نتایج جستجو برای: background antimicrobial peptides with relative length 2
تعداد نتایج: 10328747 فیلتر نتایج به سال:
Abstract Background and purpose: Multiple drug-resistant (MDR) bacterial strains have spread in different parts of hospitals. The aim of this study was to design and synthesize an effective hybrid peptide by combining different parts of two peptides to achieve the highest antibacterial activity and its inhibitory effect against Staphylococcus aureus and Pseudomonas aeruginosa strains. Materia...
abstract background antibiotic resistance makes antimicrobial peptides (amps) agents an alternative for treatment of pathogenic diseases. they are isolated from various animals invertebrates, vertebrates and plants. the present study shows the electrophoretic pattern of protein and peptides from vicia faba seed and reports our first attempt to study the antibacterial activity of vicia faba seed...
BACKGROUND AND AIMS To prevent bacterial adherence and translocation, the colonic mucosa is covered by a protecting mucus layer and the epithelium synthesizes antimicrobial peptides. The present qualitative study investigated the contents and interaction of these peptides in and with rectal mucus. METHODS Rectal mucus extracts were analyzed for antimicrobial activity and screened with matrix-...
Lysosomal cathepsin G from human neutrophils is a chymotrypsin-like protease which also possesses antimicrobial activity. The antimicrobial activity, however, is independent of protease activity, because treatment of this enzyme with the irreversible serine protease inhibitor diisopropylfluorophosphate has no effect on its antimicrobial action. In this study, we found that digestion of cathepsi...
The effectiveness of the antimicrobial peptide maximin-4, the ultrashort peptide H-Orn-Orn-Trp-Trp-NH(2), and the lipopeptide C(12)-Orn-Orn-Trp-Trp-NH(2) in preventing adherence of pathogens to a candidate biomaterial were tested utilizing both matrix- and immersion-loaded poly(2-hydroxyethyl methacrylate) (poly(HEMA)) hydrogels. Antiadherent properties correlated to both the concentration rele...
BACKGROUND Antimicrobial peptides are a promising alternative to conventional antibiotics. Plants are an important source of such peptides; their pharmacological properties are known since antiquity. Access to relevant information, however, is not straightforward, as there are practically no major repositories of experimentally validated and/or predicted plant antimicrobial peptides. PhytAMP is...
UNLABELLED Antimicrobial peptides offer potential as novel therapeutics to combat food spoilage and poisoning caused by pathogenic and nonpathogenic bacteria. Our previous studies identified the peptide human beta-defensin 3 (HBD3) as a potent antimicrobial agent against a wide range of beer-spoiling bacteria. Thus, HBD3 is an excellent candidate for development as an additive to prevent food a...
The primary structures of three human neutrophil antimicrobial peptides (HNP) were determined. The peptides, HNP-1, HNP-2, and HNP-3, which we have termed defensins, were rich in cystine, arginine, and aromatic residues, but were devoid of free sulfhydryl groups and carbohydrate moieties. They were 29-30 residues in length and identical in sequence in all but their amino terminal residues. The ...
Peptidomics and genomics analyses were used to study an anti-infection array of peptides of amphibian skin. 372 cDNA sequences of antimicrobial peptides were characterized from a single individual skin of the frog Odorrana grahami that encode 107 novel antimicrobial peptides. This contribution almost triples the number of currently reported amphibian antimicrobial peptides. The peptides could b...
Translocation of cell-penetrating peptides is often promoted by increased content of arginine or other guanidinium groups. However, relatively little research has considered the role of these functional groups on antimicrobial peptide activity. This study compared the activity of three histone-derived antimicrobial peptides-buforin II, DesHDAP1, and parasin-with variants that contain only lysin...
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