Stability of collagen with polyols against guanidine denaturation.
The effect of polyol osmolytes such as erythritol, xylitol and sorbitol on the protection of collagen against guanidine hydrochloride (GdmCl) was studied using circular dichroism and fluorescence spectroscopy. Collagen was denatured by various concentrations of GdmCl in the presence of polyols. The absorbance was high for GdmCl treated collagen than native and polyols treated analogue. Fluorescence emission properties were studied at the excitation wavelength of 235 nm. The emission wavelength is red shifted from 308 to 370 nm for GdmCl treated collagen with polyols. Increasing the concentration of GdmCl did not affect the peak position. CD studies proved that the aggregation of collagen in the presence of lower concentrations of GdmCl. At higher concentrations of GdmCl due to the loss of secondary structure no clear CD spectra were observed. This shows that the unfolding of collagen is closely related to GdmCl concentrations. The ability of the polyols to protect collagen against guanidine denaturation decreased in order from erythritol to xylitol to sorbitol. The presence of OH group in the solvent structure is important for stabilization of collagen due to the formation of additional stabilizing hydrogen bonds.
Usha
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Biophysics Laboratory, Central Leather Research Institute, Adyar, Chennai, India. usharamamoorthy54@yahoo.co.in
Ramasami
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T
D000818:Animals; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D004355:Drug Stability; D004896:Erythritol / Q000737:chemistry*; D019791:Guanidine; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D051381:Rats; D013012:Sorbitol / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014993:Xylitol / Q000737:chemistry*
D013012:Sorbitol; D003094:Collagen; D019791:Guanidine; D004896:Erythritol; D014993:Xylitol