Imaging the osteocalcin binding site on collagen

CHED 857

Piper Klemm, piper.klemm@trincoll.edu1, Ann Lehman, ann.lehman@trincoll.edu2, and Richard V. Prigodich, rprig@trincoll.edu1. (1) Chemistry Department, Trinity College, 300 Summit Street, Hartford, CT 06106, (2) Electron Microscopy Facility, Trinity College, 300 Summit Street, Hartford, CT 06106
Type I collagen is a fibrillar collagen that is an important component of skin, bone, tendon and ligament. Osteocalcin is a major component of bone tissue and has a role in bone formation and remodeling. Osteocalcin binds hydroxyapatite and collagen. The osteocalcin binding site on collagen is unknown. To identify this site, type I tropocollagen was imaged using rotary shadowing and transmission electron microscopy. Tropocollagen at a concentration of 3 µg/mL was sprayed onto freshly cleaved mica. The mica was vacuum evaporated, and at a rotary angle of six degrees, was coated with carbon and platinum. Decorin, which binds 25 nm from the tropocollagen carboxy-terminus, was used as a marker on the tropocollagen molecules to determine directionality on the tropocollagen molecule.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008