Nonadditive effects of mixed crowding on protein stability
Open accessAbstract
The crowded environments inside cells can have significant effects on the folding stability and other biophysical properties of proteins. In this study on how macromolecular crowding affects protein folding, we took a significant step toward realistically mimicking intracellular environments by using a mixture of two crowding agents, Ficoll and dextran. We found that the mixed crowding exerts a greater stabilizing effect than the sum of the two individual crowding agents. Therefore, the composition of crowders, not just the total concentration, has a significant influence on the effects of crowding on protein folding. Since the composition of intracellular macromolecules varies within the lifetime of a cell, our finding may provide an explanation for age being an important risk factor for protein aggregation‐related diseases such as Alzheimer's disease and Parkinson's disease. Proteins 2009. © 2009 Wiley‐Liss, Inc.
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Various methods exist to chemically crosslink dextran to form a hydrogel.
“There are various methods to chemically crosslink dextran to form a hydrogel [71].”
From Resorbable Biomaterials Used for 3D Scaffolds in Tissue Engineering: A Review (2023) · cites this paper as [71]
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Resorbable Biomaterials Used for 3D Scaffolds in Tissue Engineering: A Review
Vach Agocsova, S., Culenova, M., Birova, I., Omanikova, L., Moncmanova, B., Danisovic, L., Ziaran, S., Bakos, D., & Alexy, P. (2023) · Materials · doi:10.3390/ma16124267 · Cited by 98 · see citing works
- Authors
- Batra, J., Xu, K., & Zhou, H.
- Affiliations
- Florida State University (US)
- Corresponding author
- Zhou, Huan‐Xiang
- ORCID
- Zhou, Huan‐Xiang
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 2009-04-30
- Volume
- 77
- Issue
- 1
- Pages
- 133-138
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- PMC
- PMC4456354
- OpenAlex
- W2155342128
- Cited by
- 109
- References
- 2
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 5 · 2023: 5 · 2022: 7 · 2021: 7 · 2020: 6 · 2019: 8 · 2018: 3 · 2017: 3 · 2016: 9 · 2015: 7 · 2014: 3 · 2013: 12 · 2012: 7
- FWCI
- 3.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proteins Structure Function and Bioinformatics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM058187, GM058187)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- macromolecular crowding, protein folding stability, Ficoll, dextran, non-additive effects, intracellular environment, protein aggregation, Alzheimer's disease, Parkinson's disease
- MeSH terms
- Dextrans, Ficoll, Models, Biological, Thermodynamics, Protein Folding, Tacrolimus Binding Proteins, Protein Stability
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