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[PMID]:27328781
[Au] Autor:Rautenbach M; Troskie AM; Vosloo JA; Dathe ME
[Ad] Endereço:BIOPEP Peptide Group, Department of Biochemistry, Stellenbosch University, Private Bag X1, Matieland, 7600, South Africa. Electronic address: mra@sun.ac.za.
[Ti] Título:Antifungal membranolytic activity of the tyrocidines against filamentous plant fungi.
[So] Source:Biochimie;130:122-131, 2016 Nov.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The tyrocidines and analogues are cyclic decapeptides produced by Brevibacillus parabrevis with a conserved sequence of cyclo(D-Phe -Pro -X -x -Asn -Gln -X -Val -X -Leu ) with Trp /Phe in the aromatic dipeptide unit, Lys /Orn as their cationic residue and Tyr (tyrocidines), Trp (tryptocidines) or Phe (phenicidines) in position 7. Previous studies indicated they have a broad antifungal spectrum with the peptides containing a Tyr residue in position 7 being more active than those with a Phe or Trp residue in this position. Detailed analysis of antifungal inhibition parameters revealed that Phe -D-Phe in the aromatic dipeptide unit lead to more consistent activity against the three filamentous fungi in this study. These peptides exhibited high membrane activity and fast leakage kinetics against model membranes emulating fungal membranes, with selectivity towards ergosterol containing membranes. More fluid membranes and doping of liposomes with the sphingolipid, glucosylceramide, led to a decreased permeabilising activity. Peptide-induced uptake of membrane impermeable dyes was observed in hyphae of both Fusarium solani and Botrytis cinerea, with uptake more pronounced at the hyphal growth tips that are known to contain ergosterol-sphigolipid rich lipid rafts. Tyrocidine interaction with these rafts may lead to the previously observed fungal hyperbranching. However, the leakage of model membranes and Bot. cinerea did not correlate directly with the antifungal inhibition parameters, indicating another target or mode of action. Proteinase K treatment of target fungi had a minimal influence or even improved the tyrocidine activity, ruling out a mannoprotein target in the fungal cell wall. ß-glucanase treatment of Bot. cinerea did not significantly affect the tyrocidine activity, but there was a significant loss in activity towards the ß-glucanase treated F. solani. This study showed the tyrocidine antifungal membrane activity is selective towards ergosterol and possibly lipid rafts, but also point to additional targets such as the cell wall ß-glucans that could modulate their activity.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Membrana Celular/efeitos dos fármacos
Fungos/efeitos dos fármacos
Plantas/microbiologia
Tirocidina/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antifúngicos/química
Membrana Celular/química
Membrana Celular/metabolismo
Permeabilidade da Membrana Celular/efeitos dos fármacos
Parede Celular/química
Parede Celular/efeitos dos fármacos
Parede Celular/metabolismo
Ergosterol/química
Ergosterol/metabolismo
Fungos/química
Fungos/metabolismo
Glucosilceramidas/química
Glucosilceramidas/metabolismo
Hifas/química
Hifas/efeitos dos fármacos
Hifas/metabolismo
Cinética
Bicamadas Lipídicas/química
Bicamadas Lipídicas/metabolismo
Microscopia de Fluorescência
Oligopeptídeos/farmacologia
Peptídeos Cíclicos/farmacologia
Tirocidina/química
beta-Glucanas/química
beta-Glucanas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Glucosylceramides); 0 (Lipid Bilayers); 0 (Oligopeptides); 0 (Peptides, Cyclic); 0 (Tyrocidine); 0 (beta-Glucans); Z30RAY509F (Ergosterol)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160623
[St] Status:MEDLINE


  2 / 86 MEDLINE  
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[PMID]:26175103
[Au] Autor:Walsh CT
[Ad] Endereço:ChEM-H, Stanford University, Stanford, CA 94305, USA.
