AVS 46th International Symposium
    Biomaterial Interfaces Group Wednesday Sessions
       Session BI-WeP

Paper BI-WeP16
Determination of Statherin N-Terminal Peptide Conformation on Hydroxyapatite Crystals

Wednesday, October 27, 1999, 5:30 pm, Room 4C

Session: Poster Session
Presenter: W.J. Shaw, University of Washington
Authors: W.J. Shaw, University of Washington
J.R. Long, University of Washington
J.L. Dindot, University of Washington
A.A. Campbell, Battelle, PNNL
P.S. Stayton, University of Washington
G.P. Drobny, University of Washington
Correspondent: Click to Email
The interactions between proteins and inorganic crystals play an important role in the development and growth of hard tissues such as bone and teeth. Although many of these proteins have been studied in the liquid state, there is little information describing molecular recognition at the protein-crystal interface. Here we have used 13C solid state NMR (SSNMR) techniques to investigate the conformation of an N-terminal peptide of salivary statherin both free and adsorbed on hydroxyapatite (HAP) crystals. The torsional angle phi was determined at three positions along the backbone of the N-terminal 15 amino acid peptide fragment (DpSpSEEKFLRRIGRFG) by measuring 13C-13C distances between carbonyls in adjacent amino acids using the Dipolar Recoupling with a Windowless Sequence (DRAWS) technique. The peptides adsorbed to the HAP surface have an average phi of -85 degrees at the N-terminus (SS), -60 degrees in the middle (FL) and -72 degrees at the C-terminus (IG). The SS position corresponds to an angle typically associated with random coil peptides. The FL and IG positions correlate with angles known to be alpha-helical. These angles are approximately the same in the lyopholized peptides implying that secondary structure content of the peptide is retained upon adsorption to the crystal surface.