Effect of pH and urea on the proteins secondary structure at the water/air interface and in solution

Hypothesis: The secondary structure of proteins affects their functionality and performance in physiological environments or industrial applications. Change of the solution pH or the presence of protein denaturants are the main chemical means that can alter the secondary structure of proteins or lead to protein denaturation. Since proteins in the bulk solution and those residing at the solution/air interface experience different local environments, their response to chemical denaturation can be different. Experiments: We utilize circular dichroism and chiral/achiral sum frequency generation spectroscopy to study the secondary structure of selected proteins as a function of the solution pH or in the presence of 8 M urea in the bulk solution and at the solution/air interface, respectively. Findings: The liquid/air interface can enhance or decrease protein conformation stability. The change in the secondary structure of the surface adsorbed proteins in alkaline solutions occurs at pH values lower than those denaturing the studied proteins in the bulk solution. In contrast, while 8 M urea completely denatures the studied proteins in the bulk solution, the liquid/air interface prevents the urea-induced denaturation of the surface adsorbed proteins by limiting the access of urea to the hydrophobic side chains of proteins protruding to air. (c) 2021 Elsevier Inc. All rights reserved.

Automated summary

The change in protein secondary structure affects functionality and performance, with proteins responding differently to chemical denaturation in different environments. The liquid/air interface can either enhance or decrease protein conformation stability, while the presence of urea induces denaturation in bulk solution but may be prevented at the liquid/air interface.