Systematic analysis of a dipeptide library for inhibitor development using human dipeptidyl peptidase IV produced by a Saccharomyces cerevisiae expression system

Biochemical and Biophysical Research Communications

Volumn 430, Issue 4, 2013, Pages 1217-1222

  Hikida, Aya ^a   Ito, Keisuke ^a,b   Motoyama, Takayasu ^b   Kato, Ryuji ^c   Kawarasaki, Yasuaki ^a  

^a UNIVERSITY OF SHIZUOKA   (Japan)

^b Fuji Oil Co Ltd   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

Author keywords

Dipeptide; Dipeptidyl peptidase IV; Incretin; Library screening; Saccharomyces cerevisiae expression system; Type 2 diabetes

Indexed keywords

AMINO ACID; DIPEPTIDE; DIPEPTIDYL PEPTIDASE IV;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; GENE EXPRESSION SYSTEM; NONHUMAN; PEPTIDE LIBRARY; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; DIABETES MELLITUS, TYPE 2; DIPEPTIDES; DIPEPTIDYL PEPTIDASE 4; DIPEPTIDYL-PEPTIDASE IV INHIBITORS; DRUG DISCOVERY; HUMANS; MOLECULAR SEQUENCE ANNOTATION; PEPTIDE LIBRARY; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 84872837670     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.12.073     Document Type: Article

References (31)

1. Mentlein R. Dipeptidyl-peptidase IV (CD26) - role in the inactivation of regulatory peptides. Regul. Pept. 1999, 85:9-24.
2. Lu M., Wheeler M.B., Leng X.H., Boyd A.E. The role of the free cytosolic calcium level in beta-cell signal transduction by gastric inhibitory polypeptide and glucagon-like peptide I(7-37). Endocrinology 1993, 132:94-100.
3. Creutzfeldt W.O., Kleine N., Willms B., Orskov C., Holst J.J., Nauck M.A. Glucagonostatic actions and reduction of fasting hyperglycemia by exogenous glucagon-like peptide I(7-36) amide in type I diabetic patients. Diabetes Care 1996, 19:580-586.
4. Drucker D.J. Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis. Mol. Endocrinol. 2003, 17:161-171.
5. Russell-Jones D., Gough S. Recent advances in incretin-based therapies. Clin. Endocrinol. (Oxf.) 2012, 77:489-499.
6. Tulipano G., Sibilia V., Caroli A.M., Cocchi D. Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 2011, 32:835-838.
7. Velarde-Salcedo A.J., Barrera-Pacheco A., Lara-González S., Montero-Morán G.M., Díaz-Gois A., González de Mejia E., et al. In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins. Food Chem. 2013, 136:758-764.
8. Kühn-Wache K., Bär J.W., Hoffmann T., Wolf R., Rahfeld J.U., Demuth H.U. Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site. Biol. Chem. 2011, 392:223-231.
9. Hu C.X., Huang H., Zhang L., Huang Y., Shen Z.F., Cheng K.D., et al. A new screening method based on yeast-expressed human dipeptidyl peptidase IV and discovery of novel inhibitors. Biotechnol. Lett. 2009, 31:979-984.
10. Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N. Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. 2003, 10:19-25.
11. Newstead S., Kim H., von Heijne G., Iwata S., Drew D. High-throughput fluorescent-based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 2007, 104:13936-13941.
12. Ito K., Sugawara T., Shiroishi M., Tokuda N., Kurokawa A., Misaka T., et al. Advanced method for high-throughput expression of mutated eukaryotic membrane proteins in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 2008, 371:841-845.
13. Ito K., Sugawara T., Koizumi A., Nakajima K., Shimizu-Ibuka A., Shiroishi M., et al. Bulky high-mannose-type N-glycan blocks the taste-modifying activity of miraculin. Biochim. Biophys. Acta 1800, 2010:986-992.
14. Ito K., Sugawara T., Koizumi A., Nakajima K., Shimizu-Ibuka A., Shiroishi M., et al. Cysteine-to-serine shuffling using a Saccharomyces cerevisiae expression system improves protein secretion: case of a nonglycosylated mutant of miraculin, a taste-modifying protein. Biotechnol. Lett. 2011, 33:103-107.
15. T. Sahara, T. Gouda, Y. Tochigi, S. Ohgiya, A highly efficient secretory signal peptide and a protein expression system using the peptide thereof, European Patent: EP1790661, 2007.
16. Cheng Y., Prusoff W.H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol. 1973, 22:3099-3108.
17. Kawashima S., Pokarowski P., Pokarowska M., Kolinski A., Katayama T., Kanehisa M. AAindex: amino acid index database, progress report. Nucleic Acids Res. 2008, 36(2008):202-205.
18. Zimmerman J.M., Eliezer N., Simha R. The characterization of amino acid sequences in proteins by statistical methods. J. Theor. Biol. 1968, 21:170-201.
19. Fauchere J.L., Charton M., Kier L.B., Verloop A., Pliska V. Amino acid side chain parameters for correlation studies in biology and pharmacology. Int. J. Pept. Protein Res. 1988, 32:269-278.
20. Geisow M.J., Robert R.D.B. Amino acid preferences for secondary structure vary with protein class. Int. J. Biol. Macromol. 1980, 2:387-389.
21. Takano K., Yutani K. A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins. Protein Eng. 2001, 14:525-528.
22. Zhou H., Zhou Y. Quantifying the effect of burial of amino acid residues on protein stability. Proteins 2004, 54:315-322.
23. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157:105-132.
24. Crawford J.L., Lipscomb W.N., Schellman C.G. The reverse turn as a polypeptide conformation in globular proteins. Proc. Natl. Acad. Sci. USA 1973, 70:538-542.
25. Munoz V., Serrano L. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales. Proteins 1994, 20:301-311.
26. Krigbaum W.R., Komoriya A. Local interactions as a structure determinant for protein molecules: II. Biochim. Biophys. Acta 1979, 576:204-248.
27. Jukes T.H., Holmquist R., Moise H. Amino acid composition of proteins: selection against the genetic code. Science 1975, 189:50-51.
28. West R.W., Crivellone M.D., Ma J., Thomas S. Sequence of the Saccharomyces cerevisiae YTP1 gene encoding a deduced novel type-III integral membrane protein with domains of sequence similarity to mitochondrial electron-transport enzymes. Gene 1996, 169:119-124.
29. Kimata K., Yamaguchi M., Saito Y., Hata H., Miyake K., Yamane T., et al. High cell-density expression system: a novel method for extracellular production of difficult-to-express proteins. J. Biosci. Bioeng. 2012, 113:154-159.
30. Weihofen W.A., Liu J., Reutter W., Saenger W., Fan H. Crystal structures of HIV-1 Tat-derived nonapeptides Tat-(1-9) and Trp2-Tat-(1-9) bound to the active site of dipeptidyl-peptidase IV (CD26). J. Biol. Chem. 2005, 280:14911-14917.
31. Abbott C.A., McCaughan G.W., Gorrell M.D. Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity. FEBS Lett. 1999, 458:278-284.