Abstract
In this communication, sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen were studied. We used ultrasensitive differential scanning calorimetry (US-DSC) to directly monitor the thermal transition of collagen in the presence of SDS. The results show that SDS affects the conformation and thermal stability of collagen very differently depending on its concentrations. At CSDS ≤ 0.05 mM, the enhanced thermal stability of collagen indicates the stabilizing effect by SDS. However, a further increase of SDS leads to the denaturation of collagen, verifying the well-known ability of SDS to unfold proteins. This striking difference in thermodynamics and conformational changes of collagen caused by SDS concentrations can be explained in terms of their interactions. With increasing SDS, the binding of SDS to collagen can be dominated by electrostatic interaction shifting to hydrophobic interaction, and the latter plays a key role in loosening and unfolding the triple-helix structure of collagen. The important finding in the present study is the stabilizing effect of SDS on collagen molecules at extreme low concentration.
Graphical abstract
A heterozygous defect for structurally altered pro-alpha 2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinase.