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Pharmacokinetics of some newly synthesized 1, 5- benzothiazepine scaffolds: A molecular docking and molecular dynamics simulation approach

Journal of King Saud University - Science, ISSN: 1018-3647, Vol: 35, Issue: 3, Page: 102528
2023
  • 2
    Citations
  • 0
    Usage
  • 14
    Captures
  • 1
    Mentions
  • 65
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    2
  • Captures
    14
  • Mentions
    1
    • News Mentions
      1
      • News
        1
  • Social Media
    65
    • Shares, Likes & Comments
      65
      • Facebook
        65

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Department of Chemistry Researchers Have Published New Data on Health and Medicine (Pharmacokinetics of some newly synthesized 1, 5- benzothiazepine scaffolds: A molecular docking and molecular dynamics simulation approach)

2023 APR 11 (NewsRx) -- By a News Reporter-Staff News Editor at NewsRx Drug Daily -- Investigators discuss new findings in agriculture. According to news

Article Description

A highly efficient in silico pharmacokinetics was studied for some newly synthesized 1, 5- benzothiazepine derivatives. A total of fourteen title moieties were prepared by the condensation of substituted chalcones and 2- aminothiophenol that led to ring expansion in the presence of CuO nanocatalytic framework. The reported synthetic route is advantageous due to shorter reaction time and enhanced yield. The drug-target binding analysis revealed the potential therapeutic targets against 1,5- benzothiazepine derivatives using auto in silico consensus inverse docking (ACID) server. Among the seven selected 1,5- benzothiazepine derivatives, consensus inverse docking (CID) against PDB-binding database identified potential therapeutic targets using structure-based screening. The comparative analysis predicted 4-hydroxyphenylpyruvate dioxygenase (HPPD) (Uniprot ID: P32754 ), involved in the regulation of blood tyrosine levels by catalyzing the reaction of HPPD to homogentisic acid in tyrosine catabolism pathway. Dimethylglycine dehydrogenase (DMGDH) (Uniprot ID: Q9AGP8 ), a flavin adenine dinucleotide (FAD)‐ and tetrahydrofolate (THF)‐dependent, mitochondrial matrix enzyme that degrades choline and transfers electrons to the respiratory chain, one‐carbon metabolism, and folate receptor beta (Uniprot ID: P14207 ), which is a glycosylphosphatidylinositol-linked protein capturing ligands from the extracellular matrix and passages them inside the cell through endosomal pathway and recognized as an emerging biomarker for cancer and chronic inflammatory diseases, as potential targets for the selected derivatives. These findings warrant for in vitro cell-based experimental validation of the currently identified actives.

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