Archetypal tryptophan-rich antimicrobial peptides: properties and applications
| Autor: | Enzo A. Palombo, Mrinal Bhave, Nadin Shagaghi, Andrew H. A. Clayton |
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| Rok vydání: | 2016 |
| Předmět: |
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Molecular 0301 basic medicine Physiology 030106 microbiology Antimicrobial peptides Applied Microbiology and Biotechnology Microbiology 03 medical and health sciences chemistry.chemical_compound Anti-Infective Agents Lactoferricin Animals Humans biology Tryptophan Drug Resistance Microbial General Medicine Antimicrobial biology.organism_classification Lactoferrin 030104 developmental biology Biochemistry chemistry Indolicidin Nucleic acid Oligopeptides Bacteria Antimicrobial Cationic Peptides Biotechnology |
| Zdroj: | World Journal of Microbiology and Biotechnology. 32 |
| ISSN: | 1573-0972 0959-3993 |
| DOI: | 10.1007/s11274-015-1986-z |
| Popis: | Drug-resistant microorganisms ('superbugs') present a serious challenge to the success of antimicrobial treatments. Subsequently, there is a crucial need for novel bio-control agents. Many antimicrobial peptides (AMPs) show a broad-spectrum activity against bacteria, fungi or viruses and are strong candidates to complement or substitute current antimicrobial agents. Some AMPs are also effective against protozoa or cancer cells. The tryptophan (Trp)-rich peptides (TRPs) are a subset of AMPs that display potent antimicrobial activity, credited to the unique biochemical properties of tryptophan that allow it to insert into biological membranes. Further, many Trp-rich AMPs cross bacterial membranes without compromising their integrity and act intracellularly, suggesting interactions with nucleic acids and enzymes. In this work, we overview some archetypal TRPs derived from natural sources, i.e., indolicidin, tritrpticin and lactoferricin, summarising their biochemical properties, structures, antimicrobial activities, mechanistic studies and potential applications. |
| Databáze: | OpenAIRE |
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