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[PMID]:28817271
[Au] Autor:Schmidt M; Bast LK; Lanfer F; Richter L; Hennes E; Seymen R; Krumm C; Tiller JC
[Ad] Endereço:Biomaterials and Polymer Science, Department of Bio- and Chemical Engineering, TU Dortmund , Emil-Figge-Straße 66, 44227 Dortmund, Germany.
[Ti] Título:Poly(2-oxazoline)-Antibiotic Conjugates with Penicillins.
[So] Source:Bioconjug Chem;28(9):2440-2451, 2017 Sep 20.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The conjugation of antibiotics with polymers is rarely done, but it might be a promising alternative to low-molecular-weight derivatization. The two penicillins penicillin G (PenG) and penicillin V (PenV) were attached to the end groups of different water-soluble poly(2-oxazoline)s (POx) via their carboxylic acid function. This ester group was shown to be more stable against hydrolysis than the ß-lactam ring of the penicillins. The conjugates are still antimicrobially active and up to 20 times more stable against penicillinase catalyzed hydrolysis. The antibiotic activity of the conjugates against Staphylococcus aureus in the presence of penicillinase is up to 350 times higher compared with the free antibiotics. Conjugates with a second antimicrobial function, a dodecyltrimethylammonium group (DDA-X), at the starting end of the PenG and PenV POx conjugates are more antimicrobially active than the conjugates without DDA-X and show high activity in the presence of penicillinase. For example, the conjugates DDA-X-PEtOx-PenG and DDA-X-PEtOx-PenV are 200 to 350 times more active against S. aureus in the presence of penicillinase and almost as effective as the penicillinase stable cloxacollin (Clox) under these conditions. These conjugates show even greater activity compared to cloxacollin without this enzyme present. Further, both conjugates kill Escherichia coli more effectively than PenG and Clox.
[Mh] Termos MeSH primário: Antibacterianos/química
Antibacterianos/farmacologia
Bactérias/efeitos dos fármacos
Oxazóis/química
Oxazóis/farmacologia
Penicilinas/química
Penicilinas/farmacologia
[Mh] Termos MeSH secundário: Antibacterianos/síntese química
Bactérias/enzimologia
Infecções Bacterianas/tratamento farmacológico
Estabilidade de Medicamentos
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Infecções por Escherichia coli/tratamento farmacológico
Seres Humanos
Hidrólise
Oxazóis/síntese química
Penicilinase/metabolismo
Penicilinas/síntese química
Infecções Estafilocócicas/tratamento farmacológico
Staphylococcus aureus/efeitos dos fármacos
Staphylococcus aureus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Oxazoles); 0 (Penicillins); 0 (poly(2-oxazoline)); EC 3.5.2.- (Penicillinase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00424


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[PMID]:28143659
[Au] Autor:Kmiecik N; Zymanczyk-Duda E
[Ad] Endereço:Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland. Electronic address: natalia.kmiecik@pwr.edu.pl.
[Ti] Título:Enantio convergent biotransformation of O,O-dimethyl-4-oxoazetidin-2-ylphosphonate using fungal cells of Penicillium minioluteum and purified enzymes.
[So] Source:Bioorg Chem;71:81-85, 2017 Apr.
[Is] ISSN:1090-2120
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This report presents the bioconversion of O,O-dimethyl-4-oxoazetidin-2-ylphosphonate 1 performed in two ways: with the enzymatic system of P. minioluteum and with the application of purified enzymes: penicillinase and two proteases of different origin. Recorded NMR spectra allowed confirming the reaction progress and also postulating possible mechanism of conversion. The path of bioconversion was defined as enantio convergent process for both modes of applied biocatalysts. This means that kinetically driven resolution of racemic mixture of the substrate leads to the one enantiomer of the product. The bioconversion started from ester bond hydrolysis (equally in both enantiomers) with the conversion degree from 30% (whole-cell) to 35% (isolated enzymes) and with the production of optically pure monoester (compound 2; 100% of e.e). For whole-cell bioprocess it was the initiative step for the enantioselective amide bond hydrolysis, what resulted in synthesis of desired product 3-amino-3-phosphonopropanoic acid 4. However, the most effective enzymatic hydrolysis of ester bond performed with penicillinase from Enterobacter cloacae led only to the monoester product 2.
