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Structural diversity of marine cyclic peptides and their molecular mechanisms for anticancer, antibacterial, antifungal, and other clinical applications
- Source :
- Peptides. 95:94-105
- Publication Year :
- 2017
- Publisher :
- Elsevier BV, 2017.
-
Abstract
- Many cyclic peptides and analogues derived from marine sources are known to possess biological properties, including anticancer, antitumor, antibacterial, antifungal, antiparasitic, anti-inflammation, anti-proliferative, anti-hypertensive, cytotoxic, and antibiotic properties. These compounds demonstrate different activities and modes of action according to their structure such as cyclic oligopeptide, cyclic lipopeptide, cyclic glycopeptide and cyclic depsipeptide. The recent advances in application of the above-mentioned cyclic peptides were reported in dolastatins, soblidotin, didemnin B, aplidine, salinosporamide A, kahalalide F and bryostatin 1 and they are currently in clinical trials. These cyclic peptides are possible novel drugs discovered and developed from marine origin. Literature data concerning the potential properties of marine cyclic peptides were reviewed here, and the structural diversity and biological activities of marine cyclic peptides are discussed in relation to the molecular mechanisms of these marine cyclic peptides.
- Subjects :
- 0301 basic medicine
Antifungal
Aquatic Organisms
Bryostatin 1
Physiology
medicine.drug_class
Antiparasitic
Stereochemistry
Biology
Peptides, Cyclic
01 natural sciences
Biochemistry
Didemnin B
03 medical and health sciences
Cellular and Molecular Neuroscience
chemistry.chemical_compound
Endocrinology
Depsipeptides
Neoplasms
medicine
Animals
Humans
chemistry.chemical_classification
Oligopeptide
010405 organic chemistry
Cyclic peptide
Glycopeptide
0104 chemical sciences
030104 developmental biology
chemistry
Hypertension
Oligopeptides
Salinosporamide A
Subjects
Details
- ISSN :
- 01969781
- Volume :
- 95
- Database :
- OpenAIRE
- Journal :
- Peptides
- Accession number :
- edsair.doi.dedup.....bad0c831b7d5b7734df12f3e589bb00c
- Full Text :
- https://doi.org/10.1016/j.peptides.2017.06.002