The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces

Tarasevich, Barbara J.; Lea, Alan S.; Shaw, Wendy J.

doi:10.1016/j.jsb.2009.10.007

Title: The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces

Full Record
Other Related Research

Abstract

Amelogenin and amelogenin splice variants are believed to be involved in controlling the formation of the highly anisotropic and ordered hydroxyapatite crystallites that form enamel. The adsorption behavior of amelogenin proteins onto substrates is very important because protein-surface interactions are critical to it’s function. We have studied the adsorption of LRAP, a splice variant of amelogenin which may also contribute to enamel function, onto model self-assembled monolayers on gold containing of COOH, CH3, and NH2 end groups. Dynamic light scattering (DLS) experiments indicated that LRAP in phosphate buffered saline (PBS) and solutions at saturation with calcium phosphate contained aggregates of nanospheres. Null ellipsometry and atomic force microscopy (AFM) were used to study protein adsorption amounts and structures. Relatively high amounts of adsorption occurred onto the CH3 and NH2 surfaces from both calcium phosphate and PBS solutions. Adsorption was also promoted onto COOH surfaces when calcium was present in the solutions suggesting an interaction that involves calcium bridging with the negatively charged C-terminus. The ellipsometry and AFM studies suggested that the protein adsorbed onto all surfaces as LRAP monomers. We propose that the monomers adsorb onto the surfaces by disassembling or “shedding” from the nanospheres that are present in solution. Thismore »« less

Authors:: Tarasevich, Barbara J.; Lea, Alan S.; Shaw, Wendy J.

Publication Date:: Mon Mar 15 00:00:00 EDT 2010

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

Sponsoring Org.:: USDOE

OSTI Identifier:: 974941

Report Number(s):: PNNL-SA-62449
Journal ID: ISSN 1047-8477; JSBIEM; 8993; 19851a; 19851; 2466; 17092; 1724; 453040220

DOE Contract Number:: AC05-76RL01830

Resource Type:: Journal Article

Journal Name:: Journal of Structural Biology, 169(3):266-276

Additional Journal Information:: Journal Volume: 169; Journal Issue: 3; Journal ID: ISSN 1047-8477

Country of Publication:: United States

Language:: English

Subject:: Environmental Molecular Sciences Laboratory

Citation Formats


                    Tarasevich, Barbara J., Lea, Alan S., and Shaw, Wendy J. The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces.  United States: N. p., 2010. 
        Web.  doi:10.1016/j.jsb.2009.10.007.

Copy to clipboard


                    Tarasevich, Barbara J., Lea, Alan S., & Shaw, Wendy J. The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces.  United States.  https://doi.org/10.1016/j.jsb.2009.10.007

Copy to clipboard


                    Tarasevich, Barbara J., Lea, Alan S., and Shaw, Wendy J. 2010.  
        "The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces".  United States.  https://doi.org/10.1016/j.jsb.2009.10.007.

Copy to clipboard


                    
@article{osti_974941,

  title        = {The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces},

  author       = {Tarasevich, Barbara J. and Lea, Alan S. and Shaw, Wendy J.},

  abstractNote = {Amelogenin and amelogenin splice variants are believed to be involved in controlling the formation of the highly anisotropic and ordered hydroxyapatite crystallites that form enamel. The adsorption behavior of amelogenin proteins onto substrates is very important because protein-surface interactions are critical to it’s function. We have studied the adsorption of LRAP, a splice variant of amelogenin which may also contribute to enamel function, onto model self-assembled monolayers on gold containing of COOH, CH3, and NH2 end groups. Dynamic light scattering (DLS) experiments indicated that LRAP in phosphate buffered saline (PBS) and solutions at saturation with calcium phosphate contained aggregates of nanospheres. Null ellipsometry and atomic force microscopy (AFM) were used to study protein adsorption amounts and structures. Relatively high amounts of adsorption occurred onto the CH3 and NH2 surfaces from both calcium phosphate and PBS solutions. Adsorption was also promoted onto COOH surfaces when calcium was present in the solutions suggesting an interaction that involves calcium bridging with the negatively charged C-terminus. The ellipsometry and AFM studies suggested that the protein adsorbed onto all surfaces as LRAP monomers. We propose that the monomers adsorb onto the surfaces by disassembling or “shedding” from the nanospheres that are present in solution. This work reveals the importance of small subnanosphere-sized structures of LRAP at interfaces, structures that may be important in the biomineralization of tooth enamel.},

  doi          = {10.1016/j.jsb.2009.10.007},

  url          = {https://www.osti.gov/biblio/974941},
  journal      = {Journal of Structural Biology, 169(3):266-276},

  issn         = {1047-8477},

  number       = 3,

  volume       = 169,

  place        = {United States},

  year         = {Mon Mar 15 00:00:00 EDT 2010},

  month        = {Mon Mar 15 00:00:00 EDT 2010}

}

Copy to clipboard

Journal Article:

https://doi.org/10.1016/j.jsb.2009.10.007

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Neutron Reflectometry Studies of the Adsorbed Structure of the Amelogenin, LRAP

