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 antimicrobial activity and their 4-fluorophenylalanine (Pff)-containing analogues (ArXArXAr-NH(2); Ar=Phe, Pff; X=Lys, Arg) have been studied. NMR experiments carried out both in aqueous fluoroalcohol solutions and SDS micelles permitted their interactions with membrane-like environments to be explored. WaterLOGSY experiments and Mn(2+)-based paramagnetic probes were also applied to assess their orientations with respect to the SDS micelles. In addition, pulse-field gradient (PFG) diffusion NMR spectroscopy studies were conducted, under different experimental conditions (i.e., concentration, temperature) to characterize the possible changes in the peptides' aggregation states as a putative critical factor for their antimicrobial activity. Finally, molecular dynamics simulations on a variety of conformations showed the intrinsic flexibility of these peptides in both aqueous solutions and membrane-mimetic systems.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Biophys J. 2011 Sep 7;101(5):1193-201
Authors: Park TJ, Kim JS, Ahn HC, Kim Y
Abstract
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any...
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09-06-2011 06:02 PM
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Biochemistry. 2011 May 10;50(18):3784-95
Authors: Salnikov ES, Aisenbrey C, Balandin SV, Zhmak MN, Ovchinnikova TV, Bechinger B
The antimicrobial arenicin peptides are cationic amphipathic sequences that strongly interact with membranes. Through a cystine ring closure a cyclic ?-sheet structure is formed...
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07-13-2011 06:42 PM
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
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Biochemistry
DOI: 10.1021/bi1018732
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04-16-2011 02:04 AM
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...
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02-16-2011 07:40 PM
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
[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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11-24-2010 08:58 PM
[NMR paper] Relationships between protein structure and dynamics from a database of NMR-derived b
Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.
Related Articles Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.
J Mol Biol. 2000 Jan 28;295(4):963-78
Authors: Goodman JL, Pagel MD, Stone MJ
The amplitude of protein backbone NH group motions on a time-scale faster than molecular tumbling may be determined by analysis of (15)N NMR relaxation data according to the Lipari-Szabo model free formalism. An internet-accessible...
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11-18-2010 09:15 PM
[NMR paper] Structure-function relationships in human epidermal growth factor studied by site-dir
Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
Related Articles Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
Biochemistry. 1991 Sep 10;30(36):8891-8
Authors: Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID
In order to elucidate the mechanism of interaction between human epidermal growth factor (EGF) and its receptor, selected variants of EGF, differing by single amino acid substitutions, have been...
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations.
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