Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response

Mismatch repair proteins modulate the cytotoxicity of several chemotherapeutic agents. We have recently proposed a “death conformation” of the MutS homologous proteins that is distinguishable from their “repair conformation.” This conformation can be induced by a small molecule, reserpine, leading...

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Main Authors: Aksana Vasilyeva, Jill E. Clodfelter, Michael J. Gorczynski, Anthony R. Gerardi, S. Bruce King, Freddie Salsbury, Karin D. Scarpinato
Format: Article
Language:English
Published: Wiley 2010-01-01
Series:Journal of Nucleic Acids
Online Access:http://dx.doi.org/10.4061/2010/162018
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author Aksana Vasilyeva
Jill E. Clodfelter
Michael J. Gorczynski
Anthony R. Gerardi
S. Bruce King
Freddie Salsbury
Karin D. Scarpinato
author_facet Aksana Vasilyeva
Jill E. Clodfelter
Michael J. Gorczynski
Anthony R. Gerardi
S. Bruce King
Freddie Salsbury
Karin D. Scarpinato
author_sort Aksana Vasilyeva
collection DOAJ
description Mismatch repair proteins modulate the cytotoxicity of several chemotherapeutic agents. We have recently proposed a “death conformation” of the MutS homologous proteins that is distinguishable from their “repair conformation.” This conformation can be induced by a small molecule, reserpine, leading to DNA-independent cell death. We investigated the parameters for a small reserpine-like molecule that are required to interact with MSH2/MSH6 to induce MSH2/MSH6-dependent cytotoxic response. A multidisciplinary approach involving structural modeling, chemical synthesis, and cell biology analyzed reserpine analogs and modifications. We demonstrate that the parameters controlling the induction of MSH2/MSH6-dependent cytotoxicity for reserpine-analogous molecules reside in the specific requirements for methoxy groups, the size of the molecule, and the orientation of molecules within the protein-binding pocket. Reserpine analog rescinnamine showed improved MSH2-dependent cytotoxicity. These results have important implications for the identification of compounds that require functional MMR proteins to exhibit their full cytotoxicity, which will avoid resistance in MMR-deficient cells.
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institution Kabale University
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publishDate 2010-01-01
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series Journal of Nucleic Acids
spelling doaj-art-9dcf76a2d46946c4ba5aba5171c200da2025-08-20T03:38:26ZengWileyJournal of Nucleic Acids2090-021X2010-01-01201010.4061/2010/162018162018Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic ResponseAksana Vasilyeva0Jill E. Clodfelter1Michael J. Gorczynski2Anthony R. Gerardi3S. Bruce King4Freddie Salsbury5Karin D. Scarpinato6Department of Cancer Biology, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USADepartment of Cancer Biology, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USADepartment of Chemistry, Wake Forest University, Winston-Salem, NC 27109, USADepartment of Chemistry, Wake Forest University, Winston-Salem, NC 27109, USADepartment of Chemistry, Wake Forest University, Winston-Salem, NC 27109, USADepartment of Physics, Wake Forest University, Winston-Salem, NC 27109, USADepartment of Cancer Biology, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USAMismatch repair proteins modulate the cytotoxicity of several chemotherapeutic agents. We have recently proposed a “death conformation” of the MutS homologous proteins that is distinguishable from their “repair conformation.” This conformation can be induced by a small molecule, reserpine, leading to DNA-independent cell death. We investigated the parameters for a small reserpine-like molecule that are required to interact with MSH2/MSH6 to induce MSH2/MSH6-dependent cytotoxic response. A multidisciplinary approach involving structural modeling, chemical synthesis, and cell biology analyzed reserpine analogs and modifications. We demonstrate that the parameters controlling the induction of MSH2/MSH6-dependent cytotoxicity for reserpine-analogous molecules reside in the specific requirements for methoxy groups, the size of the molecule, and the orientation of molecules within the protein-binding pocket. Reserpine analog rescinnamine showed improved MSH2-dependent cytotoxicity. These results have important implications for the identification of compounds that require functional MMR proteins to exhibit their full cytotoxicity, which will avoid resistance in MMR-deficient cells.http://dx.doi.org/10.4061/2010/162018
spellingShingle Aksana Vasilyeva
Jill E. Clodfelter
Michael J. Gorczynski
Anthony R. Gerardi
S. Bruce King
Freddie Salsbury
Karin D. Scarpinato
Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response
Journal of Nucleic Acids
title Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response
title_full Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response
title_fullStr Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response
title_full_unstemmed Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response
title_short Parameters of Reserpine Analogs That Induce MSH2/MSH6-Dependent Cytotoxic Response
title_sort parameters of reserpine analogs that induce msh2 msh6 dependent cytotoxic response
url http://dx.doi.org/10.4061/2010/162018
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