[Mh] Termos MeSH primário: Bacillus licheniformis/enzimologia
Enterobacter cloacae/enzimologia
Organofosfonatos/metabolismo
Penicillium/metabolismo
Rhizopus/enzimologia
[Mh] Termos MeSH secundário: Biotransformação
Hidrólise
Cinética
Penicilinase/metabolismo
Penicillium/citologia
Penicillium/enzimologia
Peptídeo Hidrolases/metabolismo
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organophosphonates); EC 3.4.- (Peptide Hydrolases); EC 3.5.2.- (Penicillinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE


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[PMID]:28069883
[Au] Autor:Hombach M; Weissert C; Senn MM; Zbinden R
[Ad] Endereço:Institut für Medizinische Mikrobiologie, Universität Zürich, Zürich 8006, Schweiz.
[Ti] Título:Comparison of phenotypic methods for the detection of penicillinase in Staphylococcus aureus and proposal of a practical diagnostic approach.
[So] Source:J Antimicrob Chemother;72(4):1089-1093, 2017 Apr 01.
[Is] ISSN:1460-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Objectives: Disc diffusion is a cost-efficient, low-complexity, reliable method for detection of blaZ -mediated benzylpenicillin resistance in Staphylococcus aureus if the zone edge is inspected. EUCAST breakpoints cannot fully separate ß-lactamase-positive from ß-lactamase-negative strains, and EUCAST recommends the zone edge test. Literature on nitrocefin-based testing and the zone edge test is scarce with wide variations in reported assay performance. Methods: This study compared two different nitrocefin-based commercial and in-house tests and the EUCAST-based zone edge test for penicillinase detection in S. aureus applying a PCR-based gold standard. Results: In total, 215 non-duplicate clinical S. aureus isolates were included in the study, of which 127 (59.1%) did not harbour a blaZ gene, whereas 88 (40.9%) were blaZ positive. This study showed that for blaZ detection the zone edge test is more sensitive (96.6%) than nitrocefin tests independent of using nitrocefin discs (87.5% sensitivity) or solution (89.8% sensitivity), and that the significant inter-person variations of the zone edge test are probably related to the training level of the individual investigators (individual sensitivity ranging from 68.2% to 96.6%, specificity ranging from 89.8% to 100%). Conclusions: In addition to continued and strict training of investigators, we propose mandatory checking of benzylpenicillin zone edges, particularly in an investigation zone from 26 to 30 mm, which can result in improved specificity/positive predictive value of the zone edge test (from 98.4% to 100%) but retains the high sensitivity/negative predictive value of the method.
[Mh] Termos MeSH primário: Testes de Sensibilidade a Antimicrobianos por Disco-Difusão/métodos
Penicilinase/análise
Staphylococcus aureus/enzimologia
[Mh] Termos MeSH secundário: Sensibilidade e Especificidade
[Pt] Tipo de publicação:COMPARATIVE STUDY; EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.5.2.- (Penicillinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.1093/jac/dkw521


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[PMID]:27956418
[Au] Autor:Bonnin RA; Didi J; Ergani A; Lima S; Naas T
[Ad] Endereço:EA7361 "Structure, Dynamic, Function and Expression of Broad Spectrum ß-Lactamases," Université Paris Sud, Université Paris Saclay, LabEx Lermit, Faculty of Medicine, Le Kremlin-Bicêtre, France.
[Ti] Título:Chromosome-Encoded Broad-Spectrum Ambler Class A ß-Lactamase RUB-1 from Serratia rubidaea.
[So] Source:Antimicrob Agents Chemother;61(2), 2017 Feb.
