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BSA kinetically traps protein KH1 in unfolded state
Kai Cheng1, Qiong Wu2, Xiaoli Liu2
1Key Laboratory of Catalysis and Energy Materials Chemistry of Ministry of Education & Hubei Key Laboratory of Catalysis and Materials Science, Hubei R&D Center of Hyperbranched Polymers Synthesis and Applications, South-Central Minzu University, Wuhan 430074, China.
Physical Chemistry Chemical Physics : PCCP
|March 26, 2026
Summary
Bovine serum albumin (BSA) causes kinetic unfolding of KH1 proteins, trapping them via disulfide bonds. This reveals how disulfide bonds can control protein kinetic stability.
Area of Science:
- Biochemistry
- Protein Chemistry
- Biophysics
Background:
- Protein kinetic stability is crucial for biological function.
- Disulfide bonds play a significant role in protein structure and stability.
- Understanding protein unfolding mechanisms is essential for various applications.
Purpose of the Study:
- To investigate the effect of bovine serum albumin (BSA) on the kinetic unfolding of KH1 proteins.
- To elucidate the role of intermolecular disulfide bonds in protein trapping.
- To explore the modulation of protein kinetic stability through disulfide bond interactions.
Main Methods:
- 19F NMR spectroscopy was utilized to monitor protein unfolding.
- Kinetic analysis was performed to assess the time-dependent changes.
- Disulfide bond formation was investigated as a mechanism for protein trapping.
Main Results:
- BSA was shown to induce time-dependent kinetic unfolding of KH1 proteins.
- Intermolecular disulfide bonds were identified as the mechanism trapping KH1 proteins in an unfolded state.
- The formation of these disulfide bonds directly influences the kinetic stability of the proteins.
Conclusions:
- BSA triggers a process leading to the kinetic unfolding and subsequent stabilization of KH1 proteins.
- Intermolecular disulfide bond formation is a key factor in modulating protein kinetic stability.
- This study provides insights into protein dynamics and stabilization mechanisms.
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