Improving short antimicrobial peptides despite elusive rules for activity
نویسندگان
چکیده
منابع مشابه
Short cationic antimicrobial peptides interact with ATP.
The mode of action of short, nonhelical antimicrobial peptides is still not well understood. Here we show that these peptides interact with ATP and directly inhibit the actions of certain ATP-dependent enzymes, such as firefly luciferase, DnaK, and DNA polymerase. α-Helical and planar or circular antimicrobial peptides did not show such interaction with ATP.
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Short antimicrobial host-defense peptides represent a possible alternative as lead structures to fight antibiotic resistant bacterial infections. Bac2A is a 12-mer linear variant of the naturally occurring bovine host defense peptide, bactenecin, and demonstrates moderate, broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against the yeast Candida...
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Antimicrobial peptides (AMPs) are membraneactive peptides that serve as promising therapeutic alternatives to antibiotics. Due to their diverse sequences, AMPs are active against a variety of microbes including bacteria, fungi, viruses, and cancer cells. Here, we present the use of machine learning techniques to classify antifungal AMPs from antibacterial AMPs using sequence-derived physico-che...
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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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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2016
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2015.12.013