SOYBEAN AND HEALTH - University of Macau Library

Fermented Soybean Products and Their Bioactive Compounds 47Peptide sequence Peptide fragment IC 50 (μM)1 2 3 4 5Control aLPYP LPYP 484.72IAVPGEVA IAVP AVPG VPGE PGEV GEVA 201.12IAVPTGVA IAVP AVPT VPTG PTGV TGVA 152.19Set 1 bGLPTGG GLPT LPTG PTGG 19.43GLPDGG GLPD LPDG PDGG 22.31GLPEGG GLPE LPEG PEGG 27.28GFPTGG GFPT FPTG PTGG 16.94GFPDGG GFPD FPDG PDGG 1.52GFPEGG GFPE FPEG PEGG 1.78GXPTGG d GXPT d XPTG d PTGG 4.82GXPDGG d GXPD d XPDG d PDGG 6.95GXPEGG d GXPE d XPEG d PEGG 0.75GXPGGG d Negative control InactiveSet 2 cIAVE IAVE 75.23IVAE IVAE 52.67YAVE YAVE 44.81YVAE YVAE 41.21FFYVAE FFYV FYVA YVAE 2.56FPYVAE FPYV PYVA YVAE 1.47FGYVAE FGYV GYVA YVAE 0.41XVAE d XVAE d 3.84FGXVAE d FGXV d GXVA d XVAE d 8.52GFGYVAE GFGY FGYV GYVA YVAE 0.27TFGYVAE TFGY FGYV GYVA YVAE 0.26DFGYVAE DFGY FGYV GYVA YVAE 0.16EFGYVAE EFGY FGYV GYVA YVAE 0.24DFGYVAG Negative control Inactivea ‘Control’ contains the peptides isolated from soy protein (Kwon et al, 2002; Pak et al., 2005b, c).b ‘Set 1’ contains the peptides, which includes the recognized T, D or E residue as a corner residue of theβ-turn structure (Pak et al., 2007, 2008a).c ‘Set 2’ contains the peptides, where the E residue is a recognized residue for the HMG-binding pocket,and a β-turn structure is located in the N-terminus of the hexapeptides (Pak et al., 2008b).dThe substituted (4-fluoro)phenylalanine residue is indicated as ‘X‘.Table 9. Peptide sequence, peptide fragment, and inhibitory activities (IC 50 ) of thesynthesized peptides (Pak et al., 2010).space that was occupied by a peptide by using peptide fragments. In order to assess theproposed method, a competitive inhibitor for HMGR was designed by using two startingpoints: (1) determined recognition residues and (2) the structural preference of a peptide,such as a β-turn conformation in the present design. For testing the proposed design, 13