ArticleCell biochemistry and biophysics2025
Protective Effect of Curcumin on Thermally Aggregated Bovine Serum Albumin.
Article in Cell biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Curcumin is a polyphenol with medicinal properties, including antioxidant properties. It scavenges free radicals by increasing glutathione transferase activity. It is shown to inhibit the aggregation of proteins such as α-synuclein and amyloid β-peptide. In our study, BSA samples were incubated at 65 °C and then analyzed for aggregate formation. Furthermore, curcumin was examined for its anti-aggregatory potential. The inspection of aggregates was done using various spectrophotometric assays like UV-absorbance, congo red, turbidity, and CD spectra, as well as spectrofluorometric measurements such as intrinsic and ThT fluorescence. Visualisation of aggregates was done by transmission electron microscopy. BSA was incubated at 65 °C for 124 h. Intrinsic fluorescence and UV-absorbance showed increased spectra, suggesting unfolding of BSA. Aggregate formation was confirmed by increased ThT intensity, 15 nm red shift in CR absorbance, and appearance of a peak at 218 nm in CD spectra. Addition of 60 µM curcumin was found to be an effective concentration that inhibits the BSA aggregation as validated by decreased ThT fluorescence and CR absorbance. The UV-absorbance, intrinsic fluorescence, and reappearance of peaks at 208 and 222 nm in CD spectra confirmed that curcumin helps to maintain the native contacts of BSA and protects it from unfolding as well as aggregation. Protein aggregates are associated with various pathological conditions. In this study, curcumin was found to be a potential therapeutic molecule to clear aggregates in vitro. These results suggest developing a clinically used imitative of curcumin and related compounds.
Indexed as
Identifiers
40652124What OpenQuestion holds
Registered trials
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.