Barbara Brodsky
Professor

UMDNJ
Dept. Biochemistry - Room 609
Piscataway. NJ 08854
(732) 235-4048
FAX - 4783
brodsky@umdnj.edu


Structural studies of peptide models of normal collagen and its mutations in diseases


The aims of our laboratory are to use triple-helical peptides of defined sequence to determine how amino acid sequence affects triple-helix structure and recognition. and how alterations in the triple-helix can lead to molecular defects in collagen diseases. Triple-helical domains are important both as a rod-like structural component and for interactions with other molecules in collagens and in a range of host-defense proteins. Synthetic triple-helical peptides have been designed to model biologically important regions of collagen and of the macrophage scavenger receptor. The conformation. stability. dynamics. folding and binding of these peptides are being characterized through the use of circular dichroism spectroscopy. calorimetry. NMR spectroscopy. molecular modeling. and x-ray crystallography. Mutations that interrupt the repeating (Gly-X-Y)n have been found to lead to connective tissue diseases. and studies are being done to investigate the structural basis of these pathological changes. Recent accomplishments include determination of the first crystal structures of a triple-helix. in collaboration with the laboratory of Dr. Helen Berman; the first 2-D NMR structural and dynamics studies on a triple-helix. in collaboration with Dr. Jean Baum; establishment of propensities scales for the collagen triple-helix; and determining the degree of destabilization caused by different Gly mutations in collagen diseases.

View Dr. Brodsky's publications in Pub Med