan;1848(1 Pt B):350-62
Authors: Kim SJ, Chang J, Singh M
Abstract
Peptidoglycan is an essential component of cell wall in Gram-positive bacteria with unknown architecture. In this review, we summarize solid-state NMR...
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02-13-2015 05:31 PM
[NMR paper] The Structural Basis of the Green-Blue Color Switching in Proteorhodopsin determined by NMR Spectroscopy.
The Structural Basis of the Green-Blue Color Switching in Proteorhodopsin determined by NMR Spectroscopy.
The Structural Basis of the Green-Blue Color Switching in Proteorhodopsin determined by NMR Spectroscopy.
J Am Chem Soc. 2014 Nov 21;
Authors: Mao J, Do NN, Scholz F, Reggie L, Mehler M, Lakatos A, Ong YS, Ullrich SJ, Brown LJ, Brown RC, Becker-Baldus J, Wachtveitl J, Glaubitz C
Abstract
Proteorhodopsins (PRs) found in marine microbes are the most abundant retinal-based photoreceptors on this planet. PR variants show a high...
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11-23-2014 03:47 AM
[NMR paper] The Na(+) transport in Gram-positive bacteria defect in the Mrp antiporter complex measured with (23)Na-NMR.
The Na(+) transport in Gram-positive bacteria defect in the Mrp antiporter complex measured with (23)Na-NMR.
Related Articles The Na(+) transport in Gram-positive bacteria defect in the Mrp antiporter complex measured with (23)Na-NMR.
Anal Biochem. 2013 Oct 15;
Authors: Górecki K, Hägerhäll C, Drakenberg T
Abstract
(23)Na-NMR has previously been used to monitor Na(+) translocation across membranes in Gram-negative bacteria and in various other organelles and liposomes using a membrane-impermeable shift reagent to resolve the signals...
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10-23-2013 03:49 AM
[NMR paper] Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
Biophys J. 2012 Oct 3;103(7):1470-9
Authors: Lorin A, Noël M, Provencher MÈ, Turcotte V, Cardinal S, Lagüe P, Voyer N, Auger M
Abstract
We have previously...
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
Chembiochem. 2010 Nov 22;11(17):2424-32
Authors: Díaz MD, Palomino-Schätzlein M, Corzana F, Andreu C, Carbajo RJ, del Olmo M, Canales-Mayordomo A, Pineda-Lucena A, Asensio G, Jiménez-Barbero J
The conformations of two synthetic pentapeptides with...
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05-04-2011 04:14 PM
Exploring platelet chemokine antimicrobial activity: NMR backbone dynamics studies of NAP-2 and TC-1.
Exploring platelet chemokine antimicrobial activity: NMR backbone dynamics studies of NAP-2 and TC-1.
Exploring platelet chemokine antimicrobial activity: NMR backbone dynamics studies of NAP-2 and TC-1.
Antimicrob Agents Chemother. 2011 Feb 14;
Authors: Nguyen LT, Kwakman PH, Chan DI, Liu Z, de Boer L, Zaat SA, Vogel HJ
The platelet chemokines NAP-2 and TC-1 differ by only two amino acids at their carboxy-terminal end. Nevertheless they display a significant difference in their direct antimicrobial activity, with the longer NAP-2 being inactive...
Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
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