[Ti] Título:Insights into the chemical logic and enzymatic machinery of NRPS assembly lines.
[So] Source:Nat Prod Rep;33(2):127-35, 2016 Feb.
[Is] ISSN:1460-4752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Appreciation that some cyclic peptide antibiotics such as gramicidin S and tyrocidine were nonribosomally synthesized has been known for 50 years. The past two decades of research including advances in bacterial genetics, genomics, protein biochemistry and mass spectrometry have codified the principles of assembly line enzymology for hundreds of nonribosomal peptides and in parallel for thousands of polyketides. The advances in understanding the strategies used for chain initiation, elongation and termination from these assembly lines have revitalized natural product biosynthetic communities.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Produtos Biológicos/síntese química
Gramicidina/síntese química
Peptídeo Sintases/metabolismo
Peptídeos Cíclicos/síntese química
Policetídeos/química
Tirocidina/síntese química
[Mh] Termos MeSH secundário: Bactérias/metabolismo
Produtos Biológicos/química
Gramicidina/química
Estrutura Molecular
Peptídeos Cíclicos/química
Tirocidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biological Products); 0 (Peptides, Cyclic); 0 (Polyketides); 0 (Tyrocidine); 1405-97-6 (Gramicidin); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160204
[Lr] Data última revisão:
160204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150716
[St] Status:MEDLINE
[do] DOI:10.1039/c5np00035a


  3 / 86 MEDLINE  
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[PMID]:25900908
[Au] Autor:Zou Y; Zhao Q; Zhang C; Wang L; Li W; Li X; Wu Q; Hu H
[Ad] Endereço:Department of Organic Chemistry, School of Pharmacy, Second Military Medical University, Shanghai, 200433, China.
[Ti] Título:Synthesis and antibacterial activities of novel tyrocidine A glycosylated derivatives towards multidrug-resistant pathogens.
[So] Source:J Pept Sci;21(7):586-92, 2015 Jul.
[Is] ISSN:1099-1387
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycosylation can have a multifaceted impact on the properties and functions of peptides and plays a critical role in interacting with or binding to the target molecules. Herein, based on the previously reported method for macrocyclic glycopeptide synthesis, two series of tyrocidine A glycosylated derivatives (1a-f and 2a-f) were synthesized and evaluated for their antibacterial activities to further study the structure and activity relationships (SAR). Biological studies showed that the synthetic glycosylated derivatives had good antibacterial activities towards methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus. SAR studies based on various glycans and linkages were used to enhance the biochemical profile, resulting in the identification of several potent antibiotics, such as 1f, with a great improved therapeutic index than tyrocidine A.
[Mh] Termos MeSH primário: Antibacterianos/síntese química
Farmacorresistência Bacteriana Múltipla/efeitos dos fármacos
Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos
Tirocidina/análogos & derivados
Enterococos Resistentes à Vancomicina/efeitos dos fármacos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antibacterianos/farmacologia
Glicosilação
Staphylococcus aureus Resistente à Meticilina/crescimento & desenvolvimento
Testes de Sensibilidade Microbiana
Dados de Sequência Molecular
Estrutura Molecular
Relação Estrutura-Atividade
Tirocidina/síntese química
Tirocidina/farmacologia
Enterococos Resistentes à Vancomicina/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Tyrocidine)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150623
[Lr] Data última revisão:
150623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150423
[St] Status:MEDLINE
[do] DOI:10.1002/psc.2774


  4 / 86 MEDLINE  
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[PMID]:24996824
[Au] Autor:Troskie AM; de Beer A; Vosloo JA; Jacobs K; Rautenbach M
[Ad] Endereço:BIOPEP Peptide Group, Department of Biochemistry, University of Stellenbosch, Private Bag X1, Matieland 7600, South Africa.
[Ti] Título:Inhibition of agronomically relevant fungal phytopathogens by tyrocidines, cyclic antimicrobial peptides isolated from Bacillus aneurinolyticus.
