ArticleRSC advances2020
Spectroscopic demonstration of sinapic acid methyl ester complexes with serum albumins.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- Quenching of Protein Fluorescence by Fullerenol CInternational journal of molecular sciences · 2022Article
- PI3K/mTOR Dual Inhibitor Pictilisib Stably Binds to Site I of Human Serum Albumin as Observed by Computer Simulation, Multispectroscopic, and Microscopic Studies.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The methyl ester of sinapic acid (MESA) is a molecule with confirmed antioxidant properties. It is important to establish whether it can be transported across humans and animals. Therefore, we investigated MESA interactions with serum albumins, namely, human serum albumin (HSA), bovine serum albumin (BSA), rabbit serum albumin (RSA), and sheep serum albumin (SSA). Experiments were performed in a pH range from 5.9 to 10.7 using absorption and fluorescence techniques. It was found that MESA formed complexes with every albumin in the entire pH range under examination, which was confirmed by the appearances of new absorption and fluorescence complex bands. Fluorescence intensities were much higher (up to 20 times) and lifetimes were up to 340 times as compared to those for unbound MESA. The quenching experiments at pH 7.4 showed that the stoichiometry for every albumin was 1 : 1; the binding constant was the highest for HSA, which reached 52 000 M
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Registered trials
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