Bioactive Salen-type Schiff Base Transition Metal Complexes as Possible Anticancer Agents

被引:5
作者
Damercheli, Maryam [1 ]
Behzad, Mandi [1 ]
Mehravi, Bita [2 ]
Ardestani, Mehdi Shafiee [3 ]
机构
[1] Semnan Univ, Fac Chem, Dept Inorgan Chem, Semnan, Iran
[2] Iran Univ Med Sci, Fac Adv Technol Med, Dept Med Nanotechnol, Tehran, Iran
[3] Univ Tehran Med Sci, Fac Pharm, Dept Radiopharm, Tehran, Iran
来源
IRANIAN JOURNAL OF PHARMACEUTICAL RESEARCH | 2019年 / 18卷 / 04期
关键词
Histone deacetylase; Anticancer; Schiff base; Docking; COPPER(II) COMPLEXES; GOLD(I) COMPLEXES; PROTEIN-KINASE; DNA; MECHANISM; INHIBITION; ALBUMIN;
D O I
10.22037/ijpr.2019.12792.11151
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Although metal-based anticancer drugs have been recognized as the most effective agents over the organic compounds, non-selectivity and high toxic effects have limited their applications in a way that only three Pt-analogues have progressed into clinical use. These problems have spurred chemists to develop different strategics based on alternative targets. This work focuses on predicting potency and mode of interactions of a series of salen type Schiff base transition metal complexes derived from meso-1,2-diphenyl-1,2-ethylenediamine, over some proteins (HDAC7, HDAC2, CatB, B-RAF kinase, TopII, RNR, TS, and rHA) using computational docking method, to be later considered as possible anticancer agents. The obtained results showed that all complexes exhibited higher affinity for HDAC7 than the other targets. Moreover, the bromo-derivatives of the copper compounds were more active on HDAC7 than the other derivatives. Such bromo compounds showed considerable interactions with Kinase, RNR, TS, and CatB. Contrary to Histone deacetylase (HAD)C7; HDAC2 was predicted to be relatively poor target. As expected, formation of the hydrophobic interactions between the metal complexes and the protein targets were essential for activity of the metal compounds. This study provides some more information for further optimizations and development of new metallodrugs as enzyme inhibitors for potential therapeutic agents.
引用
收藏
页码:2055 / 2066
页数:12
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