Structure-Based Design, Docking and Binding Free Energy Calculations of A366 Derivatives as Spindlin1 Inhibitors

Structure-Based Design, Docking and Binding Free Energy Calculations of A366 Derivatives as Spindlin1 Inhibitors

The chromatin reader protein Spindlin1 plays an important role in epigenetic regulation, through which it has been linked to several types of malignant tumors. In the current work, we report on the development of novel analogs of the previously published lead inhibitor <b>A366</b>. In an...

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Bibliographic Details
Main Authors: Chiara Luise, Dina Robaa, Pierre Regenass, David Maurer, Dmytro Ostrovskyi, Ludwig Seifert, Johannes Bacher, Teresa Burgahn, Tobias Wagner, Johannes Seitz, Holger Greschik, Kwang-Su Park, Yan Xiong, Jian Jin, Roland Schüle, Bernhard Breit, Manfred Jung, Wolfgang Sippl
Format: Article
Language:English
Published: MDPI AG 2021-05-01
Series:International Journal of Molecular Sciences
Subjects:
Spindlin1
structure–activity relationship (SAR)
docking
molecular dynamics (MD) simulations
MM-GBSA
Online Access:https://www.mdpi.com/1422-0067/22/11/5910

Internet

https://www.mdpi.com/1422-0067/22/11/5910

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