Work

Structure–Activity Relationships of Anabaenopeptins as Carboxypeptidase and Phosphatase Inhibitors

Year: 2026

Type: article

Abstract: High Resolution Image Download MS PowerPoint Slide Anabaenopeptins are a family of cyanobacterial cyclic peptides that display potent enzyme inhibition, particularly against carboxypeptidases A and B, as well as the serine/threonine phosphatases PP1 and PP2A. Defined by a 19-membered macrocyclic ring and a ureido-linked exocyclic amino acid, these compounds vary considerably in their amino acid composition, influencing both potency and selectivity. This review compiles published IC 50 values for natural and synthetic anabaenopeptins, organizing them by enzyme target, and highlighting recurring structural motifs that drive inhibitory activity. Through this comparative analysis, we identify emerging trends in structure–activity relationships and underscore gaps in assay standardization and structural validation. These insights provide a critical foundation for advancing the biological evaluation of anabaenopeptins as environmental contaminants, mechanistic probes, and candidate scaffolds for therapeutic development.

Source: ACS Chemical Biology

DOI: 10.1021/acschembio.5c00791

Authors: Megan L. Quandt, Judy Westrick, Jeremy J. Kodanko

Institution: Wayne State University

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Pharmacology

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: Wayne State University, National Institutes of Health, National Institute of Environmental Health Sciences