Topic
Antimicrobial peptides
About: Antimicrobial peptides is a research topic. Over the lifetime, 10645 publications have been published within this topic receiving 507688 citations. The topic is also known as: host defense peptide & antimicrobial protein.
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TL;DR: Data revised here indicate that large-scale production of AMPs can be obtained using biotechnological tools, and the products may be applied in the pharmaceutical industry as well as in agribusiness.
136 citations
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TL;DR: In this paper, Hen's egg white lysozyme (HEWL) was hydrolysed with Alcalase and fractionated by cation-exchange chromatography.
136 citations
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TL;DR: This review focuses on the similarities and differences in the mode of action and target cell specificity of two families of small peptides: the naturally occurring temporins from the skin of amphibia and the engineered ultrashort lipopeptides.
Abstract: Due to the rapid emergence of resistant microbes to the currently available antibiotics, cationic antimicrobial peptides have attracted considerable interest as a possible new generation of anti-infective compounds. However, low cost development for therapeutic or industrial purposes requires, among other properties, that the peptides will be small and with simple structure. Therefore, considerable research has been devoted to optimizing peptide length combined with a simple design. This review focuses on the similarities and differences in the mode of action and target cell specificity of two families of small peptides: the naturally occurring temporins from the skin of amphibia and the engineered ultrashort lipopeptides. We will also discuss the finding that acylation of cationic peptides results in molecules with a more potent spectrum of activity and a higher resistance to proteolytic degradation. Conjugation of fatty acids to linear native peptide sequences is a powerful strategy to engineer novel successful anti-infective drugs.
136 citations
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TL;DR: Characterization of GPNP provides new insight into structural features which may be essential for the broad-spectrum antimicrobial activities of defensins, and is homologous to a recently characterized family of antimicrobial peptides isolated from rabbit and human neutrophils.
Abstract: A broad-spectrum antimicrobial peptide present in guinea pig neutrophils was isolated, characterized biochemically, and assessed for microbicidal range and potency in vitro. The guinea pig neutrophil peptide (GPNP) was purified to homogeneity from a granule-rich subcellular fraction of peritoneal exudate neutrophils by gel filtration and reversed-phase high-performance liquid chromatography. GPNP was microbicidal for selected bacterial, fungal, and viral test organisms at concentrations in the microgram per milliliter range. Composition and primary structure analyses revealed that GPNP was homologous to a recently characterized family of antimicrobial peptides, termed defensins, isolated from rabbit and human neutrophils. The entire amino acid sequence of GPNP was determined, revealing that 8 of 31 residues were among those invariant in six rabbit and three human defensin peptides. The conserved sequence included six disulfide-linked cysteine residues, a common structural feature of defensins. The sequence of GPNP also included three nonconservative substitutions in positions otherwise invariant in the human and rabbit peptides. Characterization of GPNP provides new insight into structural features which may be essential for the broad-spectrum antimicrobial activities of defensins. Images
136 citations
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TL;DR: A major role of mono-divalent cations and serum proteins on inhibition of hBD-3 antibacterial properties is demonstrated and a relative lack in sensitivity of the bactericidal activity of this peptide to trypsin andtrypsin-like proteases is indicated.
136 citations