Skip to main content

The role of structural and solvation dynamics of matrix proteins on apatite mineralization


EMSL Project ID
60172

Abstract

Our goal is to identify the spatial distributions, solvent and structural dynamics of matrix proteins (such as amelogenin, collagen) with joint ultrahigh spatial resolution as well as structural selectivity. The need for high spatial resolution is necessitated by the nanometric nature of the protein assemblies, whereby protein structures and their heterogeneous distributions control the nucleation, phase transformation and organization in biomineral (such as calcium phosphate) in ways that are largely unexplored. Only topographic imaging is nonetheless often insufficient; the need for nanoscale chemical/vibrational and solvent structure mapping, e.g. to directly probe protein conformation and solvation dynamics over the diverse protein assemblies in relevance to biomineralization, presents itself in this context. In this regard, we will apply in situ high speed atomic force microscopy (AFM), 3D Fast force mapping (3D FFM) in AFM, in situ AFM-based tip-enhanced Raman/infrared scattering-scanning near-field spectroscopy (TERS/IR s-SNOM), which will allow us to record sub-nanometer to micrometer-resolved co-localized topographic and vibrational maps of protein on mineral crystals in solution environment. We anticipate that the combination of these novel capabilities will allow to establish the relationship between mineralization kinetics, interfacial solvation structure, and protein secondary structure, which is typical in the fingerprint (300-1800 cm-1) region of Raman/FTIR.

Project Details

Project type
Exploratory Research
Start Date
2021-12-01
End Date
2023-07-03
Status
Closed

Team

Principal Investigator

Jinhui Tao
Institution
Pacific Northwest National Laboratory

Co-Investigator(s)

Garry Buchko
Institution
Pacific Northwest National Laboratory

Team Members

Ying Xia
Institution
University of Washington