Evaluation of an Antimicrobial L-Amino Acid Oxidase and Peptide Derivatives from Bothropoides mattogrosensis Pitviper Venom
| Autor: | William F. Porto, Ludovico Migliolo, Hortência H. S. Holanda, Diego Garces Gomes, Susana Elisa Moreno, Carmel S. Ramos, Carla L. Batista, Octavio L. Franco, Osmar N. Silva, Brunna Mary Okubo, Simoni Campos Dias |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Proteomics Gram-negative bacteria Protein Conformation medicine.drug_class Science Molecular Sequence Data Static Electricity Antibiotics Drug Evaluation Preclinical Microbial Sensitivity Tests In Vitro Techniques Gram-Positive Bacteria L-Amino Acid Oxidase L-amino-acid oxidase Biochemistry Microbiology Crotalid Venoms Gram-Negative Bacteria Viperidae medicine Animals Humans Amino Acid Sequence Biology Peptide sequence Multidisciplinary Sequence Homology Amino Acid biology Proteins biology.organism_classification Antimicrobial Peptide Fragments Medicine Bothrops Antibacterial activity Bacteria Antimicrobial Cationic Peptides Research Article Biotechnology |
| Zdroj: | PLoS ONE PLoS ONE, Vol 7, Iss 3, p e33639 (2012) |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0033639 |
| Popis: | Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a multifaceted mixture of peptides, proteins and inorganic components. L-amino oxidase (LAO) is a multifunctional enzyme that is able to develop different activities including antibacterial activity. In this study a novel LAO from Bothrops mattogrosensis (BmLAO) was isolated and biochemically characterized. Partial enzyme sequence showed full identity to Bothrops pauloensis LAO. Moreover, LAO here isolated showed remarkable antibacterial activity against Gram-positive and -negative bacteria, clearly suggesting a secondary protective function. Otherwise, no cytotoxic activities against macrophages and erythrocytes were observed. Finally, some LAO fragments (BmLAO-f1, BmLAO-f2 and BmLAO-f3) were synthesized and further evaluated, also showing enhanced antimicrobial activity. Peptide fragments, which are the key residues involved in antimicrobial activity, were also structurally studied by using theoretical models. The fragments reported here may be promising candidates in the rational design of new antibiotics that could be used to control resistant microorganisms. |
| Databáze: | OpenAIRE |
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