The thermal behavior of collagen in solution: Effect of glycerol and 2-propanol

Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique

“…However, many of the structural and functional features of assembled fibrils can be recreated in vitro under appropriate conditions using collagen extracted from a variety of source animal tissues into neutral salt or buffers, or, more frequently, into dilute acidic solutions (1). Fibrillogenesis can be controlled by varying the pH (17)(18)(19)(20), temperature (18,19,21,22), and buffer conditions (17,18,23,24). Under acidic conditions, collagen exists primarily as a soluble triple helix (17) below its melting transition around 42 C (24).…”

Biophysics of recellularized porcine cardiac extracellular matrix for myocardial tissue engineering

“…The mechanical properties of collagen-based materials depend critically on certain bulk material properties such as their hydration level and the thermal stability. [21,154,155] For instance, water content influences the structure, mechanical behaviors and chemical stability of the hydrated scaffolds; [156][157][158][159] while thermal stability reflects the compositions and structures of proteins in the materials and their denaturation behaviors. [160][161][162][163][164] Having collagen being the dominant protein composes our ECM, their bulk biophysical properties should be quantitatively measured in absolute temperature-controlled equipment such as scanning calorimetry, and thermogravimetric analysis.…”

“…The level of hydration has substantial influence in hydrated biomaterials' thermal stability and biomechanical properties. [155,158,159,198] Hence, thermogalvanometric analysis was done to evaluate the hydration content of the ECM, native tissues and reseeded ECM constructs with absolute temperature-controlled TA Instruments TGA 2950. Samples of each group were weighed and their changes in weight over the heating span were recorded and presented in Fig.…”

“…With reference to our published data on proteomics, the dominant proteins of the ECM would be collagen I (about 54% of coverage). [86] Li et al [155] ; Fathima et al [202] ; Leikina et al [203] ; Lee et al [204] ; and McClain et al [205] all reported single-peak DSC traces of their protein-based materials.…”

“…In addition, molecular dynamics of protein molecules are also dependent on the state of water [154,[156][157][158][159]200] and thus hydration level has substantial influence in thermal stability and mechanical properties of materials [155,158,159,198] . Correlating to the TGA results previously stated in section 9.1, the higher level of hydration in ECM could lead to more swollen collagen fibers and lower denaturation temperature, [156] resulting in more ductile material behaviors of collagenous tissues.…”