ORGN 654 |
| In previous work, we demonstrated that 4-fluoroproline residues can contribute greatly to the conformational stability of the collagen triple helix, and that this stability arises from stereoelectronic effects that fix the pucker of the pyrrolidine ring and thereby preorganize the backbone properly for triple-helix formation. However, the stability conferred by 4-fluoroprolines to collagen faces an upper limit due to a deleterious steric interaction when they are incorporated in both the Xaa and Yaa positions of a collagen triple helix. We have discovered a reciprocal approach, namely that the steric effect of a 4-methyl group confers stability similar to that from a 4-fluoro group in the opposite configuration. By judicious integration of the steric and stereoelectronic effects we have now prepared collagen triple helices with greater thermal stability than any other collagen peptides of similar size. |
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Asymmetric Reactions, Combinatorial Chemistry, Molecular Recognition and Self-Assembly, Proteins, Peptides, Amino Acids and Enzyme Inhibitors
8:00 PM-10:00 PM, Wednesday, March 28, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Organic Chemistry |