[Is] ISSN:1098-6596
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Whole-genome sequencing of Serratia rubidaea CIP 103234 revealed a chromosomally located Ambler class A ß-lactamase gene. The gene was cloned, and the ß-lactamase, RUB-1, was characterized. RUB-1 displayed 74% and 73% amino acid sequence identity with the GIL-1 and TEM-1 penicillinases, respectively, and its substrate profile was similar to that of the latter ß-lactamases. Analysis by 5' rapid amplification of cDNA ends revealed promoter sequences highly divergent from the Escherichia coli σ consensus sequence. This work further illustrates the heterogeneity of ß-lactamases among Serratia spp.
[Mh] Termos MeSH primário: Cromossomos Bacterianos/genética
Serratia/enzimologia
Serratia/metabolismo
beta-Lactamases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
DNA Complementar/genética
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Escherichia coli/metabolismo
Testes de Sensibilidade Microbiana
Penicilinase/genética
Penicilinase/metabolismo
Serratia/efeitos dos fármacos
beta-Lactamases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Complementary); EC 3.5.2.- (Penicillinase); EC 3.5.2.6 (beta-Lactamases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE


  5 / 2189 MEDLINE  
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[PMID]:28146620
[Au] Autor:Mlynarczyk-Bonikowska B; Kujawa M; Mynarczyk G; Malejczyk M; Majewski S
[Ti] Título:Dominating types of penicillinase-plasmids in Neisseria gonorrhoeae strains isolated in 2010-2012 in Warsaw.
[So] Source:Med Dosw Mikrobiol;68(1):34-38, 2016.
[Is] ISSN:0025-8601
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: The reason of Neisseria gonorrhoeae resistance to penicillin is often production of TEM beta-lactamases encoded by plasmids. The most common types of the plasmid are Africa, Asia and Toronto/Rio. Another reason of resistance can be mutations in bacterial chromosome. The aim of the study was to investigate the types of plasmids occurring in in Neisseria gonorrhoeae strains isolated in 2010-2012 in Warsaw. MATERIAL AND METHODS: From 218 isolated in 2010, 2011 and at the beginning of 2012 from patients of Medical University in Warsaw we selected 12 strains producing beta- lactamase (penicillinase producing N. gonorrhoeae, PPNG). d B-tests to investigate bacterial sensitivity to penicillin and cefiriaxon. The types of plasmids were determined with PCR. RESULTS: The Beta-lactamases were encoded by Toronto/Rio (41,7%), Asia (33,3%) and Africa (25,0%) plasmids. All the strains were resistant to penicillin (MIC 2-8 mg/L) and sensitive to ceftriaxon (MIC 0,004-0,032 mg/L). CONCLUSIONS: All of the investigate PPNG strains were penicillin resistant and ceftriaxon sensitive. The dominating type of the penicillinase plasmid was Toronto/Rio.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Neisseria gonorrhoeae/isolamento & purificação
Resistência às Penicilinas/genética
Penicilinase/genética
Plasmídeos
[Mh] Termos MeSH secundário: Gonorreia/diagnóstico
Gonorreia/enzimologia
Gonorreia/genética
Seres Humanos
Neisseria gonorrhoeae/enzimologia
Neisseria gonorrhoeae/genética
Polônia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.5.2.- (Penicillinase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170317
[Lr] Data última revisão:
170317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE


  6 / 2189 MEDLINE  
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[PMID]:27570824
[Au] Autor:Balmer TS
[Ad] Endereço:Grass Laboratory, Marine Biological Laboratory , Woods Hole, Massachusetts 02543.
[Ti] Título:Perineuronal Nets Enhance the Excitability of Fast-Spiking Neurons.
[So] Source:eNeuro;3(4), 2016 Jul-Aug.
