- Collection:
- Spelman College Faculty Publications
- Title:
- Antimalarial Peptide and Polyketide Natural Products from the Fijian Marine Cyanobacterium Moorea producens
- Creator:
- Mojib, Nazia, Spelman College
Sweeney-Jones, Anne Marie, Georgia Institute of Technology
Gagaring, Kerstin, Calibr, a division of The Scripps Research Institute
Antonova-Koch, Jenya, Calibr, a division of The Scripps Research Institute
Zhou, Hongyi, Georgia Institute of Technology
Soapi,Katy, University of the South Pacific
Skolnick, Jeffrey, Georgia Institute of Technology
McNamara, Case W., Calibr, a division of The Scripps Research Institute
Kubanek, Julia, Georgia Institute of Technology - Date of Original:
- 2020-03-18
- Subject:
- Spelman College--Faculty
African American scholars
African Americans--Education (Higher)--Georgia
African American universities and colleges--Georgia--Atlanta - Location:
- United States, Georgia, Atlanta Metropolitan Area, 33.8498, 84.4383
- Medium:
- articles
- Type:
- Text
- Format:
- application/pdf
- Description:
- A new cyclic peptide, kakeromamide B (1), and previously described cytotoxic cyanobacterial natural products ulongamide A (2), lyngbyabellin A (3), 18E-lyngbyaloside C (4), and lyngbyaloside (5) were identified from an antimalarial extract of the Fijian marine cyanobacterium Moorea producens. Compounds 1 and 2 exhibited moderate activity against Plasmodium falciparum blood-stages with EC50 values of 0.89 and 0.99 M, respectively, whereas 3 was more potent with an EC50 value of 0.15 nM. Compounds 1, 4, and 5 displayed moderate liver-stage antimalarial activity against P. berghei liver schizonts with EC50 values of 1.1, 0.71, and 0.45 M, respectively. The threading-based computational method FINDSITEcomb2.0 predicted the binding of 1 and 2 to potentially druggable proteins of Plasmodium falciparum, prompting formulation of hypotheses about possible mechanisms of action. Kakeromamide B (1) was predicted to bind to several Plasmodium actin-like proteins and a sortilin protein suggesting possible interference with parasite invasion of host cells. When 1 was tested in a mammalian actin polymerization assay, it stimulated actin polymerization in a dose-dependent manner, suggesting that 1 does, in fact, interact with actin.
- External Identifiers:
- Metadata URL:
- http://hdl.handle.net/20.500.12322/sc.fac.pubs:2022_mojib_nazia
- Rights Holder:
- Spelman College
- Original Collection:
- Marine Drugs
- Holding Institution:
- Spelman College
- Rights:
-
