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1.
Arch Microbiol ; 199(2): 215-222, 2017 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-27671474

RESUMO

Staphylococcus aureus and methicillin-resistant S. aureus are major pathogens. The antimicrobial peptides and essential oils (EOs) display narrow- or broad-spectrum activity against bacteria including these strains. A centralized resource, such as a database, designed specifically for anti-S. aureus/anti-methicillin-resistant S. aureus antimicrobial peptides and EOs is therefore needed to facilitate the comprehensive investigation of their structure/activity associations and combinations. The database ANTISTAPHYBASE is created to facilitate access to important information on antimicrobial peptides and essential peptides against methicillin-resistant S. aureus and S. aureus. At the moment, the database contains 596 sequences of antimicrobial peptides produced by diverse organisms and 287 essential oil records. It permits a quick and easy search of peptides based on their activity as well as their general, physicochemical properties and literature data. These data are very useful to perform further bioinformatic or chemometric analysis and would certainly be useful for the development of new drugs for medical use. The ANTISTAPHYBASE database is freely available at: https://www.antistaphybase.com/ .


Assuntos
Antibacterianos/farmacologia , Bases de Dados de Produtos Farmacêuticos , Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos , Óleos Voláteis/farmacologia , Peptídeos/farmacologia , Staphylococcus aureus/efeitos dos fármacos , Antibacterianos/química , Peptídeos/química , Relação Estrutura-Atividade
2.
Pharm Biol ; 54(12): 3136-3150, 2016 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-27246787

RESUMO

CONTEXT: Drug-resistant bacterial infections cause considerable patient mortality and morbidity. The annual frequency of deaths from methicillin-resistant Staphylococcus aureus (MRSA) has surpassed those caused by human immunodeficiency virus/acquired immune deficiency syndrome. The antimicrobial peptides (AMPs), plant essential oils (EOs) and their combinations have proven to be quite effective in killing a wide selection of bacterial pathogens including MRSA. OBJECTIVES: This review summarizes the studies in the use of AMPs, plant EOs and their combinations for coping with MRSA bacteria, and to formulate new prospects for future studies on this topic. METHODS: The sources of scientific literature such as PubMed, library search, Google Scholar, Science Direct and electronic databases such as 'The Antimicrobial Peptide Database', 'Collection of Anti-Microbial Peptides' and 'YADAMP'. Physicochemical data of anti-MRSA peptides were determined by Scientific DataBase Maker software. RESULTS: Of the 118 peptides, 88 exhibited an activity against MRSA with the highest activity of minimum inhibitory concentration values. Various plant EOs have been effective against MRSA. Remarkably, lemongrass EOs completely inhibited all MRSA growth on the plate. Lemon myrtle, Mountain savory, Cinnamon bark and Melissa EOs showed a significant inhibition. CONCLUSION: Several of these AMPs, EOs and their combinations were effective against MRSA. Their activities have implications for the development of new drugs for medical use.


Assuntos
Anti-Infecciosos/farmacologia , Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos , Óleos Voláteis/farmacologia , Peptídeos/farmacologia , Óleos de Plantas/farmacologia , Sequência de Aminoácidos , Animais , Anti-Infecciosos/isolamento & purificação , Humanos , Staphylococcus aureus Resistente à Meticilina/fisiologia , Testes de Sensibilidade Microbiana , Óleos Voláteis/isolamento & purificação , Peptídeos/genética , Óleos de Plantas/isolamento & purificação
3.
C R Biol ; 332(5): 426-32, 2009 May.
Artigo em Inglês | MEDLINE | ID: mdl-19393974

RESUMO

alpha-Amylase (alpha-1-4 D-glucan glucanohydrolase EC 3.2.1.1) crude extract was obtained from safflower (Carthamus tinctorius L.) cotyledons excised from 5-day-old dark grown seedlings. The enzyme was purified by precipitating the crude extract with ammonium sulphate at 20-60% saturation, and then by subjecting this fraction to affinity chromatography on a beta-cyclodextrin-Sepharose 6B column. The active fraction was dialysed and concentrated. An overall purification of about 131 folds with an activity yield of 81.25% was achieved. The molecular mass of purified enzyme determined by SDS-PAGE was 35 kD. When the purified alpha-amylase was subjected to gel electrophoresis followed by negative staining, only one band of active protein was detected. Its maximal activity was in the pH 6.0 and at a temperature of 55 degrees C. This enzyme was activated by Ca(2+) and inhibited by Fe(2+).


Assuntos
Carthamus tinctorius/enzimologia , Proteínas de Plantas/isolamento & purificação , alfa-Amilases/isolamento & purificação , Carthamus tinctorius/crescimento & desenvolvimento , Cátions Bivalentes/farmacologia , Cromatografia de Afinidade , Cromatografia em Agarose , Germinação , Concentração de Íons de Hidrogênio , Hidrólise , Peso Molecular , Proteínas de Plantas/metabolismo , Sementes/enzimologia , Amido/metabolismo , Temperatura , alfa-Amilases/metabolismo
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