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Synchrotron FTIR microspectroscopy for quantitative assessment of collagen mineralization: a comparative analytical
Selçuk Kaan Hacıosmanoğlu1, Abdulbaki Belet1, Gihan Kamel2,3
1Nanoscience and Nanoengineering Program, Graduate School, Istanbul Medeniyet University, 34700, Istanbul, Turkey.
Abstract:
This study employs synchrotron Fourier transform infrared (SR-FTIR) microspectroscopy to comparatively assess structural changes in wet-spun collagen fibers mineralized by three methods: polymer-induced liquid precursor (PILP), in situ precipitation, and hydroxyapatite mineral addition (H.A.M.A.). Spectroscopic analysis revealed method-dependent protein structural perturbations, with PILP and in situ methods showing minor amide I perturbations (≤ 4 cm⁻1) (1656-1658 cm⁻1) while H.A.M.A. induced shifts to 1650 cm⁻1. Mineral quality assessment via Ca/PO₄ peak ratios and mineral-to-organic ratios (0.21-0.32) distinguished between approaches. PILP mineralization exhibited minimal structural disruption with the highest Ca/PO₄ ratios, whereas H.A.M.A. achieved maximum mineral loading (MTO = 0.32) with greater structural alteration. These analytical findings establish spectroscopic markers correlating mineralization pathway with collagen structural integrity and mineral composition.
