Cyanobacteria-derived peptide antibiotics discovered since 2000
•Members of cyanobacteria are an important source of peptide products.•Peptides exhibit potent activity against various human and plant pathogens.•Four distinctive categories of cyanobacteria-derived peptides are reported.•Structure-activity relationships and antibiotic activity are discussed.•Pepti...
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Published in | Peptides (New York, N.Y. : 1980) Vol. 107; pp. 17 - 24 |
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Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.09.2018
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Subjects | |
Online Access | Get full text |
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Summary: | •Members of cyanobacteria are an important source of peptide products.•Peptides exhibit potent activity against various human and plant pathogens.•Four distinctive categories of cyanobacteria-derived peptides are reported.•Structure-activity relationships and antibiotic activity are discussed.•Peptides will be explored as novel pharmaceutical drugs or biocontrol agents.
Members of cyanobacteria, including Moorea spp., Okeania spp., Lyngbya spp., Schizothrix spp., Leptolyngbya spp., Microcystis spp., Symploca spp., Hassallia sp., Anabaena spp., Planktothrix sp., Tychonema spp., Oscillatoria spp., Tolypothrix sp., Nostoc sp., and Hapalosiphon sp. produce an enormously diverse range of peptide antibiotics with huge potential as pharmaceutical drugs and biocontrol agents following screening of structural analogues and analysis of structure-activity relationships (SAR). The need for novel antibiotic lead compounds is urgent, and this review summarizes 78 cyanobacteria-derived compounds reported since 2000, including 32 depsipeptides, 18 cyclic lipopeptides, 13 linear lipopeptides, 14 cyclamides, and one typical cyclic peptide. The current and potential therapeutic applications of these peptides are discussed, including for SAR, antituberculotic, antifungal, antibacterial, antiviral, and antiparasitic (anti-plasmodial, antitrypanosomal and antileishmanial) activities. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/j.peptides.2018.08.002 |