[Is] ISSN:2373-2822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Perineuronal nets (PNNs) are specialized complexes of extracellular matrix molecules that surround the somata of fast-spiking neurons throughout the vertebrate brain. PNNs are particularly prevalent throughout the auditory brainstem, which transmits signals with high speed and precision. It is unknown whether PNNs contribute to the fast-spiking ability of the neurons they surround. Whole-cell recordings were made from medial nucleus of the trapezoid body (MNTB) principal neurons in acute brain slices from postnatal day 21 (P21) to P27 mice. PNNs were degraded by incubating slices in chondroitinase ABC (ChABC) and were compared to slices that were treated with a control enzyme (penicillinase). ChABC treatment did not affect the ability of MNTB neurons to fire at up to 1000 Hz when driven by current pulses. However, f-I (frequency-intensity) curves constructed by injecting Gaussian white noise currents superimposed on DC current steps showed that ChABC treatment reduced the gain of spike output. An increase in spike threshold may have contributed to this effect, which is consistent with the observation that spikes in ChABC-treated cells were delayed relative to control-treated cells. In addition, parvalbumin-expressing fast-spiking cortical neurons in >P70 slices that were treated with ChABC also had reduced excitability and gain. The development of PNNs around somata of fast-spiking neurons may be essential for fast and precise sensory transmission and synaptic inhibition in the brain.
[Mh] Termos MeSH primário: Matriz Extracelular/metabolismo
Neurônios/fisiologia
Complexo Olivar Superior/fisiologia
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Análise de Variância
Animais
Fármacos do Sistema Nervoso Central/farmacologia
Condroitina ABC Liase/farmacologia
Matriz Extracelular/efeitos dos fármacos
Feminino
Imuno-Histoquímica
Masculino
Camundongos Endogâmicos C57BL
Microscopia de Fluorescência
Neurônios/efeitos dos fármacos
Técnicas de Patch-Clamp
Penicilinase/farmacologia
Complexo Olivar Superior/efeitos dos fármacos
Técnicas de Cultura de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Central Nervous System Agents); EC 3.5.2.- (Penicillinase); EC 4.2.2.20 (Chondroitin ABC Lyase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160830
[St] Status:MEDLINE


  7 / 2189 MEDLINE  
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[PMID]:27108966
[Au] Autor:Mazuet C; Yoon EJ; Boyer S; Pignier S; Blanc T; Doehring I; Meziane-Cherif D; Dumant-Forest C; Sautereau J; Legeay C; Bouvet P; Bouchier C; Quijano-Roy S; Pestel-Caron M; Courvalin P; Popoff MR
[Ad] Endereço:Unité des Bactéries anaérobies et Toxines, Institut Pasteur, Paris, France.
[Ti] Título:A penicillin- and metronidazole-resistant Clostridium botulinum strain responsible for an infant botulism case.
[So] Source:Clin Microbiol Infect;22(7):644.e7-644.e12, 2016 Jul.
[Is] ISSN:1469-0691
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The clinical course of a case of infant botulism was characterized by several relapses despite therapy with amoxicillin and metronidazole. Botulism was confirmed by identification of botulinum toxin and Clostridium botulinum in stools. A C. botulinum A2 strain resistant to penicillins and with heterogeneous resistance to metronidazole was isolated from stool samples up to 110 days after onset. Antibiotic susceptibility was tested by disc agar diffusion and MICs were determined by Etest. Whole genome sequencing allowed detection of a gene cluster composed of blaCBP for a novel penicillinase, blaI for a regulator, and blaR1 for a membrane-bound penicillin receptor in the chromosome of the C. botulinum isolate. The purified recombinant penicillinase was assayed. Resistance to ß-lactams was in agreement with the kinetic parameters of the enzyme. In addition, the ß-lactamase gene cluster was found in three C. botulinum genomes in databanks and in two of 62 genomes of our collection, all the strains belonging to group I C. botulinum. This is the first report of a C. botulinum isolate resistant to penicillins. This stresses the importance of antibiotic susceptibility testing for adequate therapy of botulism.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Botulismo/diagnóstico
Botulismo/microbiologia
Clostridium botulinum/efeitos dos fármacos
Clostridium botulinum/isolamento & purificação
Farmacorresistência Bacteriana
Metronidazol/farmacologia
Penicilinas/farmacologia
[Mh] Termos MeSH secundário: Toxinas Botulínicas/análise
Botulismo/tratamento farmacológico
Botulismo/patologia
Fezes/química
Fezes/microbiologia
Feminino
Genes Reguladores
Genoma Bacteriano
Seres Humanos
Lactente
Proteínas de Membrana Transportadoras/genética
Testes de Sensibilidade Microbiana
Família Multigênica
Penicilinase/genética
Penicilinase/isolamento & purificação
Penicilinase/metabolismo
Análise de Sequência de DNA
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Membrane Transport Proteins); 0 (Penicillins); 140QMO216E (Metronidazole); EC 3.4.24.69 (Botulinum Toxins); EC 3.5.2.- (Penicillinase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170126
[Lr] Data última revisão:
170126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160426
[St] Status:MEDLINE


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[PMID]:26597276
[Au] Autor:Mlynarczyk-Bonikowska B; Kujawa M; Mlynarczyk G; Malejczyk M; Majewski S
[Ad] Endereço:Department of Sexually Transmitted Diseases Diagnostics, Medical University of Warsaw, Koszykowa 82A, 02-008, Warsaw, Poland.
