Molecular Interactions of LLCs with Proteins and Nucleotides

8 Molecular Interactions of LLCs with Proteins and Nucleotides 

Amar-Yuli et al. combined the potential of both liquid crystalline structure as well as glycerol as cosolvent to enhance insulin thermal stability and moderate the aggregation progress [49]. Insulin was incorporated into several modified reverse hexagonal systems based on friendly surfactant and polyols to explore the impact of the protein confinement on its stability, unfolding behavior, and morphology with severe external conditions, low pH, and higher temperatures (up to 70 °C). 

The investigators focused on solubilizing insulin in GMO/decane/water, GMO/ decane/glycerol/water, and GMO/phosphatidylchoUne (PC)/decane/glycerol/water 

All fourth matrices did not reveal any significant changes in content of the conformational elements up to 60 °C (Fig. 12.10). However, prolonged incubation of insulin at 60 °C for 60 min caused an increase in the jS-sheet configurations from 25 to 36 % only when insulin was confined in the water-filled Hn phase (first Hn system, data not shown). Once the temperature reached 70 °C, marked increase in the parallel and anti-parallel /1-sheet bands (Fig. 12.10) were detected in all 

The results presented in this study provide valuable insights into the protection abilities and mechanism of the used colloid structures, containing cosolvent as a medium for long-term protein stabihty. Moreover, these findings yield valuable information regarding the effect of these colloid structures confinement on insulin fibrillation and/or aggregation. 

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