Grayson H. Snyder

Physical Biochemistry: Protein Engineering

Associate Professor

Ph.D 1975 Harvard University
Postdoctoral work 1975 Stanford University
Assistant Professor 1977;
Associate Professor 1984 University at Buffalo

Address Information

Grayson H. Snyder
Department of Biological Sciences
343 Cooke Hall
State University of New York at Buffalo
Buffalo, NY 14260

(716) 645-2363 ext: 212

To send e-mail: gsnyder@acsu.buffalo.edu

RESEARCH SUMMARY

The structures of many naturally occurring enzyme inhibitors, toxins, and hormones include a small rigid tightlycrosslinked disulfiderich polypeptide mainframe. By chemical synthesis of mutants, computer modeling, nmr spectroscopy, and analysis of disulfide pair formation, we are determining factors responsible for the folding of conotoxin (a snail toxin), apamin (a bee venom toxin), and endothelin (a human hormone). The latter two of these small disulfide rich proteins have four cysteines at identical positions in the primary sequence, but those cysteines pair with each other to make different sets of disulfides. The specific aim of this research is to develop a rational approach for engineering and designing new proteins capable of regulating human diseaserelated processes.

The envelope protein of the AIDS virus binds to receptors on T4 immune cells. Infected humans develop antibodies against an immunodominant decoy region of the envelope protein, instead of against the functional receptorbinding region. We are expressing recombinant fragments of the AIDS envelope protein in genetically engineered E.Coli bacteria. Since the decoy region is absent in our constructions, the fragment might elicit medically useful antibodies directed against the receptor binding region. The specific aim of this research is to develop novel protein molecules for use in developing drugs against AIDS.

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