Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups
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Приказ свих података о документуАпстракт
The binding site of the second catalytic domain of human histone deacetylase 6 (HDAC6 CDII) has structural features that differ from the other human orthologues, being also mainly responsible for the overall enzymatic activity of this isoform. Aiming to identify new fragments as a possible novel selective zinc binding group (ZBG) for HDAC6 CDII, two fragment libraries were designed: one library consisting of known chelators and a second one using the fragments of the ZINC15 database. The most promising fragments identified in a structure-based virtual screening of designed libraries were further evaluated through molecular docking and molecular dynamics simulations. An interesting benzimidazole fragment was selected from the in silico studies and presented as potential zing binding group for the development of novel HDAC6 selective inhibitors.
Кључне речи:
Histone deacetylase / fragment-based drug design / molecular docking / epigenetics / zinc binding groupИзвор:
Journal of Biomolecular Structure and Dynamics, 2019, 38, 11Издавач:
- Taylor & Francis
Финансирање / пројекти:
- Синтеза, квантитативни однос између структуре и дејства, физичко-хемијска карактеризација и анализа фармаколошки активних супстанци (RS-MESTD-Basic Research (BR or ON)-172033)
Напомена:
- This is peer-reviewed version of the following article:Alves Avelar, L. A.; Ruzic, D.; Djokovic, N.; Kurz, T.; Nikolic, K. Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups. J. Biomol. Struct. Dyn. 2020, 38 (11), 3166–3177. https://doi.org/10.1080/07391102.2019.1652687
Повезане информације:
- Повезани садржај
https://doi.org/10.1080/07391102.2019.1652687
DOI: 10.1080/07391102.2019.1652687
ISSN: 0739-1102
PubMed: 31382868
WoS: 000481595300001
Scopus: 2-s2.0-85070913828
Институција/група
PharmacyTY - JOUR AU - Alves Avelar, Leandro AU - Ružić, Dušan AU - Đoković, Nemanja AU - Kurz, Thomas AU - Nikolić, Katarina PY - 2019 UR - https://farfar.pharmacy.bg.ac.rs/handle/123456789/4909 AB - The binding site of the second catalytic domain of human histone deacetylase 6 (HDAC6 CDII) has structural features that differ from the other human orthologues, being also mainly responsible for the overall enzymatic activity of this isoform. Aiming to identify new fragments as a possible novel selective zinc binding group (ZBG) for HDAC6 CDII, two fragment libraries were designed: one library consisting of known chelators and a second one using the fragments of the ZINC15 database. The most promising fragments identified in a structure-based virtual screening of designed libraries were further evaluated through molecular docking and molecular dynamics simulations. An interesting benzimidazole fragment was selected from the in silico studies and presented as potential zing binding group for the development of novel HDAC6 selective inhibitors. PB - Taylor & Francis T2 - Journal of Biomolecular Structure and Dynamics T1 - Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups VL - 38 VL - 3166 VL - 3177 IS - 11 DO - 10.1080/07391102.2019.1652687 ER -
@article{ author = "Alves Avelar, Leandro and Ružić, Dušan and Đoković, Nemanja and Kurz, Thomas and Nikolić, Katarina", year = "2019", abstract = "The binding site of the second catalytic domain of human histone deacetylase 6 (HDAC6 CDII) has structural features that differ from the other human orthologues, being also mainly responsible for the overall enzymatic activity of this isoform. Aiming to identify new fragments as a possible novel selective zinc binding group (ZBG) for HDAC6 CDII, two fragment libraries were designed: one library consisting of known chelators and a second one using the fragments of the ZINC15 database. The most promising fragments identified in a structure-based virtual screening of designed libraries were further evaluated through molecular docking and molecular dynamics simulations. An interesting benzimidazole fragment was selected from the in silico studies and presented as potential zing binding group for the development of novel HDAC6 selective inhibitors.", publisher = "Taylor & Francis", journal = "Journal of Biomolecular Structure and Dynamics", title = "Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups", volume = "38, 3166, 3177", number = "11", doi = "10.1080/07391102.2019.1652687" }
Alves Avelar, L., Ružić, D., Đoković, N., Kurz, T.,& Nikolić, K.. (2019). Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups. in Journal of Biomolecular Structure and Dynamics Taylor & Francis., 38(11). https://doi.org/10.1080/07391102.2019.1652687
Alves Avelar L, Ružić D, Đoković N, Kurz T, Nikolić K. Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups. in Journal of Biomolecular Structure and Dynamics. 2019;38(11). doi:10.1080/07391102.2019.1652687 .
Alves Avelar, Leandro, Ružić, Dušan, Đoković, Nemanja, Kurz, Thomas, Nikolić, Katarina, "Structure-Based Design of Selective Histone Deacetylase 6 Zinc Binding Groups" in Journal of Biomolecular Structure and Dynamics, 38, no. 11 (2019), https://doi.org/10.1080/07391102.2019.1652687 . .