Far-infrared spectroscopy of salt penetration into a collagen fiber scaffold

Journal of Biological Physics
Maya MizunoHiroaki Kojima

Abstract

We employed far-infrared spectroscopy to observe the amount of salt that penetrates into collagen fiber masses. The absorption properties of collagen sheets prepared from tilapia skin, bovine skin, rat tail, and sea cucumber dermis were measured using a transmission Fourier transform spectrometer in a band from approximately 100 to 700 cm(-1). We confirmed that the absorbance spectra of the four types of dried collagen sheet show good agreement, even though the amino acid compositions differed. The absorbance peaks observed in the band corresponded to collective vibrations of plural functional groups such as methylene and imino groups in collagen. When salt solution was added to the collagen sheets and then dried, the spectral shapes of the sheets at approximately 166 cm(-1) were clearly different from those of the plain collagen sheets. The differential absorbance between wavenumbers 166 cm(-1) and 250 cm(-1) sensitively reflected the difference between higher-order structures, and the salt diffusion (crystallization) depended on the collagen fiber condition. From these results, we consider that spectral changes can be used for the numerical evaluation of salt penetration into a collagen fiber scaffold.

References

Jan 9, 2007·Biophysical Journal·Uwe FreudenbergCarsten Werner
Dec 8, 2010·Micron : the International Research and Review Journal for Microscopy·Benedicto de Campos Vidal, Maria Luiza S Mello
Apr 6, 2011·Biophysical Journal·Corinne GulleksonLaurent Kreplak
Jan 17, 2014·Nature Communications·Gheorghe AcbasA G Markelz
Mar 29, 2014·Applied Biochemistry and Biotechnology·Nasim AdibzadehNaser Farrokhi

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Citations

May 16, 2018·Biomedical Optics Express·Maya MizunoSoichi Watanabe

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