2. Academic Validation
  3. Amphiphilic Polyamine α-Synuclein Aggregation Inhibitors from the Sponge Aaptos lobata

Amphiphilic Polyamine α-Synuclein Aggregation Inhibitors from the Sponge Aaptos lobata

  • J Nat Prod. 2023 Mar 24;86(3):475-481. doi: 10.1021/acs.jnatprod.2c01125.
Tanja M Voser 1 2,  Joshua B Hayton 1 2,  Dale W Prebble 1 2,  Ju Jin 3,  Gary Grant 3,  Merrick G Ekins 4,  Anthony R Carroll 1 2
Affiliations

Affiliations

  • 1 School of Environment and Science, Griffith University (Gold Coast Campus), Parklands Drive, Southport, QLD 4222, Australia.
  • 2 Griffith Institute for Drug Discovery, Griffith University (Brisbane Innovation Park), Don Young Road, Nathan, QLD 4111, Australia.
  • 3 School of Pharmacy and Medical Sciences, Griffith University, Parklands Drive, Southport, QLD 4222, Australia.
  • 4 Queensland Museum, South Brisbane BC, QLD 4101, Australia.
PMID: 36795859 DOI: 10.1021/acs.jnatprod.2c01125
Abstract

Bioassay-guided investigation of the Sponge Aaptos lobata resulted in the isolation and identification of two new amphiphilic polyamines, aaptolobamines A (1) and B (2). Their structures were determined through analysis of NMR and MS data. MS analysis also indicated that A. lobata contained a complex mixture of aaptolobamine homologues. Both aaptolobamines A (1) and B (2) show broad bioactivity, including cytotoxicity against Cancer cell lines, moderate antimicrobial activity against a methicillin-resistant strain of Staphylococcus aureus, and weak activity against a Pseudomonas aeruginosa strain. The mixtures of aaptolobamine homologues were shown to contain compounds that bind to the Parkinson's disease associated amyloid protein α-synuclein and inhibit its aggregation.

Figures