The effects of certain glycols, substituted glycols and related organic solvents on the thermal stability of soluble collagen.
The effects of a number of related diols, substituted diols and glycerol on the thermal stability of acid-soluble calf skin collagen were investigated. Thermal transition temperatures were determined by optical rotation measurement. Short-chain diols with terminal hydroxyl groups, i.e. ethylene glycol and propane-1,3-diol, stabilized the protein at all accessible concentrations. Stabilization was also observed with glycerol and diethylene glycol. Higher homologues in the diol series produced various effects, as did hydroxyl-group positional isomerism. Monoalkyl substitution of diols progressively lowered the denaturation temperature of collagen. Results are discussed in relation to possible mechanisms of perturbant action.
D000818:Animals; D002417:Cattle; D003094:Collagen; D005990:Glycerol; D006018:Glycols; D006358:Hot Temperature; D009904:Optical Rotation; D011409:Propylene Glycols; D011487:Protein Conformation; D011489:Protein Denaturation; D012867:Skin; D012997:Solvents; D013237:Stereoisomerism
D006018:Glycols; D011409:Propylene Glycols; D012997:Solvents; D003094:Collagen; D005990:Glycerol