| Literature DB >> 30255943 |
José R Almeida1, Antonio L V Palacios1, Ricardo S P Patiño1, Bruno Mendes2, Cátia A S Teixeira3, Paula Gomes3, Saulo L da Silva4.
Abstract
The emergence of antibiotic resistance drives an essential race against time to reveal new molecular structures capable of addressing this alarming global health problem. Snake venoms are natural catalogs of multifunctional toxins and privileged frameworks, which serve as potential templates for the inspiration of novel treatment strategies for combating antibiotic resistant bacteria. Phospholipases A2 (PLA2 s) are one of the main classes of antibacterial biomolecules, with recognized therapeutic value, found in these valuable secretions. Recently, a number of biomimetic oligopeptides based on small fragments of primary structure from PLA2 toxins has emerged as a meaningful opportunity to overcome multidrug-resistant clinical isolates. Thus, this review will highlight the biochemical and structural properties of antibacterial PLA2 s and peptides thereof, as well as their possible molecular mechanisms of action and key roles in development of effective therapeutic strategies. Chemical strategies possibly useful to convert antibacterial peptides from PLA2 s to efficient drugs will be equally addressed.Entities:
Keywords: antibacterial peptides; antibiotic-resistant bacteria; peptidomimetics; phospholipase A2; snake venom
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Year: 2018 PMID: 30255943 DOI: 10.1002/ddr.21456
Source DB: PubMed Journal: Drug Dev Res ISSN: 0272-4391 Impact factor: 4.360