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Docking and molecular dynamic simulations of Mithramycin-A and Tolfenamic acid against Sp1 and survivin.
Lambring, Christoffer Briggs; Fiadjoe, Hope; Behera, Santosh Kumar; Basha, Riyaz.
Afiliación
  • Lambring CB; UNT Health Science Center at Fort Worth, Fort Worth, TX 76107, USA.
  • Fiadjoe H; UNT Health Science Center at Fort Worth, Fort Worth, TX 76107, USA.
  • Behera SK; Department of Biotechnology, IPER, Ahmedabad, India.
  • Basha R; UNT Health Science Center at Fort Worth, Fort Worth, TX 76107, USA.
Process Biochem ; 137: 207-216, 2024 Feb.
Article en En | MEDLINE | ID: mdl-38912413
ABSTRACT
Therapeutic targeting of Sp1 transcription factor and survivin, are studied in various cancers due to their consistent overexpression. These markers result in poorer cancer prognoses and their downregulation has been investigated as an effective treatment approach. Mithramycin-A and Tolfenamic acid are two drugs with innate anti-cancer properties and are suggested to be able to target Sp1 through GC/GT DNA binding interference, however in-depth binding and mechanistic studies are lacking. Through docking analysis, we investigated Mithramycin-A and Tolfenamic acid in terms of their specific binding interactions with Sp1 and survivin. Through further molecular dynamics simulations including Root Mean Square (RMS) Fluctuation and RMS Deviation, rGYr, and H-bond analysis, we identified critical residues involved in drug interactions with each protein in question. We show Mithramycin-A as the superior binding candidate to each protein and found that it exhibited stronger binding with Sp1, and then survivin. Subsequent molecular dynamics simulations followed the same trend as initial binding energy calculations and showed crucial amino acids involved in each Mithramycin-A-protein complex. Our findings warrant further investigation into Mithramycin-A and its specific interaction with Sp1 and their downstream targets giving a better understanding of Mithramycin-A and its potential as an effective cancer treatment.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Process Biochem Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Process Biochem Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido