Citation
Weidner, Tobias; Dubey, Manish; Breen, Nicholas F.; Ash, Jason; Baio, J. E.; Jaye, Cherno; Fischer, Daniel A.; Drobny, Gary P.; & Castner, David G. (2012).
Direct Observation of Phenylalanine Orientations in Statherin Bound to Hydroxyapatite Surfaces.
Journal of the American Chemical Society, 134(21), 8750-8753.
Abstract
Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Despite the important role that statherin plays in the regulation of hard tissue formation in humans, the surface recognition mechanisms involved are poorly understood. The protein-surface interaction likely involves very specific contacts between the surface atoms and key protein side chains. This study demonstrates, for the first time, the power of combining near-edge X-ray absorption fine structure (NEXAFS) spectroscopy with element labeling to quantify the orientation of individual side chains. In this work, the 15 amino acid N-terminal binding domain of statherin, SN15, has been adsorbed onto HAP surfaces and the orientations of both phenylalanine rings F7 and F14 have been determined using NEXAFS analysis and fluorine labels at individual phenylalanine sites. The NEXAFS-derived phenylalanine tilt angles have been verified with sum frequency generation spectroscopy.
Reference Type
Journal Article
Secondary Title
Journal of the American Chemical Society
Author(s)
Weidner, TobiasDubey, ManishBreen, Nicholas F.Ash, JasonBaio, J. E.Jaye, ChernoFischer, Daniel A.Drobny, Gary P.Castner, David G.
Year Published
2012
Date Published
1338336000
Volume Number
134
Issue Number
21
Pages
8750-8753
DOI
10.1021/ja301711w
