Saturday, October 27, 2007
Ballroom Posters (Greenville Hyatt Regency Hotel)
806

Ferric-Complexes of Bryostatin: Site Verses Territorial Binding

Justin Smith1, Giso Abadi2, Lyn Noble2, Paul Groundwater2, and Thomas Manning1. (1) Chemistry, Valdosta State University, Valdosta, GA, (2) Sunderland University, Sunderland, United Kingdom

Bryostatin-1 (C47H68O17) is a marine natural product that is produced by marine bacteria. The macrolid is held together by a key ester bond that forms a bryophan ring. Past experimental work in this group has shown that bryostatin binds the ferric species and computational studies indicate the structure is an octahedral geometry with six Fe-O bonds that range in length from 1.9 to 2.3 Angstroms. This data suggested the function of bryostatin as well as a host of the MNP's maybe siderophores in the marine environment. In this computational study (semiempirical, PM3) we show that there are over 100 potential variations in which six of bryostatins' seventeen oxygen atoms bind the Fe(III) cation with an octahedral geometry. We also show over 100 variations in which there are five Fe-O bonds and the sixth site is occupied by water or a hydroxide ion. This study shows that the stability of the Fe(III)-bryostatin complex in solution does not come from a single set of Fe-O bonds but rather the trivalent cation is held in place by a dynamic interaction with a number of bryostatins oxygen atoms.