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MOLECULAR RECOGNITION AT THE PROTEIN-HYDROXYAPATITE INTERFACE

¹ Departments of Bioengineering, Box 351721, and ² Chemistry, Box 351700, University of Washington, Seattle, WA 98195;

^* corresponding authors, stayton{at}u.washington.edu and drobny{at}u.washington.edu

Proteins found in mineralized tissues act as nature’s crystal engineers, where they play a key role in promoting or inhibiting the growth of minerals such as hydroxyapatite (bones/teeth) and calcium oxalate (kidney stones). Despite their importance in hard-tissue formation and remodeling, and in pathological processes such as stone formation and arterial calcification, there is little known of the protein structure-function relationships that govern hard-tissue engineering. Here we review early studies that have utilized solid-state NMR (ssNMR) techniques to provide in situ secondary-structure determination of statherin and statherin peptides on their biologically relevant hydroxyapatite (HAP) surfaces. In addition to direct structural study, molecular dynamics studies have provided considerable insight into the protein-binding footprint on hydroxyapatite. The molecular insight provided by these studies has also led to the design of biomimetic fusion peptides that utilize nature’s crystal-recognition mechanism to display accessible and dynamic bioactive sequences from the HAP surface. These peptides selectively engage adhesion receptors and direct specific outside-in signaling pathway activation in osteoblast-like cells.

Key words. Biomineralization, molecular recognition, hydroxyapatite, biomaterials

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