This proposal represents a request for an RSDA to support my career development in the area of opioid peptide biosynthesis. Active opioid peptides, like other neuropeptides and hormones, are formed through the action of intracellular processing enzymes which cleave and then modify precursor proteins. This proposal addresses the specific proteolytic mechanisms resulting in opioid peptide formation. Since the biochemical basis for the addictive properties of opiate drugs may relate to deficiencies in the biosynthetic capacity for opiold peptides, a thorough understanding of key regulatory enzymes has potential relevance to the rational design of enzyme-based drugs serving as therapeutic agents in opiate addiction. My short-term goals are to describe the interaction of the newly discovered PC processing enzymes with proenkephalin, both in vitro and in cells. My long-term objectives are to understand the cell biology, biochemistry, and turnover of opioid peptides.

Agency
National Institute of Health (NIH)
Institute
National Institute on Drug Abuse (NIDA)
Type
Research Scientist Development Award - Research (K02)
Project #
5K02DA000204-03
Application #
2116136
Study Section
Drug Abuse Biomedical Research Review Committee (DABR)
Project Start
1993-09-30
Project End
1998-08-31
Budget Start
1995-09-01
Budget End
1996-08-31
Support Year
3
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Louisiana State University Hsc New Orleans
Department
Biochemistry
Type
Schools of Dentistry
DUNS #
782627814
City
New Orleans
State
LA
Country
United States
Zip Code
70112
Apletalina, E V; Juliano, M A; Juliano, L et al. (2000) Structure-function analysis of the 7B2 CT peptide. Biochem Biophys Res Commun 267:940-2