From dolastatin 13 to cyanopeptolins, micropeptins, and lyngbyastatins: the chemical biology of Ahp-cyclodepsipeptides
Abstract
Ahp-cyclodepsipeptides (also known as Ahp-containing cyclodepsipeptides, cyanopeptolins, micropeptins, microginines, and lyngbyastatins, and by many other names) are a natural product family with potent serine protease inhibitory properties.
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Peptides 1-4 and 6 are among the six most potent natural chymotrypsin inhibitors from the compound class of Ahp-cyclodepsipeptides reported to date.
“Peptides 1-4 and 6 are among the six most potent natural chymotrypsin inhibitors from the compound class of Ahp-cyclodepsipeptides that have been reported to date36 (Supplementary Table 5).”
From Native metabolomics identifies the rivulariapeptolide family of protease inhibitors (2022) · cites this paper as [36]
Cyanobacteria are a rich source of highly bioactive natural products, and in particular, protease inhibitors from numerous chemical classes.
“Cyanobacteria are known to be a rich source of highly bioactive natural products32–35, and in particular, protease inhibitors from numerous chemical classes36–41.”
From Native metabolomics identifies the rivulariapeptolide family of protease inhibitors (2022) · cites this paper as [36]
At nanomolar concentration, the compounds' IC50 values show high potency and distinct selectivity compared to other Ahp-cyclodepsipeptides.
“At nanomolar concentration, their IC50 show high potency and exhibits distinct selectivity when compared to other Ahp-cyclodepsipeptides36, Fig. 4 and Supplementary Table 5).”
From Native metabolomics identifies the rivulariapeptolide family of protease inhibitors (2022) · cites this paper as [36]
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Additional file 1 of Distribution and diversity of dimetal-carboxylate halogenases in cyanobacteria
Eusébio, N., Rego, A., Glasser, N. R., Castelo‐Branco, R., Balskus, E. P., & Leão, P. N. (2021) · Figshare · doi:10.6084/m9.figshare.16544304
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- Authors
- Köcher, S., Resch, S., Kessenbrock, T., Schrapp, L., Ehrmann, M., & Kaiser, M.
- Affiliations
- University of Duisburg-Essen (DE)
- Corresponding author
- Kaiser, Markus
- Venue
- Natural Product Reports
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2020
- Volume
- 37
- Issue
- 2
- Pages
- 163-174
- ISSN
- 0265-0568 (ISSN-L)
- 1460-4752
- OpenAlex
- W2970556009
- Cited by
- 41
- References
- 120
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 5 · 2023: 6 · 2022: 6 · 2021: 7 · 2020: 6
- FWCI
- 0.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Natural Product Reports (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (CRC 1093)
- Topics
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Keywords
- cyanopeptolins, nonribosomal peptide biosynthesis, serine protease inhibitors, natural product isolation, structure elucidation, biosynthesis, drug discovery
- MeSH terms
- Biological Products, Oligopeptides, Molecular Structure, Serine Proteinase Inhibitors, Depsipeptides
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