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Details

Autor(en) / Beteiligte
Titel
Binding of colchicine and ascorbic acid (vitamin C) to bovine serum albumin: An in-vitro interaction study using multispectroscopic, molecular docking and molecular dynamics simulation study
Ist Teil von
  • Journal of molecular liquids, 2021-11, Vol.342, p.117542, Article 117542
Ort / Verlag
Elsevier B.V
Erscheinungsjahr
2021
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
  • •Ascorbic acid or vitamin C is an antioxidant prescribed in flu infections (COVID).•Colchicine is used to treat gouty arthritis Ascorbic acid or.•Plasma protein binding plays significant role in pharmacokinetics of drugs.•Colchicine and vitamin C can displace each other from plasma protein binding site.•Effect of vitamin C was investigated on colchicine-BSA interaction. Two or more drugs are prescribed commonly to patients depending on their physical health conditions. Concomitant drugs might lead to specific drug-drug interactions with serum albumin, the main transporter protein present in the blood. This study evaluated the effect of colchicine on the binding of ascorbic acid (vitamin C) commonly prescribed in viral infections to bovine serum albumin (BSA). The interaction was evaluated using fluorescence spectroscopy, absorption spectroscopy, molecular docking, and molecular dynamic simulation. A static quenching mechanism was observed for both BSA-colchicine and BSA-ascorbic interaction. The binding constant for the BSA-ascorbic acid system decreased from 1.23 × 105 to 0.26 × 102 in the presence of colchicine, whereas the binding constant of BSA-colchicine decreased from 1.39 × 105 to 4.81 × 102 in the presence of ascorbic acid. Thus, the binding of ascorbic acid and colchicine was significantly affected in the presence of each other. Co-administration of colchicine and ascorbic acid needs to be studied further as the co-administration may lead to serious adverse events in patients taking vitamin C supplements and under treatment with colchicine.
Sprache
Englisch
Identifikatoren
ISSN: 0167-7322
eISSN: 1873-3166
DOI: 10.1016/j.molliq.2021.117542
Titel-ID: cdi_crossref_primary_10_1016_j_molliq_2021_117542

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