Structure and Dynamics of Hydrated Statherin on Hydroxyapatite As Determined by Solid-State NMR

Proteins directly control the nucleation and growth of biominerals, but the details of molecular recognition at the protein−biomineral interface remain poorly understood. The elucidation of recognition mechanisms at this interface may provide design principles for advanced materials development in m...

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Bibliographic Details
Published in:Biochemistry (Easton) 2001-12, Vol.40 (51), p.15451-15455
Main Authors: Long, Joanna R, Shaw, Wendy J, Stayton, Patrick S, Drobny, Gary P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Durapatite - chemistry
Humans
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular - methods
Peptide Fragments - chemistry
Protein Structure, Secondary
Protein Structure, Tertiary
Salivary Proteins and Peptides - chemistry
Structure-Activity Relationship
Thermodynamics
Water
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Summary:Proteins directly control the nucleation and growth of biominerals, but the details of molecular recognition at the protein−biomineral interface remain poorly understood. The elucidation of recognition mechanisms at this interface may provide design principles for advanced materials development in medical and ceramic composite technologies. Here, we have used solid-state NMR techniques to provide the first high-resolution structural and dynamic characterization of a hydrated biomineralization protein, salivary statherin, adsorbed to its biologically relevant hydroxyapatite (HAP) surface. Backbone secondary structure for the N-terminal dodecyl region was determined using a combination of homonuclear and heteronuclear dipolar recoupling techniques. Both sets of experiments indicate the N-terminus is α-helical in character with the residues directly binding to the HAP being stabilized in the α-helical conformation by the presence of water. Dynamic NMR studies demonstrate that the highly anionic N-terminus is strongly adsorbed and immobilized on the HAP surface, while the middle and C-terminal regions of this domain are mobile and thus weakly interacting with the mineral surface. The direct binding footprint of statherin is thus localized to the negatively charged N-terminal pentapeptide sequence. Study of a site-directed mutant demonstrated that alteration of the only anionic side chain outside of this domain did not affect the dynamics of statherin on the HAP surface, suggesting that it does not play an important role in HAP binding.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi010864c