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ARS Home » Research » Publications at this Location » Publication #72789


item Rothfus, John
item Wolf, Walter

Submitted to: Journal of the American Oil Chemists' Society
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/22/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary: Environmental concerns and the need to reduce dependence on fossil resources call for massive quantities of cheap new materials from agriculture. At the same time, concerns for human safety and health provide opportunity to enhance substantially the value of smaller amounts of existing materials. Both goals require new knowledge of agricultural commodities. This research developed tools for identifying potentially useful polypeptides in seed proteins. The techniques were used to locate a soybean peptide capable of binding aspirin with the same affinity as peptides from serum albumin, the blood protein that transports nutrients and medicines in animals. Future applications of the approach, which simplifies the search for utility in seed proteins, will guide the development of new products.

Technical Abstract: Molecular mechanics energy calculations for computed non-ionized and ionized interactions in vacuo identify two major salicylic acid affinity regions in human serum albumin and a single analogous region in soybean beta-conglycinin. Salicylic acid interactions with 21-residue segments from both proteins suggest redundant binding sites with multiple degrees of faffinity. High-affinity segments incorporate hydrophobic amino acids with combinations or multiple residues of histidine, tryptophan, lysine, or arginine in keeping with a preference of salicylic acid for homopolymers of these acids over other homopolypeptides. Residue spacing also seems important. High affinity is associated with but not imparted by genetic similarity. Profiles from beta-sheet conformations simplify identification of analogous segments.