[Ti] Título:Susceptibility to ceftriaxone and occurrence of penicillinase plasmids in Neisseria gonorrhoeae strains isolated in Poland in 2012-2013.
[So] Source:Folia Microbiol (Praha);61(4):269-73, 2016 Jul.
[Is] ISSN:1874-9356
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent years have seen rising concerns over increasing antibiotic resistance of the gonorrhea-causing bacterium, Neisseria gonorrhoeae. This is especially true for third-generation cephalosporins, which are currently recommended for the treatment of such infections. Therefore, susceptibility to these antibiotics should be monitored internationally to the greatest extent possible. The susceptibility of N. gonorrhoeae strains to ceftriaxone and penicillin, as well as production of beta-lactamase by the Cefinase test was determined. Moreover, the presence and type of penicillinase plasmids were determined by PCR. All strains were susceptible to ceftriaxone, the minimal inhibitory concentration (MIC) values ranged from 0.002 to 0.125 mg/L; MIC50 was =0.016 mg/L and MIC90 was =0.064 mg/L. As much as 7.7 % of the strains demonstrated ceftriaxone MIC of 0.125 mg/L. For penicillin, the MICs ranged from 0.064 to 32 mg/L; MIC50 was =0.5 mg/L and MIC90 was =4 mg/L. It was shown that only 1.5 % of the strains were sensitive to penicillin according to The European Committee on Antimicrobial Susceptibility Testing (EUCAST). Among the penicillin-resistant strains, six (30.0 %) produced penicillinase. The MICs of penicillin were substantially higher for penicillinase-producing than for penicillin-resistant, penicillinase-negative strains. MICs of ceftriaxone for penicillinase-producing strains were low (0.002-0.016 mg/L). Three of the penicillinase-producing strains possessed plasmids of African type (50 %) and three Toronto/Rio type (50 %). An increase of the proportion of beta-lactamase-positive strains in the last years as well as emergence of strains with elevated MIC of ceftriaxone indicate a need to constantly monitor N. gonorrhoeae strains for their susceptibility to beta-lactam antibiotics, as well as for their ability to produce beta-lactamases.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Ceftriaxona/farmacologia
Neisseria gonorrhoeae/efeitos dos fármacos
Neisseria gonorrhoeae/isolamento & purificação
Penicilinase/secreção
Plasmídeos/análise
[Mh] Termos MeSH secundário: Cefalosporinas/metabolismo
Feminino
Gonorreia/microbiologia
Seres Humanos
Masculino
Testes de Sensibilidade Microbiana
Neisseria gonorrhoeae/genética
Penicilinas/farmacologia
Polônia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Cephalosporins); 0 (Penicillins); 75J73V1629 (Ceftriaxone); EC 3.5.2.- (Penicillinase); EWP54G0J8F (nitrocefin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151125
[St] Status:MEDLINE
[do] DOI:10.1007/s12223-015-0434-7


  9 / 2189 MEDLINE  
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[PMID]:26521981
[Au] Autor:Zou Q; Yang KL
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, National University of Singapore, 4 Engineering Drive 4, Singapore, 117585, Singapore.
