Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties

Marine Drugs

Susan Matthew²  Ranjala Ratnayake²  Mikel A. Becerro¹  Raphael Ritson-Williams¹  Valerie J. Paul¹ 

[1] Smithsonian Marine Station, 701 Seaway Drive, Fort Pierce, FL 34949, USA; E-Mails:;Department of Medicinal Chemistry, University of Florida, 1600 SW Archer Road, Gainesville, FL 32610, USA; E-Mails:

关键词: cyanobacteria;    Lyngbya;    antifeedant activity;    serine protease inhibitors;    cyclodepsipeptides;   

DOI  :  10.3390/md8061803

来源: mdpi

【 摘 要 】

Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further chemical and NMR spectroscopic investigation led us to isolate and structurally characterize a new serine protease inhibitor 1 that is formally derived from an intramolecular condensation of largamide D (2). The cyclization resulted in diminished activity, but to different extents against two serine proteases tested. This finding suggests that cyanobacteria can endogenously modulate the activity of their protease inhibitors.

【 授权许可】

CC BY   
© 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland