MOLECULAR DOCKING STUDIES OF N-(2-BENZOYLPHENYL)-L-TYROSINE DERIVATIVES WITH ANTI-DIABETIC ACTIVITY OF TYPE 2 DIABETES
TABLE 1: VARIOUS SUBSTITUTENTS ATTACHED TO BASIC STRUCTURE OFN-(2-BENZOYLPHENYL)-L-TYROSINES.
RESULTS AND DISCUSSION
Glide dock is used to study the docking molecules within the active site region of protein 3ETO and number of H-bond and amino acid involved in H-bond were determined. Docking studies may help elucidating the mechanism of PPARγ receptor-ligand interactions. Key feature of the modeling results include logical interaction of the ligand with the putative binding site of the receptor. The binding pocket within the PPARγ receptor is formed by Glu 295, Arg 288, Ser 302, Asp 381, Leu330 and Leu 333. Some of the newly designed molecules have glide score more than -7.029, which is the glide score of Pioglitazone. Hence further proof was provided by plotting a graph between experimental values and glide score, where it is clear that they represented a correlation of 0.634. Glide score and number of hydrogen bond interaction and hydrogen bond length of the docked ligand are shown in the Table 2. The docking study reveals following information with respect to N-(2-benzoylphenyl)-l-tyrosines derivatives.
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