Proteins enforce structural integrity via their polypeptide """"""""backbone"""""""", which serves as a matrix controlling the access to and the orientation of residues in the active site. Duplication of these features in model complexes using simple carboxylate ligands is often difficult due to their kinetic lability and large variety of binding modes to metal ions. This research proposal describes a series of cyclophanes with two craboxylate moieties positioned in an endo-fashion and oriented to bind two metal ions in a bidentate bridging mode. It is proposed that such a series of cyclophane dicarboxylate ligands would provide a pocket that would sterically protect the dimetallic core and offer increased kinetic stability via the macrocyclic effect. The role of these ligands is to afford dimetallic models for a variety of biologically relevant metalloproteins.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM020679-01
Application #
6208987
Study Section
Metallobiochemistry Study Section (BMT)
Program Officer
Marino, Pamela
Project Start
2000-09-01
Project End
Budget Start
2000-09-01
Budget End
2001-08-31
Support Year
1
Fiscal Year
2000
Total Cost
$32,416
Indirect Cost
Name
Massachusetts Institute of Technology
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139