[So] Source:Microbiology;160(Pt 9):2089-101, 2014 Sep.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The tyrocidines, a complex of analogous cyclic decapeptides produced by Bacillus aneurinolyticus, exhibited noteworthy activity against a range of phytopathogenic fungi, including Fusarium verticillioides, Fusarium solani and Botrytis cinerea. The activity of the tyrocidine peptide complex (Trc mixture) and purified tyrocidines exhibited minimum inhibition concentrations below 13 µg ml(-1) (~10 µM) and was significantly more potent than that of the commercial imidazole fungicide, bifonazole. Although the tyrocidines' activity was negatively influenced by the presence of Ca(2+), it remained unaffected by the presence of Mg(2+), Na(+) and K(+). Microscopic analysis revealed significant impact on the morphology of F. solani and Bot. cinerea including retarded germination and hyperbranching of hyphae. Studies with membrane-impermeable dyes, SYTOX green and propidium iodide suggested that the main mode of action of tyrocidines involves the disruption of fungal membrane integrity. Because of the tyrocidines' broad spectrum and potent antifungal activity, possible multiple targets reducing the risk of overt resistance and general salt tolerance, they are promising candidates that warrant further investigation as bio-fungicides.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Bacillales/metabolismo
Botrytis/efeitos dos fármacos
Fusarium/efeitos dos fármacos
Tirocidina/farmacologia
[Mh] Termos MeSH secundário: Botrytis/citologia
Membrana Celular/efeitos dos fármacos
Membrana Celular/fisiologia
Fusarium/citologia
Testes de Sensibilidade Microbiana
Microscopia
Permeabilidade/efeitos dos fármacos
Tirocidina/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Tyrocidine)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:140902
[Lr] Data última revisão:
140902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140706
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.078840-0


  5 / 86 MEDLINE  
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[PMID]:24766734
[Au] Autor:Leussa AN; Rautenbach M
[Ad] Endereço:BIOPEP Peptide Group, Department of Biochemistry, University of Stellenbosch, Private Bag X1, Matieland, 7602, Stellenbosch, South Africa.
[Ti] Título:Detailed SAR and PCA of the tyrocidines and analogues towards leucocin A-sensitive and leucocin A-resistant Listeria monocytogenes.
[So] Source:Chem Biol Drug Des;84(5):543-57, 2014 Nov.
[Is] ISSN:1747-0285
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The tyrocidines, antimicrobial cyclic decapeptides from Bacillus aneurinolyticus, have potent activity with drug/disinfectant potential, specifically against Listeria monocytogenes. The tyrocidine activity is dependent on an amphipathic balance. Structure-activity relationship (SAR) analysis combined with principal component analysis showed the best activity correlation with hydropathy and solvent accessible volume (hydrophobicity parameters), Mr and molecular volume (steric/size parameters), coupled with rigid sequence and charge prerequisites. For potent activity against L. monocytogenes strains, there is a prerequisite for a Tyr or Phe in the (W/F)(w/f)NQ(Y/F/W) sequence of the variable pentapeptide and ornithine (Orn, O) as cationic residue in the conserved V(K/O)LfP pentapeptide, particularly with Trp in the aromatic dipeptide moiety of the variable pentapeptide. The roles of Trp and Orn in the tyrocidines were confirmed with most active peptide, tyrocidine B (TrcB) containing Orn and a Trp-D-Phe in the aromatic dipeptide moiety. However, a novel analogue with a trimethylated ornithine and Phe-D-Phe showed an activity rivalling that of TrcB. Our results emphasized that activity is dictated by interplay between the character of the aromatic residues in the variable pentapeptide and the cationic residue. Any residue change resulting in tighter membrane/cell wall interaction is likely to trap tyrocidines and impede their mechanism of action.
