Curcumin analogues were evaluated for COX-2 inhibitory as anti-inflammatory activities. The designed analogues significantly enhance COX-2 selectivity. The three compounds could dock into the active site of COX-2 successfully. The binding energies of -8.2, - 7.6 and -7.5 kcal/mol were obtained for three analogues of curcumin respectively. Molecular docking study revealed the binding orientations of curcumin analogues in the active sites of COX-2 towards the design of potent inhibitors.

The synthesis of chalcone derivatives as target compounds and anticancer test against breast (T47D) and colon (WiDr) cell line had been performed. The synthesis was performed by Claisen-Schmidt condensation by using acetophenone and benzaldehyde derivatives. The anticancer activity test of chalcone derivatives was carried out by MTT assay against T47D and WiDr cell lines. The synthesis was started by reacting 4-hydroxyacetophenone and benzaldehyde derivatives such as p-anisaldehyde (chalcone A [(E)-4'-hydroxy-4-methoxychalcone]), veratraldehyde (chalcone B [(E)-4'-hydroxy-3,4-dimethoxychalcone]), 4-chlorobenzaldehyde (chalcone C [(E)-4'-hydroxy-4-chlorochalcone]) and 2,4-dihydroxyacetophenone with 4-chlorobenzaldehyde (chalcone D [(E)-2',4'-dihydroxy-4-chlorochalcone]) in methanol as solvent. The synthesis was carried out in alkaline condition (KOH) by stirring the mixture at room temperature for 48 h. The structures of products were identified by FTIR, GC-MS, 1H- and 13C-NMR spectrometers. The results showed that the chalcone derivatives (A-D) were yielded in 96; 97; 96; and 93%, respectively as yellow solid. The anticancer test indicated that the chalcone D was the most active towards T47D cell line with IC50 of 42.66 μg/mL and the chalcone C was the most active against WiDr cell line with IC50 of 20.42 μg/mL.

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Antimicrobial peptide (AMP) peptide-based lead compound has become interesting target in developing new antibiotics. AMP is possibly generated through the digestion of protein. The protein of castor (Ricinus communis) seed is characterized as a ribosome-inactivating protein (RIP) that can be a source of AMP. The objectives of this research are to identify antibacterial peptides from Ricinus communis seed protein hydrolysate.   The seed protein was isolated using sodium dodecyl sulfate and subsequently digested using trypsin. The hydrolysate was fractionated using a strong cation exchange chromatography system, and the resulting fractions were tested for antibacterial activity. The peptides present in the active fraction were identified using high-resolution mass spectrometry. As the result, the pH 4 and pH 5 fractions of the elution buffer indicated antibacterial activity, with the pH 4 fraction of the hydrolysate having high activity against both gram-negative (Escherichia coli) and gram-positive (Staphylococcus aureus) bacteria. Three peptides that have the sequences EESETVGQR, GQSTGTGQQER, and LDALEPDNR could be responsible for the activity of the pH 4 fraction. The antibacterial activity of these peptides, which is due to their ionic properties and secondary structure, supports the disruption of the bacterial cell membrane. It can be concluded that Ricinus communis seed protein hydrolysate contains peptides with sequence EESETVGQR, GQSTGTGQQER, and LDALEPDNR that potent to be used as AMP lead compounds

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