Related ArticlesFluorine-19 NMR spectroscopy of fluorinated analogs of tritrpticin highlights a distinct role for Tyr residues in antimicrobial peptides.
Biochim Biophys Acta Biomembr. 2020 Mar 03;:183260
Authors: Arias M, Aramini JM, Riopel ND, Vogel HJ
Abstract
Because of their potential as novel antibiotic agents, antimicrobial peptides (AMPs) have generated considerable interest. The mechanism of bacterial toxicity of AMPs often involves the disruption and/or permeabilization of the bacterial membrane; even those that act intracellularly first have to traverse the membrane. In this work we have explored the incorporation of the fluorinated aromatic amino acids fluoro-Phe and fluoro-Tyr into the Trp- and Arg-rich AMP tritrpticin, and investigated their role in the membrane binding properties and the antimicrobial activity of the peptide. Fluorinated peptides were obtained with good yield by recombinant expression of tritrpticin as a calmodulin-fusion protein in Escherichia coli. Cells were grown in the presence of glyphosate, an inhibitor of aromatic amino acid biosynthesis, and the peptides were released by proteolysis from the purified fusion protein. By using SDS micelles, as a simplified model of the bacterial cytoplasmic membrane, we could study the peptide-membrane interactions and the preferred location of individual fluorinated residues in the micelles by 19F NMR spectroscopy. Solvent-perturbation 19F NMR measurements revealed that para-fluoro-Phe residues are embedded deeply in the hydrophobic region of the micelles. On the other hand, 3-fluoro-Tyr residues introduced in tritrpticin were located near the surface of the micelles with high solvent exposure, while 2-fluoro-Tyr sidechains were less solvent exposed. In combination with the outcome of determinations of their antimicrobial activity, our 19F NMR results indicate that the higher solvent exposure of Tyr residues correlates with a decrease of the antimicrobial potency. This different role of Tyr can likely be extended from tritrpticin to other cationic AMPs.
PMID: 32142822 [PubMed - as supplied by publisher]
[NMR paper] Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H solid-state NMR.
Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H 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 Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by (2)H solid-state NMR.
Biochim Biophys Acta. 2016 12;1858(12):2959-2964
Authors: Laadhari M, Arnold AA, Gravel AE, Separovic F, Marcotte I
Abstract
Nuclear magnetic resonance (NMR) is...
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[NMR paper] Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Related Articles Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Methods Mol Biol. 2017;1548:73-88
Authors: Wimmer R, Uggerhřj LE
Abstract
NMR spectroscopy is a well-established technique to determine the structure of peptides and small proteins in solution, also when bound to detergent micelles or phospholipid bicelles. The structure of the peptide alone is,...
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[NMR paper] NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.
NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.
NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.
Biophys J. 2016 Jan 19;110(2):423-430
Authors: Jeong JH, Kim JS, Choi SS, Kim Y
Abstract
Lactophoricin (LPcin), a component of proteose peptone (113-135) isolated from bovine milk, is a cationic amphipathic antimicrobial peptide consisting of 23 amino acids. We designed a series of N- or C-terminal truncated variants, mutated analogs, and truncated mutated analogs using peptide-engineering techniques....
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[NMR paper] On the role of NMR spectroscopy for characterization of antimicrobial peptides.
On the role of NMR spectroscopy for characterization of antimicrobial peptides.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles On the role of NMR spectroscopy for characterization of antimicrobial peptides.
Methods Mol Biol. 2013;1063:159-80
Authors: Porcelli F, Ramamoorthy A, Barany G, Veglia G
Abstract
Antimicrobial peptides (AMPs) provide a primordial source of immunity, conferring upon eukaryotic cells resistance against bacteria,...
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NMR Structural Studies of Antimicrobial Peptides as In-Plane Helix of Membrane Proteins
NMR Structural Studies of Antimicrobial Peptides as In-Plane Helix of Membrane Proteins
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Yongae Kim , Ji-Ho Jeong , Ji-Sun Kim</br>
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01-29-2014 12:50 AM
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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[NMR paper] NMR studies of fluorinated visual pigment analogs.
NMR studies of fluorinated visual pigment analogs.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of fluorinated visual pigment analogs.
Biochem Biophys Res Commun. 1991 Sep 30;179(3):1337-43
Authors: Colmenares LU, Asato AE, Denny M, Mead D, Zingoni JP, Liu RS
The 19F-nmr chemical shift data of isomeric pigments (11-cis and 9-cis) of four vinyl fluororhodopsins and two trifluororhodopsins have been recorded. When compared with model protonated Schiff...
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[NMR paper] NMR studies of fluorinated visual pigment analogs.
NMR studies of fluorinated visual pigment analogs.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of fluorinated visual pigment analogs.
Biochem Biophys Res Commun. 1991 Sep 30;179(3):1337-43
Authors: Colmenares LU, Asato AE, Denny M, Mead D, Zingoni JP, Liu RS
The 19F-nmr chemical shift data of isomeric pigments (11-cis and 9-cis) of four vinyl fluororhodopsins and two trifluororhodopsins have been recorded. When compared with model protonated Schiff...