[Ti] Título:Identification of peptide inhibitors of penicillinase using a phage display library.
[So] Source:Anal Biochem;494:4-9, 2016 Feb 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There is a constant need to identify novel inhibitors to combat ß-lactamase-mediated antibiotic resistance. In this study, we identify three penicillinase-binding peptides, P1 (DHIHRSYRGEFD), P2 (NIYTTPWGSNWS), and P3 (SHSLPASADLRR), using a phage display library. Surface plasmon resonance (SPR) is utilized for quantitative determination and comparison of the binding specificity of selected peptides to penicillinase. An SPR biosensor functionalized with P3-GGGC (SHSLPASADLRRGGGC) is developed for detection of penicillinase with excellent sensitivity (15.8 RU nM(-1)) and binding affinity (KD = 0.56 nM). To determine if peptides can be good inhibitors for penicillinase, these peptides are mixed with penicillinase and their inhibition efficiency is determined by measuring the hydrolysis of substrate penicillin G using UV-vis spectrophotometry. Peptide P2 (NIYTTPWGSNWS) is found to be a promising penicillinase inhibitor with a Ki of 9.22 µM and a Ki' of 33.12 µM, suggesting that the inhibition mechanism is a mixed pattern. This peptide inhibitor (P2) can be used as a lead compound to identify more potent small molecule inhibitors for penicillinase. This study offers a potential approach to both detection of ß-lactamases and development of novel inhibitors of ß-lactamases.
[Mh] Termos MeSH primário: Penicilinase/metabolismo
Espectrofotometria Ultravioleta
Inibidores de beta-Lactamases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Hidrólise
Cinética
Penicilina G/metabolismo
Penicilinase/química
Biblioteca de Peptídeos
Ligação Proteica
Especificidade por Substrato
Ressonância de Plasmônio de Superfície
Inibidores de beta-Lactamases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptide Library); 0 (beta-Lactamase Inhibitors); EC 3.5.2.- (Penicillinase); Q42T66VG0C (Penicillin G)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151228
[Lr] Data última revisão:
151228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151103
[St] Status:MEDLINE


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[PMID]:26023821
[Au] Autor:Zhao Y; Li G
[Ad] Endereço:a College of Bioengineering , Henan University of Technology , Zhengzhou , China.
[Ti] Título:Detection of Penicillinase in Milk by Sandwich ELISA Based Polyclonal and Monoclonal Antibody.
[So] Source:J Immunoassay Immunochem;37(1):80-9, 2016.
[Is] ISSN:1532-4230
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A sandwich ELISA has been developed using polyclonal and monoclonal antibody for the determination of penicillinase in milk. For this purpose, specific polyclonal and monoclonal antibodies against penicillinase were generated and characterized. Using penicillinase standards prepared from 1-128 ng/mL, the method indicated that the detection limit of the sandwich ELISA, as measured in an ELISA plate reader, was as low as 0.86 ng/mL of penicillinase. For determine the accuracy, raw milk containing 2, 8, 32, and 64 ng/mL of penicillinase were tested by sandwich ELISA. Recoveries were from 93-97.5%, and the coefficient of variation [CV (%)] were from 5.55-8.38%. For interassay reproducibility, recoveries were from 89.5-95.1%, the coefficient of variation [CV (%)] were from 5.26-9.58%. This sandwich ELISA provides a useful screening method for quantitative detection of penicillinase in milk.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/química
Proteínas de Bactérias/análise
Ensaio de Imunoadsorção Enzimática/métodos
Leite/química
Penicilinase/análise
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/biossíntese
Calibragem
Ensaio de Imunoadsorção Enzimática/normas
Feminino
Análise de Alimentos
Hibridomas/química
Hibridomas/imunologia
Limite de Detecção
Masculino
Camundongos Endogâmicos BALB C
Coelhos
Padrões de Referência
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Bacterial Proteins); EC 3.5.2.- (Penicillinase)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150530
[St] Status:MEDLINE
[do] DOI:10.1080/15321819.2015.1050108



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