I am a physician-scientist with a Ph.D. in nucleic acid biochemistry who is within a year of completing an anatomical pathology residency at the Brigham and Women's Hospital. My immediate goal is to resume research, after a three-year absence from the laboratory, to learn the fields of protein biochemistry and stucture in the laboratory of Dr. Blacklow at the Brigham and Women's Hospital, Department of Pathology. This will give me the training necessary to pursue my long term goal of translational research in protein pharmacology. The overall goal of these studies is to test the feasibility of developing D-peptide drug candidates using the method of mirror image phage display (Schumacher et al., 1996; Forster, 1996; Fig. 1).
The specific aims of this proposal are: 1. To establish that the D-enantiomer of a selected L-peptide ligand of D-interleukin-8 binds specifically and with measurable affinity to L-interleukin-8. 2. To investigate the specific molecular interactions responsible for the measured affinity and specificity of the D-peptide for the interleukin-8 target. 3. To apply this strategy for drug discovery to other potential therapeutic targets, including the gp41 subunit of the HIV envelope glycoprotein and the breast-cancer specific, cell- surface glycoprotein MUC1.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Clinical Investigator Award (CIA) (K08)
Project #
5K08CA080833-04
Application #
6513487
Study Section
Subcommittee G - Education (NCI)
Program Officer
Lohrey, Nancy
Project Start
1999-06-22
Project End
2004-05-31
Budget Start
2002-06-01
Budget End
2003-05-31
Support Year
4
Fiscal Year
2002
Total Cost
$139,320
Indirect Cost
Name
Brigham and Women's Hospital
Department
Type
DUNS #
071723621
City
Boston
State
MA
Country
United States
Zip Code
02115
Tan, Zhongping; Blacklow, Stephen C; Cornish, Virginia W et al. (2005) De novo genetic codes and pure translation display. Methods 36:279-90
Forster, A C; Weissbach, H; Blacklow, S C (2001) A simplified reconstitution of mRNA-directed peptide synthesis: activity of the epsilon enhancer and an unnatural amino acid. Anal Biochem 297:60-70