ArticlePloS one2013
Quantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albumin.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Refolding Increases the Chaperone-like Activity of αInternational journal of molecular sciences · 2023Article
- SEDNTERP: a calculation and database utility to aid interpretation of analytical ultracentrifugation and light scattering data.European biophysics journal : EBJ · 2023Article
- Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding.International journal of molecular sciences · 2020Article
- Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ.International journal of molecular sciences · 2020Article
- A New Functional Model for Prediction of Chaperone Activity of the RecombinantThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2019Article
- A change in the aggregation pathway of bovine serum albumin in the presence of arginine and its derivatives.Scientific reports · 2017Article
- Article
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Authors and funding
8 authors.
Funding
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Abstract
The methodology for quantification of the anti-aggregation activity of protein and chemical chaperones has been elaborated. The applicability of this methodology was demonstrated using a test-system based on dithiothreitol-induced aggregation of bovine serum albumin at 45°C as an example. Methods for calculating the initial rate of bovine serum albumin aggregation (v agg) have been discussed. The comparison of the dependences of v agg on concentrations of intact and cross-linked α-crystallin allowed us to make a conclusion that a non-linear character of the dependence of v agg on concentration of intact α-crystallin was due to the dynamic mobility of the quaternary structure of α-crystallin and polydispersity of the α-crystallin-target protein complexes. To characterize the anti-aggregation activity of the chemical chaperones (arginine, arginine ethyl ester, arginine amide and proline), the semi-saturation concentration [L]0.5 was used. Among the chemical chaperones studied, arginine ethyl ester and arginine amide reveal the highest anti-aggregation activity ([L]0.5 = 53 and 58 mM, respectively).
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