Serine protease inhibitors from the Floridian marine cyanobacterium Lyngbya confervoides

S. Matthew; C. Ross; V. J. Paul; H. Luesch

doi:10.1055/s-0028-1084380

Planta Medica, Table of Contents

Serine protease inhibitors from the Floridian marine cyanobacterium Lyngbya confervoides

S Matthew ¹, C Ross ²^,³, VJ Paul ², H Luesch ¹

¹Department of Medicinal Chemistry, University of Florida, 1600 SW Archer Road, Gainesville, Florida 32610, USA
²Smithsonian Marine Station, 701 Seaway Drive, Fort Pierce, Florida 34949, USA.
³University of North Florida, 1 UNF Drive, Jacksonville, FL 32224, USA

Abstract

Marine cyanobacteria are prolific sources of bioactive secondary metabolites with intriguing structures and, consequently, have tremendous potential to yield small molecule therapeutic agents and biological probes. A collection of the cyanobacterium Lyngbya confervoides from Ft. Lauderdale (Florida, USA) afforded four new serine protease inhibitors (1–4), consisting of multiple modified amino acid moieties [1–3], along with a cyclic pentapeptide having a rare ureido linkage (5) [3]. The planar structures of (1–5) were determined by extensive spectroscopic analysis and the absolute configurations established using advanced Marfey's method and chiral HPLC analysis of chemical degradation products.

Acknowledgements: Florida Sea Grant College Program for financial support; AMRIS (McKnight Brain Institute, University of Florida) and NHMFL External User Program (NSF) for NMR infrastructure and instrument time.

References: 1. Matthew, S. et al. (2007)J. Nat. Prod. 70:124.

2. Taori, K. et al. (2007)J. Nat. Prod. 70:1593.

3. Matthew, S. et al. (2008) http://www.sciencedirect.com/science? _ob=RedirectURL&_method=gejLink&_linkType=general&_cdi=5289&_issn=00404020&_targetURL =http%3A%2F%2Fwww.elsevier.com%2Flocate%2Fissn%2F00404020&_acct=C000050221&_version=1&_userid=10&md5=4ccaf6fc027b281239b16e0bb366e62bTetrahedron 64:4081.