[Mh] Termos MeSH primário: Anti-Infecciosos/química
Anti-Infecciosos/farmacologia
Listeria monocytogenes/efeitos dos fármacos
Relação Estrutura-Atividade
Tirocidina/química
[Mh] Termos MeSH secundário: Bacteriocinas/farmacologia
Relação Dose-Resposta a Droga
Farmacorresistência Bacteriana/efeitos dos fármacos
Testes de Sensibilidade Microbiana
Análise de Componente Principal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Bacteriocins); 0 (Tyrocidine); 0 (leucocin A-QU, Leuconostoc pseudomesenteroides); 145170-92-9 (leucocin A-UAL 187)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:141013
[Lr] Data última revisão:
141013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140429
[St] Status:MEDLINE
[do] DOI:10.1111/cbdd.12344


  6 / 86 MEDLINE  
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[PMID]:24752256
[Au] Autor:Troskie AM; Rautenbach M; Delattin N; Vosloo JA; Dathe M; Cammue BP; Thevissen K
[Ad] Endereço:BIOPEP Peptide Group, Department of Biochemistry, Science Faculty, University of Stellenbosch, Stellenbosch, South Africa.
[Ti] Título:Synergistic activity of the tyrocidines, antimicrobial cyclodecapeptides from Bacillus aneurinolyticus, with amphotericin B and caspofungin against Candida albicans biofilms.
[So] Source:Antimicrob Agents Chemother;58(7):3697-707, 2014 Jul.
[Is] ISSN:1098-6596
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tyrocidines are cationic cyclodecapeptides from Bacillus aneurinolyticus that are characterized by potent antibacterial and antimalarial activities. In this study, we show that various tyrocidines have significant activity against planktonic Candida albicans in the low-micromolar range. These tyrocidines also prevented C. albicans biofilm formation in vitro. Studies with the membrane-impermeable dye propidium iodide showed that the tyrocidines disrupt the membrane integrity of mature C. albicans biofilm cells. This membrane activity correlated with the permeabilization and rapid lysis of model fungal membranes containing phosphatidylcholine and ergosterol (70:30 ratio) induced by the tyrocidines. The tyrocidines exhibited pronounced synergistic biofilm-eradicating activity in combination with two key antifungal drugs, amphotericin B and caspofungin. Using a Caenorhabditis elegans infection model, we found that tyrocidine A potentiated the activity of caspofungin. Therefore, tyrocidines are promising candidates for further research as antifungal drugs and as agents for combinatorial treatment.
[Mh] Termos MeSH primário: Anfotericina B/farmacologia
Antifúngicos/farmacologia
Bacillus/química
Candida albicans/efeitos dos fármacos
Equinocandinas/farmacologia
Peptídeos/farmacologia
Tirocidina/farmacologia
[Mh] Termos MeSH secundário: Animais
Biofilmes/efeitos dos fármacos
Caenorhabditis elegans/microbiologia
Candidíase/tratamento farmacológico
Candidíase/microbiologia
Permeabilidade da Membrana Celular
Sinergismo Farmacológico
Lipopeptídeos
Testes de Sensibilidade Microbiana
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Echinocandins); 0 (Lipopeptides); 0 (Peptides); 0 (Reactive Oxygen Species); 0 (Tyrocidine); 7XU7A7DROE (Amphotericin B); F0XDI6ZL63 (caspofungin)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140423
[St] Status:MEDLINE
[do] DOI:10.1128/AAC.02381-14


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[PMID]:24530898
[Au] Autor:Loll PJ; Upton EC; Nahoum V; Economou NJ; Cocklin S
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USA. Electronic address: ploll@drexelmed.edu.
[Ti] Título:The high resolution structure of tyrocidine A reveals an amphipathic dimer.
[So] Source:Biochim Biophys Acta;1838(5):1199-207, 2014 May.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Tyrocidine A, one of the first antibiotics ever to be discovered, is a cyclic decapeptide that binds to membranes of target bacteria, disrupting their integrity. It is active against a broad spectrum of Gram-positive organisms, and has recently engendered interest as a potential scaffold for the development of new drugs to combat antibiotic-resistant pathogens. We present here the X-ray crystal structure of tyrocidine A at a resolution of 0.95Å. The structure reveals that tyrocidine forms an intimate and highly amphipathic homodimer made up of four beta strands that associate into a single, highly curved antiparallel beta sheet. We used surface plasmon resonance and potassium efflux assays to demonstrate that tyrocidine binds tightly to mimetics of bacterial membranes with an apparent dissociation constant (K(D)) of 10 µM, and efficiently permeabilizes bacterial cells at concentrations equal to and below the K(D). Using variant forms of tyrocidine in which the fluorescent probe p-cyano-phenylalanine had been inserted on either the polar or apolar face of the molecule, we performed fluorescence quenching experiments, using both water-soluble and membrane-embedded quenchers. The quenching results, together with the structure, strongly support a membrane association model in which the convex, apolar face of tyrocidine's beta sheet is oriented toward the membrane interior, while the concave, polar face is presented to the aqueous phase.
[Mh] Termos MeSH primário: Tirocidina/química
[Mh] Termos MeSH secundário: Antibacterianos/química
Antibacterianos/farmacologia
Bactérias/efeitos dos fármacos
Membrana Celular/efeitos dos fármacos
Cristalização/métodos
Cristalografia por Raios X
Modelos Moleculares
Estrutura Secundária de Proteína
Tirocidina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Tyrocidine)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140218
[St] Status:MEDLINE


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[PMID]:24151934
[Au] Autor:Munyuki G; Jackson GE; Venter GA; Kövér KE; Szilágyi L; Rautenbach M; Spathelf BM; Bhattacharya B; van der Spoel D
[Ad] Endereço:Department of Chemistry, University of Cape Town , P Bag X3, Rondebosch, Cape Town, South Africa 7701.
[Ti] Título:ß-sheet structures and dimer models of the two major tyrocidines, antimicrobial peptides from Bacillus aneurinolyticus.
[So] Source:Biochemistry;52(44):7798-806, 2013 Nov 05.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The structures of two major tyrocidines, antibiotic peptides from Bacillus aneurinolyticus, in an aqueous environment were studied using nuclear magnetic resonance spectroscopy, restrained molecular dynamics (MD), circular dichroism, and mass spectrometry. TrcA and TrcC formed ß-structures in an aqueous environment. Hydrophobic and hydrophilic residues were not totally separated into nonpolar and polar faces of the peptides, indicating that tyrocidines have low amphipathicity. In all the ß-structures, residues Trp(4)/Phe(4) and Orn(9) were on the same face. The ability of the peptides to form dimers in aqueous environment was studied by replica exchange MD simulations. Both peptides readily dimerize, and predominant complex structures were characterized through cluster analysis. The peptides formed dimers by either associating sideways or stacking on top of each other. Dimers formed through sideways association were mainly stabilized by hydrogen bonding, while the other dimers were stabilized by hydrophobic interactions. The ability of tyrocidine peptides to form different types of dimers with different orientations suggests that they can form larger aggregates, as well.
[Mh] Termos MeSH primário: Antibacterianos/química
Bacillus/metabolismo
Tirocidina/química
[Mh] Termos MeSH secundário: Antibacterianos/metabolismo
Bacillus/química
Dimerização
Espectroscopia de Ressonância Magnética
Simulação de Dinâmica Molecular
Estrutura Secundária de Proteína
Tirocidina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Tyrocidine)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:131105
[Lr] Data última revisão:
131105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131025
[St] Status:MEDLINE
[do] DOI:10.1021/bi401363m


  9 / 86 MEDLINE  
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[PMID]:23729217
[Au] Autor:Walsh CT; O'Brien RV; Khosla C
[Ad] Endereço:Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
[Ti] Título:Nonproteinogenic amino acid building blocks for nonribosomal peptide and hybrid polyketide scaffolds.