Journal Article Tarasevich, Barbara; Perez-Salas, Ursula; Masica, David; ... - Journal of Physical Chemistry B, 117(11):3098-3109

Amelogenins make up over 90 percent of the protein present during enamel formation and have been demonstrated to be critical in proper enamel development, but the mechanism governing this control is not well understood. Leucine-rich amelogenin peptide (LRAP) is a 59-residue splice variant of amelogenin and contains the charged regions from the full protein thought to control crystal regulation. In this work, we utilized neutron reflectivity (NR) to investigate the structure and orientation of LRAP adsorbed from solutions onto molecularly smooth COOH-terminated self-assembled monolayers (SAMs) surfaces. Sedimentation velocity experiments revealed that LRAP is primarily a monomer in saturated calcium phosphatemore »« less
https://doi.org/10.1021/jp311936j
The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution

Journal Article Tarasevich, Barbara; Philo, John; Maluf, Nasib; ... - Journal of Structural Biology

Amelogenin proteins are critical to the formation of enamel in teeth and may have roles in promoting nucleation, controlling growth, and regulating microstructures of the intricately woven hydroxyapatite (HAP). Leucine-rich amelogenin protein (LRAP) is a 59-residue splice variant of amelogenin and contains the N- and C-terminal charged regions of the full-length protein thought to control crystal growth. Although the quaternary structure of full-length amelogenin in solution has been well studied and can consist of self-assemblies of monomers called nanospheres, the quaternary structure of LRAP is not as well studied. Here, analytical ultracentrifugation sedimentation velocity (SV) and small angle neutron scatteringmore »« less
Cited by 10
https://doi.org/10.1016/j.jsb.2014.10.007

Full Text Available
Adsorption of Amelogenin onto Self-Assembled and Fluoroapatite Surfaces

Journal Article Tarasevich, Barbara; Lea, Alan; Bernt, William; ... - Journal of Physical Chemistry B, 113(7):1833-1842

Abstract. The interactions of proteins at surfaces are of great importance to biomineralizaton processes and to the development and function of biomaterials. Amelogenin is a unique biomineralization protein because it self-assembles to form supramolecular structures called “nanospheres,” spherical aggregates of monomers that are 20-60 nm in diameter. Although the nanosphere quaternary structure has been observed in solution, the quaternary structure of amelogenin adsorbed onto surfaces is also of great interest because the surface structure is critical to its function. We report studies of the adsorption of the amelogenin onto self-assembled monolayers (SAMs) with COOH and CH3 end group functionality andmore »« less
https://doi.org/10.1021/jp804548x
Changes in the quaternary structure of amelogenin when adsorbed onto surfaces

Journal Article Tarasevich, Barbara; Lea, Alan; Bernt, William; ... - Biopolymers, 91(2):103-107

The amelogenin protein is involved in the formation of highly controlled and anisotropic hydroxyapatite crystals in tooth enamel. Amelogenin is unique in that it self assembles to form supramolecular quaternary structures called “nanospheres,” spherical aggregates of amelogenin monomers typically 20-60 nm in diameter. Although nanospheres have been observed in solution, the quaternary structure of amelogenin adsorbed onto surfaces is not well known. A better understanding of the surface structure is of great importance, however, because the function of amelogenin depends on it. We report studies of the adsorption of amelogenin onto self-assembled monolayers (SAMs) containing COOH and CH3 end groupmore »« less
https://doi.org/10.1002/bip.21095
A Solution NMR Investigation into the Murine Amelogenin Splice-Variant LRAP (Leucine-Rich Amelogenin Protein).

Journal Article Buchko, Garry; Tarasevich, Barbara; Roberts, Jacky; ... - Biochimica et Biophysica Acta--Proteins and Proteomics, 1804(9):1768-1774

Amelogenins are the dominant proteins present in ameloblasts during the early stages of enamel biomineralization, making up >90% of the matrix protein. Along with the full-length protein there are several splice-variant isoforms of amelogenin present including LRAP (Leucine-Rich Amelogenin Protein), a protein that consists of the first 33 and the last 26 residues of full-length amelogenin. Using solution-state NMR spectroscopy we have assigned the 1H-15N HSQC spectrum of murine LRAP (rp(H)LRAP) in 2% acetic acid at pH 3.0 by making extensive use of previous chemical shift assignments for full-length murine amelogenin (rp(H)M180). This correlation was possible because LRAP, like themore »« less
https://doi.org/10.1016/j.bbapap.2010.03.006

Similar Records