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Title: MOLECULAR DYNAMICS SIMULATIONS ON THE MYCOTOXIN, FUMONISIN B1

Author
item Momany, Frank
item Dombrink Kurtzman, Mary Ann

Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/7/2000
Publication Date: N/A
Citation: N/A

Interpretive Summary: Understanding molecular mechanisms is a basic requirement for interpreting the significance of test results regarding food safety. Molds capable of producing the mycotoxins, fumonisins, are frequently found in corn worldwide. Fumonisin B1, the most commonly occurring of the fumonisins, has been studied using molecular dynamics simulations to determine the conformation that fumonisin B1 assumes in solution. Results suggested that the structure of fumonisin B1 is relatively extended in solution. The study forms a basis for future research on the structure and function of fumonisin B1, for comparison with fumonisin B1-related forms which occur naturally, and for studies on the possible transmission of fumonisin from plant to feed and food and to animals and humans.

Technical Abstract: The solution conformational properties of the mycotoxin, fumonisin B1, have been studied using molecular dynamics methodology. Fumonisins have been shown to inhibit sphinganine (sphingosine) N-acyltransferase (ceramide synthase) and show a wide range of toxic effects in many animals. This study of the solution properties of fumonisin B1 attempts to add to the structural models necessary for the understanding of the binding and activity properties. The computational method uses a box with periodic boundaries, filled with explicit TIP3P water molecules, the substrate fumonisin B1, and selected counterions for charge neutrality. The starting structure of fumonisin B1 is added to the box by excluding water molecules. The explicit image method using 12 A cutoffs is applied to the system and molecular dynamics carried out on different starting conformations at 300 K in 100 picosecond (ps) steps. Examination of the resulting equilibrated conformations suggests that the structure is relatively extended and that previous computational studies in vacuo, showing a compact folded structure, may not be consistent with the solution structure.