A Solid-State NMR Study of the Dynamics and Interactions of Phenylalanine Rings in a Statherin Fragment Bound to Hydroxyapatite Crystals

Gibson, James M; Popham, Jennifer M; Raghunathan, Vinodhkumar; Stayton, Patrick; Drobny, Gary P

doi:10.1021/ja056731m

Title: A Solid-State NMR Study of the Dynamics and Interactions of Phenylalanine Rings in a Statherin Fragment Bound to Hydroxyapatite Crystals

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Abstract

Extracellular matrix proteins regulate hard tissue growth by acting as adhesion sites for cells, by triggering cell signaling pathways, and by directly regulating the primary and/or secondary crystallization of hydroxyapatite, the mineral component of bone and teeth. Despite the key role that these proteins play in the regulation of hard tissue growth in humans, the exact mechanism used by these proteins to recognize mineral surfaces is poorly understood. Interactions between mineral surfaces and proteins very likely involve specific contacts between the lattice and the protein side chains, so elucidation of the nature of interactions between protein side chains and their corresponding inorganic mineral surfaces will provide insight into the recognition and regulation of hard tissue growth. Isotropic chemical shifts, chemical shift anisotropies (CSAs), NMR line-width information, 13C rotating frame relaxation measurements, as well as direct detection of correlations between 13C spins on protein side chains and 31P spins in the crystal surface with REDOR NMR show that, in the peptide fragment derived from the N-terminal 15 amino acids of salivary statherin (i.e., SN-15), the side chain of the phenylalanine nearest the C-terminus of the peptide (F14) is dynamically constrained and oriented near the surface, whereas the side chain of themore »« less

Authors:: Gibson, James M; Popham, Jennifer M; Raghunathan, Vinodhkumar; Stayton, Patrick; Drobny, Gary P

Publication Date:: Wed Apr 26 00:00:00 EDT 2006

Research Org.:: Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)

Sponsoring Org.:: USDOE

OSTI Identifier:: 899484

DOE Contract Number:: AC05-76RL01830

Resource Type:: Journal Article

Journal Name:: Journal of the American Chemical Society, 128(16):5364-5370

Additional Journal Information:: Journal Name: Journal of the American Chemical Society, 128(16):5364-5370

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; ADHESION; AMINO ACIDS; CHEMICAL SHIFT; CRYSTALLIZATION; DETECTION; LYSINE; ORIENTATION; PEPTIDES; PHENYLALANINE; PROTEINS; REGULATIONS; RELAXATION; Environmental Molecular Sciences Laboratory

Citation Formats


                    Gibson, James M, Popham, Jennifer M, Raghunathan, Vinodhkumar, Stayton, Patrick, and Drobny, Gary P. A Solid-State NMR Study of the Dynamics and Interactions of Phenylalanine Rings in a Statherin Fragment Bound to Hydroxyapatite Crystals.  United States: N. p., 2006. 
        Web.  doi:10.1021/ja056731m.

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                    Gibson, James M, Popham, Jennifer M, Raghunathan, Vinodhkumar, Stayton, Patrick, & Drobny, Gary P. A Solid-State NMR Study of the Dynamics and Interactions of Phenylalanine Rings in a Statherin Fragment Bound to Hydroxyapatite Crystals.  United States.  https://doi.org/10.1021/ja056731m

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                    Gibson, James M, Popham, Jennifer M, Raghunathan, Vinodhkumar, Stayton, Patrick, and Drobny, Gary P. 2006.  
        "A Solid-State NMR Study of the Dynamics and Interactions of Phenylalanine Rings in a Statherin Fragment Bound to Hydroxyapatite Crystals".  United States.  https://doi.org/10.1021/ja056731m.

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@article{osti_899484,

  title        = {A Solid-State NMR Study of the Dynamics and Interactions of Phenylalanine Rings in a Statherin Fragment Bound to Hydroxyapatite Crystals},

  author       = {Gibson, James M and Popham, Jennifer M and Raghunathan, Vinodhkumar and Stayton, Patrick and Drobny, Gary P},

  abstractNote = {Extracellular matrix proteins regulate hard tissue growth by acting as adhesion sites for cells, by triggering cell signaling pathways, and by directly regulating the primary and/or secondary crystallization of hydroxyapatite, the mineral component of bone and teeth. Despite the key role that these proteins play in the regulation of hard tissue growth in humans, the exact mechanism used by these proteins to recognize mineral surfaces is poorly understood. Interactions between mineral surfaces and proteins very likely involve specific contacts between the lattice and the protein side chains, so elucidation of the nature of interactions between protein side chains and their corresponding inorganic mineral surfaces will provide insight into the recognition and regulation of hard tissue growth. Isotropic chemical shifts, chemical shift anisotropies (CSAs), NMR line-width information, 13C rotating frame relaxation measurements, as well as direct detection of correlations between 13C spins on protein side chains and 31P spins in the crystal surface with REDOR NMR show that, in the peptide fragment derived from the N-terminal 15 amino acids of salivary statherin (i.e., SN-15), the side chain of the phenylalanine nearest the C-terminus of the peptide (F14) is dynamically constrained and oriented near the surface, whereas the side chain of the phenylalanine located nearest to the peptide?s N-terminus (F7) is more mobile and is oriented away from the hydroxyapatite surface. The relative dynamics and proximities of F7 and F14 to the surface together with prior data obtained for the side chain of SN-15's unique lysine (i.e., K6) were used to construct a new picture for the structure of the surface-bound peptide and its orientation to the crystal surface.},

  doi          = {10.1021/ja056731m},

  url          = {https://www.osti.gov/biblio/899484},
  journal      = {Journal of the American Chemical Society, 128(16):5364-5370},
number       = ,

  volume       = ,

  place        = {United States},

  year         = {Wed Apr 26 00:00:00 EDT 2006},

  month        = {Wed Apr 26 00:00:00 EDT 2006}

}

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