ArticleThe Journal of chemical physics2013
Electrostatic origin of in vitro aggregation of human γ-crystallin.
Article in The Journal of chemical physics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Observational Clinical Studies of Human Lens Transparency Using the Vision Index Pen.Translational vision science & technology · 2019Article
- Crystal Structure of Chicken γS-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the βγ-Crystallins.Structure (London, England : 1993) · 2017Article
- Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutations.Protein engineering, design & selection : PEDS · 2016Article
- Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.Analytical biochemistry · 2016Review
- Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein.The Journal of biological chemistry · 2016Article
- Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.Biochimica et biophysica acta · 2016Article
- Lack of Dependence of the Sizes of the Mesoscopic Protein Clusters on Electrostatics.Biophysical journal · 2015Article
- Staying Together: Protein Molecules in Mesoscopic Clusters.Biophysical journal · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The proteins α-, β-, and γ-crystallins are the major components of the lens in the human eye. Using dynamic light scattering method, we have performed in vitro investigations of protein-protein interactions in dilute solutions of human γ-crystallin and α-crystallin. We find that γ-crystallin spontaneously aggregates into finite-sized clusters in phosphate buffer solutions. There are two distinct populations of unaggregated and aggregated γ-crystallins in these solutions. On the other hand, α-crystallin molecules are not aggregated into large clusters in solutions of α-crystallin alone. When α-crystallin and γ-crystallin are mixed in phosphate buffer solutions, we demonstrate that the clusters of γ-crystallin are prevented. By further investigating the roles of temperature, protein concentration, pH, salt concentration, and a reducing agent, we show that the aggregation of γ-crystallin under our in vitro conditions arises from non-covalent electrostatic interactions. In addition, we show that aggregation of γ-crystallin occurs under the dilute in vitro conditions even in the absence of oxidizing agents that can induce disulfide cross-links, long considered to be responsible for human cataracts. Aggregation of γ-crystallin when maintained under reducing conditions suggests that oxidation does not contribute to the aggregation in dilute solutions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.