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Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
Published on: August 22, 2016
Implications of macromolecular crowding for protein assembly
1Laboratory of Biochemistry and Genetics, Section on Physical Biochemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA. minton@helix.nih
Current Opinion in Structural Biology
|February 19, 2000
Summary
Macromolecular crowding influences protein assembly by stabilizing native structures and promoting functional complex formation. However, overcrowding can lead to pathological aggregation, forming amyloid and inclusion bodies.
Area of Science:
- Biochemistry
- Biophysics
- Molecular Biology
Background:
- High concentrations of macromolecules in solution, termed macromolecular crowding, significantly impact biological processes.
- Excluded volume effects in crowded solutions are increasingly recognized for their influence on protein behavior.
Purpose of the Study:
- To explore the role of macromolecular crowding in protein structure stabilization and complex formation.
- To investigate the potential for overcrowding to induce non-functional protein aggregation.
Main Methods:
- Theoretical analysis of excluded volume effects in concentrated macromolecular solutions.
- Review of experimental studies on protein folding, complexation, and aggregation under crowded conditions.
Main Results:
- Crowding generally favors the stabilization of native protein structures over non-native conformations.
- Formation of functional protein complexes is promoted by macromolecular crowding.
- Pathological conditions characterized by 'overcrowding' can drive the aggregation of non-native proteins, leading to amyloid and inclusion bodies.
Conclusions:
- Macromolecular crowding is a critical factor in modulating protein assembly pathways.
- Understanding crowding effects is essential for comprehending both normal protein function and disease-associated aggregation.
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