[So] Source:Angew Chem Int Ed Engl;52(28):7098-124, 2013 Jul 08.
[Is] ISSN:1521-3773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Freestanding nonproteinogenic amino acids have long been recognized for their antimetabolite properties and tendency to be uncovered to reactive functionalities by the catalytic action of target enzymes. By installing them regiospecifically into biogenic peptides and proteins, it may be possible to usher a new era at the interface between small molecule and large molecule medicinal chemistry. Site-selective protein functionalization offers uniquely attractive strategies for posttranslational modification of proteins. Last, but not least, many of the amino acids not selected by nature for protein incorporation offer rich architectural possibilities in the context of ribosomally derived polypeptides. This Review summarizes the biosynthetic routes to and metabolic logic for the major classes of the noncanonical amino acid building blocks that end up in both nonribosomal peptide frameworks and in hybrid nonribosomal peptide-polyketide scaffolds.
[Mh] Termos MeSH primário: Aminoácidos/química
Peptídeos/química
Policetídeos/química
[Mh] Termos MeSH secundário: Aminoácidos/biossíntese
Compostos Macrocíclicos/química
Compostos Macrocíclicos/metabolismo
Peptídeos/metabolismo
Policetídeos/metabolismo
Proteínas/química
Proteínas/metabolismo
Sirolimo/química
Sirolimo/metabolismo
Tirocidina/biossíntese
Tirocidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Amino Acids); 0 (Macrocyclic Compounds); 0 (Peptides); 0 (Polyketides); 0 (Proteins); 0 (Tyrocidine); W36ZG6FT64 (Sirolimus)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130605
[St] Status:MEDLINE
[do] DOI:10.1002/anie.201208344


  10 / 86 MEDLINE  
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[PMID]:23046554
[Au] Autor:Ando M; Kamei R; Komagoe K; Inoue T; Yamada K; Katsu T
[Ad] Endereço:Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Kita, Okayama, Japan.
[Ti] Título:In situ potentiometric method to evaluate bacterial outer membrane-permeabilizing ability of drugs: example using antiprotozoal diamidines.
[So] Source:J Microbiol Methods;91(3):497-500, 2012 Dec.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We introduced a new assay system, combining tyrocidine A and a K(+)-selective electrode, to evaluate the bacterial outer membrane-permeabilizing ability of drugs. Tyrocidine A, in the presence of an outer membrane permeabilizer, increased the permeability to K(+) of the cytoplasmic membrane of Escherichia coli, because this antibiotic could markedly increase the permeability of phospholipid layers constituting the cytoplasmic membrane, while it acted weakly on the outer membrane. Hence, the novel function of agents increasing the permeability of the outer membrane could be examined directly by monitoring the tyrocidine A-induced leakage of K(+) from the bacterial cytoplasm using a K(+)-selective electrode. We found that antiprotozoal diamidines, such as diminazene, pentamidine, and 4',6-diamidino-2-phenylindole (DAPI), can increase the permeability of the bacterial outer membrane and appropriate lipophilicity is important for diamidines to permeabilize the outer membrane.
[Mh] Termos MeSH primário: Antiprotozoários/farmacologia
Permeabilidade da Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Escherichia coli/metabolismo
Pentamidina/metabolismo
Potenciometria/métodos
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Transporte Biológico/efeitos dos fármacos
Membrana Celular/química
Membrana Celular/efeitos dos fármacos
Escherichia coli/química
Escherichia coli/efeitos dos fármacos
Interações Hidrofóbicas e Hidrofílicas
Potássio/metabolismo
Tirocidina/farmacologia
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antiprotozoal Agents); 0 (Tyrocidine); 673LC5J4LQ (Pentamidine); RWP5GA015D (Potassium)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121011
[St] Status:MEDLINE



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