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Structure-based design of new poly (ADP-ribose) polymerase (PARP-1) inhibitors.
Mol Divers. 2017 Aug; 21(3):655-660.MD

Abstract

Poly (ADP-ribose) polymerase (PARP-1) is a well-established nuclear protein with prominent role in signaling and DNA repair. Various clinical candidates have been identified with the role in PARP-1 inhibition. Based on the pharmacophoric features identified from previous studies and molecular docking interactions, thiazolidine-2,4-dione derivatives have been evaluated for their PARP inhibitory activity. From an in vitro assay, 5-((1-(4-isopropylbenzyl)-1H-indol-3-yl)methylene)thiazolidine-2,4-dione (16) was identified as a potent inhibitor having low micromolar inhibitory activity [Formula: see text]. Thus, a structure-based design approach utilized in the present study helped to identify thiazolidine-2,4-dione as a novel scaffold against PARP-1 for potential development of potent anticancer therapeutics.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Chadha N
Molecular Modeling Lab (MML), Department of Pharmaceutical Sciences and Drug Research, Punjabi University, Patiala, 147002, Punjab, India.
Jaggi AS
Department of Pharmaceutical Sciences and Drug Research, Punjabi University, Patiala, 147002, India.
Silakari O
Molecular Modeling Lab (MML), Department of Pharmaceutical Sciences and Drug Research, Punjabi University, Patiala, 147002, Punjab, India. omsilakari@gmail.com.

MeSH

Catalytic DomainDrug DesignHumansModels, MolecularMolecular Docking SimulationPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsStructure-Activity RelationshipThiazolidinediones

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28653128

Citation

Chadha, Navriti, et al. "Structure-based Design of New Poly (ADP-ribose) Polymerase (PARP-1) Inhibitors." Molecular Diversity, vol. 21, no. 3, 2017, pp. 655-660.
Chadha N, Jaggi AS, Silakari O. Structure-based design of new poly (ADP-ribose) polymerase (PARP-1) inhibitors. Mol Divers. 2017;21(3):655-660.
Chadha, N., Jaggi, A. S., & Silakari, O. (2017). Structure-based design of new poly (ADP-ribose) polymerase (PARP-1) inhibitors. Molecular Diversity, 21(3), 655-660. https://doi.org/10.1007/s11030-017-9754-7
Chadha N, Jaggi AS, Silakari O. Structure-based Design of New Poly (ADP-ribose) Polymerase (PARP-1) Inhibitors. Mol Divers. 2017;21(3):655-660. PubMed PMID: 28653128.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure-based design of new poly (ADP-ribose) polymerase (PARP-1) inhibitors. AU - Chadha,Navriti, AU - Jaggi,Ameteshar Singh, AU - Silakari,Om, Y1 - 2017/06/26/ PY - 2016/10/14/received PY - 2017/05/27/accepted PY - 2017/6/28/pubmed PY - 2018/7/14/medline PY - 2017/6/28/entrez KW - Docking KW - Indole KW - Molecular modeling KW - PARP KW - Structure-based drug design KW - Thiazolidine-2,4-dione SP - 655 EP - 660 JF - Molecular diversity JO - Mol Divers VL - 21 IS - 3 N2 - Poly (ADP-ribose) polymerase (PARP-1) is a well-established nuclear protein with prominent role in signaling and DNA repair. Various clinical candidates have been identified with the role in PARP-1 inhibition. Based on the pharmacophoric features identified from previous studies and molecular docking interactions, thiazolidine-2,4-dione derivatives have been evaluated for their PARP inhibitory activity. From an in vitro assay, 5-((1-(4-isopropylbenzyl)-1H-indol-3-yl)methylene)thiazolidine-2,4-dione (16) was identified as a potent inhibitor having low micromolar inhibitory activity [Formula: see text]. Thus, a structure-based design approach utilized in the present study helped to identify thiazolidine-2,4-dione as a novel scaffold against PARP-1 for potential development of potent anticancer therapeutics. SN - 1573-501X UR - https://www.unboundmedicine.com/medline/citation/28653128/Structure_based_design_of_new_poly__ADP_ribose__polymerase__PARP_1__inhibitors_ DB - PRIME DP - Unbound Medicine ER -