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Title: Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite

Abstract

The ability to develop materials with hierarchical structure and controlled properties is highly desirable. Biomineralization processes govern the formation of hierarchical hard tissues such as bone and teeth and mimicking these processes could allow new materials with difffernet properties. The proteins present during biomineral formation are proposed to play a critical role in the unique properties of these minerals. While structure is commonly affiliated with the function of proteins, biomineralization proteins are bound to a solid surface in their physiologically relevant form, limiting the role of protein structure due to the inability to use many conventional structure characterization techniques. Here, solid state NMR spectroscopy was applied to study the intermolecular interactions of amelogenin in self-assembled oligomers bound to hydroxyapatite. Amelogenin is the most abundant protein present during the early stages of enamel formation and is essential for normal enamel development. Intermolecular dipolar couplings were identified that support amelogenin dimer formation due to interactions between residues in the C-termini. These dipolar interactions were corroborated by molecular dynamics computer simulations. We also identified b-sheet structure in multiple regions of the protein, further developing our knowledge of this protein. This is the first intermolecular protein-protein interaction reported for a biomineralization protein, representing anmore » advancement in understanding enamel development and a new general strategy towards investigating biomineralization proteins.« less

Authors:
; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1503553
Report Number(s):
PNNL-SA-131727
Journal ID: ISSN 0006-3495
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Journal Name:
Biophysical Journal
Additional Journal Information:
Journal Volume: 115; Journal Issue: 9; Journal ID: ISSN 0006-3495
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
amelogenin, biomineralization, intermolecular, interactions, Solid state NMR, protien structure

Citation Formats

Arachchige, Rajith Jayasinha, Burton, Sarah D., Lu, Jun-Xia, Ginovska, Bojana, Harding, Larisa K., Taylor, Megan E., Tao, Jinhui, Dohnalkova, Alice, Tarasevich, Barbara J., Buchko, Garry W., and Shaw, Wendy J. Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite. United States: N. p., 2018. Web. doi:10.1016/j.bpj.2018.08.027.
Arachchige, Rajith Jayasinha, Burton, Sarah D., Lu, Jun-Xia, Ginovska, Bojana, Harding, Larisa K., Taylor, Megan E., Tao, Jinhui, Dohnalkova, Alice, Tarasevich, Barbara J., Buchko, Garry W., & Shaw, Wendy J. Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite. United States. doi:10.1016/j.bpj.2018.08.027.
Arachchige, Rajith Jayasinha, Burton, Sarah D., Lu, Jun-Xia, Ginovska, Bojana, Harding, Larisa K., Taylor, Megan E., Tao, Jinhui, Dohnalkova, Alice, Tarasevich, Barbara J., Buchko, Garry W., and Shaw, Wendy J. Thu . "Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite". United States. doi:10.1016/j.bpj.2018.08.027.
@article{osti_1503553,
title = {Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite},
author = {Arachchige, Rajith Jayasinha and Burton, Sarah D. and Lu, Jun-Xia and Ginovska, Bojana and Harding, Larisa K. and Taylor, Megan E. and Tao, Jinhui and Dohnalkova, Alice and Tarasevich, Barbara J. and Buchko, Garry W. and Shaw, Wendy J.},
abstractNote = {The ability to develop materials with hierarchical structure and controlled properties is highly desirable. Biomineralization processes govern the formation of hierarchical hard tissues such as bone and teeth and mimicking these processes could allow new materials with difffernet properties. The proteins present during biomineral formation are proposed to play a critical role in the unique properties of these minerals. While structure is commonly affiliated with the function of proteins, biomineralization proteins are bound to a solid surface in their physiologically relevant form, limiting the role of protein structure due to the inability to use many conventional structure characterization techniques. Here, solid state NMR spectroscopy was applied to study the intermolecular interactions of amelogenin in self-assembled oligomers bound to hydroxyapatite. Amelogenin is the most abundant protein present during the early stages of enamel formation and is essential for normal enamel development. Intermolecular dipolar couplings were identified that support amelogenin dimer formation due to interactions between residues in the C-termini. These dipolar interactions were corroborated by molecular dynamics computer simulations. We also identified b-sheet structure in multiple regions of the protein, further developing our knowledge of this protein. This is the first intermolecular protein-protein interaction reported for a biomineralization protein, representing an advancement in understanding enamel development and a new general strategy towards investigating biomineralization proteins.},
doi = {10.1016/j.bpj.2018.08.027},
journal = {Biophysical Journal},
issn = {0006-3495},
number = 9,
volume = 115,
place = {United States},
year = {2018},
month = {11}
}