Abstract
Histone deacetylases2, Class 1 HDAC family are emerged as an important therapeutic target for the treatment of various cancers. HDAC2 inhibitors are potent anti-cancer agents. Two inhibitors of HDAC2 are hydroxamic acid and valporic acid which are potent inducers of growth arrest, differentiation, and/or apoptotic cell death. Total 34 ligands optimized using triazole group substitution for the target protein Histone deacetylase2 on the basis of SAHA and valporic acid. All the ligands are docked with the target protein and results are compared with test compound SAHA. Eight ligands showed better binding affinity towards HDAC2.The binding affinity, free energy and drug scan screening of the above eight ligands have shown that P2, P6 and V6 molecules are best suitable to inhibit HDAC2.
Highlights
HDACs are the enzyme deacetylating the ε-amino groups of lysine located near the amino termini of core histone proteins (Mai et al, 2002 and Monneret, 2005)
SAHA hydrophobic group with triazole linked with sulfur bond and styrene group conduct molecular docking with HDAC2, and testing its drug score and toxicity using computational tools, and compare the result with standard SAHA inhibitor
The hydrophobic tendency of triazole compared with the amide group on SAHA was expected to increase the binding affinity of modified ligands toward HDAC2
Summary
HDACs are the enzyme deacetylating the ε-amino groups of lysine located near the amino termini of core histone proteins (Mai et al, 2002 and Monneret, 2005). In silco studies on modified hydroxamic acid and valporic acid as potential inhibitors for HDAC2. All the ligands are docked with the target protein and results are compared with test compound SAHA.
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