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Role of solvents in stability of collagen

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Abstract

The influence of hydroxymethyl chain length of the solvents on collagen was established with conformational stability and thermal stability. Thermal stability of monomeric collagen and RTT fibres (rat tail tendon) treated with methanol, ethylene glycol (EG) and glycerol were reported using the melting temperature for helix-coil transition and the peak temperature for collagen-gelatin transition. Both melting temperature and peak temperature increases as the hydroxymethyl chain length increases. Conformational stability of collagen solution treated with lower and higher concentrations of methanol, ethylene glycol and glycerol indicates that aggregation of collagen molecule is more at higher concentrations of these solvents. The concentration dependence is greater for the increased number of OH groups. Since protein aggregation is associated with neuro degenerative diseases, aggregation of collagen molecule in the presence of solvents is of great importance for biomedical application.

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Authors and Affiliations

  1. Biophysics Laboratory, Central Leather Research Institute, Adyar, Chennai, 600 020, India

    R. Usha & T. Ramasami

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  1. R. Usha
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  2. T. Ramasami
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Correspondence to R. Usha.

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Usha, R., Ramasami, T. Role of solvents in stability of collagen. J Therm Anal Calorim 93, 541–545 (2008). https://doi.org/10.1007/s10973-006-7887-5

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  • DOI: https://doi.org/10.1007/s10973-006-7887-5

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