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Supplementary material
Biological Features, Drug-likeness, Pharmacokinetic Properties, and Docking
of 2-Arylidenehydrazinyl-4-arylthiazole Analogues
Mohammad Sayed Alam1 ⋅ Junaid Uddin Ahmed2 ⋅ Dong-Ung Lee1,*
1
Division of Bioscience, Dongguk University, Gyeongju 780-714, Republic of Korea
2
Department of Chemistry, Jagannath University, Dhaka 1100, Bangladesh
(A)
(B)
(C)
(D)
ALA246
ALA246
5.38
2.10
GLY152
MET207
ALA246
VAL212
VAL212
ILE156
ALA216
ALA216
ALA216
MET207
ILE156
2.99
GLY209
VAL212
MET207
ILE156
GLY209
GLY209
5.17
TRP32
TRP32
TRP32
Fig. 1 (A) Binding model of compound 3c into E. coli FabH (Protein Data Bank entry: 1HNJ).
The green dotted lines show the hydrogen bond, the blue dotted lines show -alkyl interactions,
and the yellow dotted lines show -sulfur interactions. (B) 2D ligand interaction diagram with E.
coli FabH using Discovery Studio program with the essential amino acid residues at the binding
site are tagged in circles. The purple circles show the amino acids which involve in electrostatic
and covalent interactions and the green circles show the amino acids which participate in the van
der Waals interactions. (C) Hydrogen bond interaction showing donor (pink) and acceptor
surfaces (green). (D) Hydrophobic interaction showing hydrophobic surface (brown)
(A)
ALA246
(B)
(C)
(D)
ALA246
PHE213
ALA246
PHE213
PHE213
4.26
3.07
ASN247
ASN247
2.21
2.03
GLY209 5.09
5.49
GLY209
GLY209
ILE156
ILE156
MET207
ASN247
MET207
ILE156
MET207
4.82
ARG151
ARG151
ARG151
Fig. 2 (A) Binding model of compound 3j into E. coli FabH (Protein Data Bank entry: 1HNJ).
The green dotted lines show the hydrogen bond, the blue dotted lines show -alkyl interactions,
and the yellow dotted lines show -sulfur interactions. (B) 2D ligand interaction diagram with E.
coli FabH using Discovery Studio program with the essential amino acid residues at the binding
site are tagged in circles. The purple circles show the amino acids which involve in electrostatic
and covalent interactions and the green circles show the amino acids which participate in the van
der Waals interactions. (C) Hydrogen bond interaction showing donor (pink) and acceptor
surfaces (green). (D) Hydrophobic interaction showing hydrophobic surface (brown)
(A)
(B)
(C)
Fig. 3 Energy map of compound 3c into the binding site E. coli FabH. (A) The green, red and
blue color regions are energetically favorable for steric, negative electrostatic and positive
electrostatic interactions, respectively. (B) The yellow and cyan color regions are energetically
favorable for H-bond donor and acceptor interactions, respectively. (C) Pharmacophore model of
protein-ligand interactions
(A)
(B)
(C)
Fig. 4 Energy map of compound 3j into the binding site E. coli FabH. (A) The green, red and
blue color regions are energetically favorable for steric, negative electrostatic and positive
electrostatic interactions, respectively. (B) The yellow and cyan color regions are energetically
favorable for H-bond donor and acceptor interactions, respectively. (C) Pharmacophore model of
protein-ligand interactions
(A)
(B)
(C)
(D)
(E)
(F)
Fig. 5 Field patterns and physicochemical properties of compound 3c. (A) The cyan, red, yellow,
gold points indicating negative, positive, surface and hydrophobic fields, respectively which are
potentially involve in the interactions. (B) White smoke areas indicates solvent-accessible
surface. (C) Positive field (red color) points like to interact with negatives/H-bond acceptors on a
protein receptor. (D) Negative field (cyan color) points like to interact with positives/H-bond
donors on a protein receptor. (E) van der Waals surface filed (yellow color) points involve in the
vdW interactions. (F) Hydrophobic field (gold color) points describing the regions with high
polarizability/hydrophobicity
(A)
(D)
(B)
(E)
(C)
(F)
Fig. 6 Field patterns and physicochemical properties of compound 3j. (A) The cyan, red, yellow,
gold points indicating negative, positive, surface and hydrophobic fields, respectively which are
potentially involve in the interactions. (B) White smoke areas indicates solvent-accessible
surface. (C) Positive field (red color) points like to interact with negatives/H-bond acceptors on a
protein receptor. (D) Negative field (cyan color) points like to interact with positives/H-bond
donors on a protein receptor. (E) van der Waals surface filed (yellow color) points involve in the
vdW interactions. (F) Hydrophobic field (gold color) points describing the regions with high
polarizability/hydrophobicity.