Organizing co mmittee

–9.1 
–7.2 
–7.6 
–8.5 
–9.3 
G-6-O-CH
2
COOH 
–7.4 
–7.5 
–8.0 
–8.2 
–8.7 
G-6,6

-O-di-CH
2
COOH 
–7.3 
–7.5 
–7.5 
–8.0 
–8.9 
G-6-O-CH
2
CONH
2
–8.7 
–7.3 
–7.8 
–8.5 
–9.1 
G-6,6

-di-O-CH
2
CONH
2
–7.5 
–7.3 
–7.6 
–8.1 
–8.9 
The 3D structures of the proteins (or enzymes) EGFR (transferase/transferase 
inhibitor, PDB ID: 4RJ8 with resolution of 2.50 Å), HNE (hydrolase, ID: 1H1B, 2.00 
Å) and MMP 2 (gelatinase, ID: 1QIB, 2.80 Å), MMP 9 (hydrolase/hydrolase inhibitor, 
ID: 4H1Q, 1.59 Å) and Tyrosinase (oxidoreductase, ID: 2Y9W, 2.30 Å) were 
downloaded from Protein Data Bank (PDB) server.
In conclusion, gossypol derivatives have shown potential to dock with all the five 
selected proteins. The present docking investigation has shown mono-substituted alkyl 
derivatives of gossypol are exhibited lower (stronger binding) energy for selected 
enzymes than di-substituted derivatives. Gossypol exhibits lower (stronger binding) 
energy then its 
O
6-mono- and 
O
6,
O
6

-di-alkyl derivatives, exception for HNE (1H1B).
References: 
1. Y. Wang, H. Lai, X. Fan, L. Luo, F. Duan, Z. Jiang, Q. Wang, E.L.H. Leung, L. 
Liu, and X. Yao. 
Front. Pharmacol
., 2018, 
9
, 728. 
2. V. Ragavan, A. Ramesh, and R. Narayanaswamy. 
Rasayan J. Chem.
, 2020, 
13(1)
, 
469–475. 

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Poster presentation 
152