The effect of protein mutations on drug binding suggests ensuing personalised drug selection [electronic resource]

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Tác giả:

Ngôn ngữ: eng

Ký hiệu phân loại: 574.8 [Unassigned]

Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2021

Mô tả vật lý: Size: Article No. 13452 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 259663

The advent of personalised medicine promises a deeper understanding of mechanisms and therefore therapies. However, the connection between genomic sequences and clinical treatments is often unclear. We studied 50 breast cancer patients belonging to a population-cohort in the state of Qatar. From Sanger sequencing, we identified several new deleterious mutations in the estrogen receptor 1 gene (ESR1). The effect of these mutations on drug treatment in the protein target encoded by ESR1, namely the estrogen receptor, was achieved via rapid and accurate protein?ligand binding affinity interaction studies which were performed for the selected drugs and the natural ligand estrogen. Four nonsynonymous mutations in the ligand-binding domain were subjected to molecular dynamics simulation using absolute and relative binding free energy methods, leading to the ranking of the efficacy of six selected drugs for patients with the mutations. Our study shows that a personalised clinical decision system can be created by integrating an individual patient?s genomic data at the molecular level within a computational pipeline which ranks the efficacy of binding of particular drugs to variant proteins.
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