The Effect of Geometrical Isomerism of 3,5-Dicaffeoylquinic Acid on Its Binding Affinity to HIV-Integrase Enzyme: A Molecular Docking Study

Table 1

The relative energies for the 3,5-diCQA geometrical isomers and the results from the rigid docking studies with the HIV-1 integrase enzyme.

Isomer	Relative energy (kcal/mol)	Free binding energy (kcal/mol)	Contacting residues	H-bonded residues
3^trans,5^trans-diCQA	1.758	−9.332	ASP64 CYS65 THR66 HIS67 VAL72 ALA91 GLU92 ASP116 ASN117 GLN148 ILE151 GLU152 ASN155 LYS156	CYS65 HIS67 GLU152 ASN155
3^cis,5^trans-diCQA,	1.320	−8.837	ASP64 CYS65 GLU 92 THR 115 ASP116 PHE139 ILE141 GLN148 ILE151 GLU152 ASN155 LYS156 MG1001	CYS65 THR66 ASN117 GLU152
3^trans,5^cis-diCQA	0.000	−9.173	ASP64 THR66 HIS67 ASP116 GLN148 ILE151 GLU152 ASN155 LYS156 LYS159 LYS160	ASP64 GLU92 SER119 GLN148
3^cis,5^cis-diCQA	5.096	−9.082	ASP64 CYS65 THR66 HIS67 VAL72 ALA91 GLU92 ASP116 GLY118 GLN148 ILE151 GLU152 ASN155 MG1001	ASP64 THR66 HIS67 GLN148

Divalent magnesium ion.