Abstract
Bone construction has been under intensive scrutiny for many years using numerous techniques. Solid-state NMR spectroscopy helped unravel key characteristics of the mineral structure in bone owing to its capability of analyzing crystalline and disordered phases at high-resolution. This has invoked new questions regarding the roles of persistent disordered phases in structural integrity and mechanical function of mature bone as well as regarding regulation of early events in formation of apatite by bone proteins which interact intimately with the different mineral phases to exert biological control. Here, spectral editing tethered to standard NMR techniques is employed to analyze bone-like apatite minerals prepared synthetically in the presence and absence of two non-collagenous bone proteins, osteocalcin and osteonectin. A 1H spectral editing block allows excitation of species from the crystalline and disordered phases selectively, facilitating analysis of phosphate or carbon species in each phase by magnetization transfer via cross polarization. Further characterization of phosphate proximities using SEDRA dipolar recoupling, cross-phase magnetization transfer using DARR and T1/T2 relaxation times demonstrate that the mineral phases formed in the presence of bone proteins are more complex than bimodal. They reveal disparities in the physical properties of the mineral layers, indicate the layers in which the proteins reside and highlight the effect that each protein imparts across the mineral layers.
Original language | English |
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Article number | 101860 |
Journal | Solid State Nuclear Magnetic Resonance |
Volume | 124 |
DOIs | |
State | Published - Apr 2023 |
Bibliographical note
Publisher Copyright:© 2023 Elsevier Inc.
Funding
This manuscript is dedicated to the late Professor Shimon Vega, a unique and inspiring mentor with a creative grasp of spin physics and magnetic resonance. The authors thank Dr Yuval Elias and Lilian Cohen for critical editing of the manuscript and valuable contributions. This work was supported by research grants from the Israel Science Foundation ( #2104/20 and #1059/09 ).
Funders | Funder number |
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Israel Science Foundation | 1059/09, 2104/20 |