Development of decision trees to discriminate HDAC8 inhibitors and non-inhibitors using recursive partitioning

被引:16
作者
Amin, Sk Abdul [1 ]
Adhikari, Nilanjan [1 ]
Jha, Tarun [1 ]
机构
[1] Jadavpur Univ, Dept Pharmaceut Technol, Div Med & Pharmaceut Chem, Nat Sci Lab, Kolkata, India
关键词
Cancer; HDAC8; inhibitor; recursive partitioning model; molecular fingerprint; ECFP_6; FCFP_6; decision tree; HISTONE DEACETYLASE 8; CANCER; DESIGN; TARGET;
D O I
10.1080/07391102.2019.1661876
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Histone deacetylase 8 (HDAC8) is involved in malignancy. Overexpression of HDAC8 is correlated with various cancers. Design of selective HDAC8 inhibitors is always a challenging task to the chemistry audiences. In this communication, a diverse set comprising large number of compounds are subjected to recursive partitioning (RP) analysis to develop decision trees to discriminate compounds into HDAC8 inhibitors (active) and non-inhibitors (inactive). Acquiring knowledge about the essential structural and physicochemical parameters can be useful in designing potential and selective HDAC8 inhibitors. Moreover, this work validates our previous results observed in Bayesian modelling study of this dataset. This comparative learning will surely enrich drug discovery aspects related to HDAC8 inhibitors. Communicated by Ramaswamy H. Sarma
引用
收藏
页码:1 / 8
页数:8
相关论文
共 41 条
[1]  
Accelrys Inc San Diego USA, 2015, DISC STUD 3 0 DS 3 0
[2]   HDAC3 is a potential validated target for cancer: An overview on the benzamide-based selective HDAC3 inhibitors through comparative SAR/QSAR/QAAR approaches [J].
Adhikari, Nilanjan ;
Amin, Sk. Abdul ;
Trivedi, Prakruti ;
Jha, Tarun ;
Ghosh, Balaram .
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 2018, 157 :1127-1142
[3]   Robust design of some selective matrix metalloproteinase-2 inhibitors over matrix metalloproteinase-9 through in silico/fragment-based lead identification and de novo lead modification: Syntheses and biological assays [J].
Adhikari, Nilanjan ;
Halder, Amit K. ;
Mallick, Sumana ;
Saha, Achintya ;
Saha, Kishna D. ;
Jha, Tarun .
BIOORGANIC & MEDICINAL CHEMISTRY, 2016, 24 (18) :4291-4309
[4]   Histone deacetylase 8 as a novel therapeutic target in oral squamous cell carcinoma [J].
Ahn, Mee-Young ;
Yoon, Jung-Hoon .
ONCOLOGY REPORTS, 2017, 37 (01) :540-546
[5]   Structure-activity relationships of hydroxamate-based histone deacetylase-8 inhibitors: reality behind anticancer drug discovery [J].
Amin, S. K. Abdul ;
Adhikari, Nilanjan ;
Jha, Tarun .
FUTURE MEDICINAL CHEMISTRY, 2017, 9 (18) :2211-2237
[6]   Is dual inhibition of metalloenzymes HDAC-8 and MMP-2 a potential pharmacological target to combat hematological malignancies? [J].
Amin, Sic. Abdul ;
Adhikari, Nilanjan ;
Jha, Tarun .
PHARMACOLOGICAL RESEARCH, 2017, 122 :8-19
[7]   Designing potential HDAC3 inhibitors to improve memory and learning [J].
Amin, Sk. Abdul ;
Adhikari, Nilanjan ;
Jha, Tarun ;
Ghosh, Balaram .
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2019, 37 (08) :2133-2142
[8]   Diverse classes of HDAC8 inhibitors: in search of molecular fingerprints that regulate activity [J].
Amin, Sk Abdul ;
Adhikari, Nilanjan ;
Jha, Tarun .
FUTURE MEDICINAL CHEMISTRY, 2018, 10 (13) :1589-1602
[9]   Structure-activity relationships of HDAC8 inhibitors: Non-hydroxamates as anticancer agents [J].
Amin, Sk. Abdul ;
Adhikari, Nilanjan ;
Jha, Tarun .
PHARMACOLOGICAL RESEARCH, 2018, 131 :128-142
[10]   Inside HDAC with HDAC inhibitors [J].
Bertrand, Philippe .
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 2010, 45 (06) :2095-2116