Structure characterization of human serum proteins in solution and dry state

Area of Science:

• Biochemistry
• Protein Chemistry
• Analytical Chemistry

Background:

• Coronary atherosclerosis involves alterations in protein metabolism.
• Human serum proteins, including albumin (HSA) and globulin (HSG), play crucial roles in physiological processes.
• Understanding protein structure changes is vital for disease management.

Purpose of the Study:

• To investigate the impact of moderate beer consumption on the structure of human serum proteins (HSA and HSG).
• To establish correlations between beer consumption and changes in protein metabolism in patients with coronary atherosclerosis.
• To compare the stability of HSA and HSG fractions post-consumption.

Main Methods:

• Utilized intrinsic fluorescence, circular dichroism (CD), differential scanning calorimetry, and hydrophobicity (So) measurements.
• Denatured HSA and HSG using varying concentrations of urea.
• Analyzed thermal denaturation parameters (Td, DeltaH, DeltaS) and calculated hydrogen bonds ruptured and degree of denaturation (%D).

Main Results:

• Observed differences in the secondary and tertiary structures of HSA and HSG before and after beer consumption.
• Qualitative changes in thermal denaturation profiles indicated altered protein structures.
• Beer consumption, particularly ethanol, influenced protein compactability and structural stability, with HSG exhibiting greater stability than HSA.

Conclusions:

• Human serum protein structure undergoes conformational changes upon moderate beer consumption.
• HSG demonstrates higher stability compared to HSA under the studied conditions.
• These findings contribute to understanding protein metabolism shifts in coronary atherosclerosis patients related to dietary factors.