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This study examined the presence of antioxidant, mineral binder and antimicrobial peptides in traditional Turkish goat and cow milk Tulum cheeses. Water soluble extracts (WSE) were extracted from these cheeses at ripening periods (0, 15, 30, 60, 90 and 120 days). WSEs of these cheeses were subjected to reverse-phase HPLC. The highest amounts of peptides (>500 mAU) were at 120th ripening period in both cheeses. Results of DPPH and ABTS demonstrated that the antioxidant activity increased with ripening periods for these cheeses. While no differences were observed between these cheeses in DPPH assay, the highest antioxidant activity was observed in cow milk Tulum cheese at 90th and 120th days in ABTS assay. The highest Iron(II) binding activity was determined in goat milk Tulum cheese at 60th day. WSE obtained from goat milk Tulum cheese at 90th day demonstrated inhibitory effect against Salmonella typhimurium ATTC 14028. [ABSTRACT FROM AUTHOR]

In search for the important residues that might have involve in the binding interaction between the p24 caspid protein of HIV-1 fragment (MET68 - PRO90) with the single chain fragment variable (scFv) of FAB23.5, modern computational chemistry approach has been conducted and applied. The p24 fragment was initially taken out from the 1AFV protein molecule consisting of both light (VL) and heavy (VH) chains of FAB23.5 as well as the HIV-1 caspid protein. From there, the p24 (antigen) fragment was made to dock back into the protein pocket receptor (antibody) by using the CDOCKER algorithm to conduct the molecular docking process. The score calculated from the CDOCKER gave 15 possible docked poses with various docked ligand's positions, the interaction energy as well as the binding energy. The best docked pose that imitates the original antigen's position was determined and further processed to the In Situ minimization to obtain the residues interaction energy as well as to observe the hydrogen bonds interaction in the protein-peptide complex. Based on the results demonstrated, the specific residues in the complex that have shown immense lower interaction energies in the 5Å vicinity region from the peptide are from the heavy chain (VH:TYR105) and light chain (VL: ASN31, TYR32, and GLU97). Those residues play vital roles in the binding mechanism of Antibody- Antigen (Ab-Ag) complex of p24 with FAB23.5. [ABSTRACT FROM AUTHOR]