Molecular dynamics based antimicrobial activity descriptors for synthetic cationic peptides
نویسندگان
چکیده
منابع مشابه
Cationic hydrophobic peptides with antimicrobial activity.
The MICs of cationic, hydrophobic peptides of the prototypic sequence KKAAAXAAAAAXAAWAAXAAAKKKK-amide (where X is one of the 20 commonly occurring amino acids) are in a low micromolar range for a panel of gram-negative and gram-positive bacteria, with no or low hemolytic activity against human and rabbit erythrocytes. The peptides are active only when the average segmental hydrophobicity of the...
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Members of the cationic host defense (antimicrobial) peptide family are widely distributed in nature, existing in organisms from insects to plants to mammals and non-mammalian vertebrates. Although many demonstrate direct antimicrobial activity against bacteria, fungi, eukaryotic parasites and/or viruses, it has been established that cationic peptides have a key modulatory role in the innate im...
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OBJECTIVES The present study aimed to investigate the antimicrobial and biofilm inhibition activity of synthetic antimicrobial peptides (AMPs) against microbes such as Enterococcus faecalis, Staphylococcus aureus, and Candida albicans which are involved in endodontic infections. MATERIALS AND METHODS Agar diffusion test was done to determine the activity of peptides. The morphological changes...
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Cationic antimicrobial peptides are important components of the innate immune defences of all species of life. Variants of these natural molecules have a broad range of antibiotic, antifungal, antiviral and anti-endotoxic activity. Two of these cationic peptides have shown signs of efficacy in early clinical trials of oral mucositis and the sterilisation of central venous catheters, respectivel...
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Yeast-like fungi are the most common cause of fungal infections in humans. Actually, in the age of opportunistic infections and increasing resistance, development of modern antifungal agents becomes a very important challenge. This paper describes synthesis and antimicrobial assay of four naturally occurring peptide antibiotics (aurein 1.2, citropin 1.1, temporin A, uperin 3.6) and three chemic...
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ژورنال
عنوان ژورنال: Journal of Chemical Sciences
سال: 2019
ISSN: 0974-3626,0973-7103
DOI: 10.1007/s12039-019-1590-0