The bioactive conformation of glucose-dependent insulinotropic polypeptide by NMR and CD spectroscopy

Proteins: Structure, Function and Genetics

Volumn 68, Issue 1, 2007, Pages 92-99

  Alaña, Iñigo ^a   Malthouse, J Paul G ^a   O'Harte, Finbarr P M ^b   Hewage, Chandralal M ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

^b UNIVERSITY OF ULSTER   (United Kingdom)

Author keywords

CD; Gastric inhibitory polypeptide; GIP; Molecular modeling; NMR; Protein structure; Solution structure; Type 2 diabetes

Indexed keywords

EXENDIN 4; GASTRIC INHIBITORY POLYPEPTIDE; GASTROINTESTINAL HORMONE; GLUCAGON; INCRETIN; INSULIN; TRIFLUOROETHANOL;

ARTICLE; BIOLOGICAL ACTIVITY; CIRCULAR DICHROISM; HORMONE ACTION; HYDROPHILICITY; INSULIN RELEASE; MOLECULAR MODEL; NON INSULIN DEPENDENT DIABETES MELLITUS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE ALIGNMENT;

CIRCULAR DICHROISM; GASTRIC INHIBITORY POLYPEPTIDE; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; TRIFLUOROETHANOL;

EID: 34249932868     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21372     Document Type: Article

References (49)

1. Meier JJ, Nauck MA, Schmidt WE, Gallwitz B. Gastric inhibitory polypeptide: the neglected incretin revisited. Regul Pept 2002;107:1-13.
2. Gault VA, O'Harte FP, Harriott P, Mooney MH, Green BD, Flatt PR. Effects of the novel (Pro3) GIP antagonist and exendin (9-39)amide on GIP- and GLP-1-induced cyclic AMP generation, insulin secretion and postprandial insulin release in obese diabetic (ob/ob) mice: evidence that GIP is the major physiological incretin. Diabetologia 2003;46:222-230.
3. Amiranoff B, Vauclin-Jacques N, Laburthe M. Functional GIP receptors in a hamster pancreatic β cell line, In 111: specific binding and biological effects. Biochem Biophys Res Commun 1984;123:671-676.
4. Rossowski WJ, Zacharia S, Mungan Z, Ozmen V, Ertan A, Baylor LM, Jiang NY, Coy DH. Reduced gastric acid inhibitory effect of a pGIP(1-30) NH2 fragment with potent pancreatic amylase inhibitory activity. Regul Pept 1992;39:9-17.
5. Usdin TB, Mezey E, Button DC, Brownstein MJ, Bonner TI. Gastric inhibitory polypeptide receptor, a member of the secretin-vasoactive intestinal peptide receptor family, is widely distributed in peripheral organs and the brain. Endocrinology 1993;133:2861-2870.
6. Gault VA, Flatt PR, O'Harte FP. Glucose-dependent insulinotropic polypeptide analogues and their therapeutic potential for the treatment of obesity-diabetes. Biochem Biophys Res Commun 2003;308:207-213.
7. Carlquist M, Kaiser R, Tatemoto K, Jornvall H, Mutt V. A novel form of the polypeptide PHI isolated in high yield from bovine upper intestine. Relationships to other peptides of the glucagon-secretin family. Eur J Biochem 1984;144:243-247.
8. Maletti M, Altman JJ, Hoa DH, Carlquist M, Rosselin G. Evidence of functional gastric inhibitory polypeptide (GIP) receptors in human insulinoma. Binding of synthetic human GIP 1-31 and activation of adenylate cyclase. Diabetes 1987;36:1336-1340.
9. Maletti M, Carlquist M, Portha B, Kergoat M, Mutt V, Rosselin G. Structural requirements for gastric inhibitory polypeptide (GIP) receptor binding and stimulation of insulin release. Peptides 1986;7(Suppl 1):75-78.
10. Gelling RW, Wheeler MB, Xue J, Gyomorey S, Nian C, Pederson RA, McIntosh CH. Localization of the domains involved in ligand binding and activation of the glucose-dependent insulinotropic polypeptide receptor. Endocrinology 1997;138:2640-2643.
11. Hinke SA, Manhart S, Pamir N, Demuth H, R WG, Pederson RA, McIntosh CH. Identification of a bioactive domain in the amino-terminus of glucose-dependent insulinotropic polypeptide (GIP). Biochim Biophys Acta 2001;1547:143-155.
12. Gault VA, Irwin N, Harriott P, Flatt PR, O'Harte FP. DPP IV resistance and insulin releasing activity of a novel di-substituted analogue of glucose-dependent insulinotropic polypeptide, (Ser2-Asp13)GIP Cell Biol Int 2003;27:41-46.
13. O'Harte FP, Gault VA, Parker JC, Harriott P, Mooney MH, Bailey CJ, Flatt PR. Improved stability, insulin-releasing activity and antidiabetic potential of two novel N-terminal analogues of gastric inhibitory polypeptide: N-acetyl-GIP and pGlu-GIP. Diabetologia 2002;45:1281-1291.
14. Hopp TP, Woods KR. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 1981;78:3824-3828.
15. Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASy server. In: Walker JM, editor. The proteomics protocols handbook. Totowa, NJ: Humana; 2005. pp 571-607.
16. Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988;85:2444-2448.
17. Clamp M, Cuff J, Searle SM, Barton GJ. The Jalview Java alignment editor. Bioinformatics 2004;20:426-427.
18. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL
19. Andrade MA, Chacon P, Merelo JJ, Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng 1993;6:383-390.
20. Whitmore L, Wallace BA. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 2004;32(Web Server issue):W668-W673.
21. Lobley A, Whitmore L, Wallace BA. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002;18:211-212.
22. Shaka AJ, Freeman R. Simplification of NMR spectra by filtration through multiple-quantum coherence. J Magn Reson 1983;51:169-173.
23. Bax A, Davis DG. MLEV-17 based two-dimensional homonuclear magnetisation transfer spectroscopy. J Magn Reson 1985;65:355-360.
24. Kumar A, Ernst RR, Wüthrich K. A two-dimensional nuclear Overhauser enhancement experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem Biophys Res Commun 1980;95:1-6.
25. Goddard TD, Kneller DG. SPARKY 3 software. San Francisco, CA: University of California.
26. Güntert P, Braun W, Wüthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol 1991;217:517-530.
27. Wüthrich K, Billeter M, Braun W. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J Mol Biol 1983;169:949-961.
28. Güntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 1997;273:283-298.
29. Tripos. St. Louis, MO 63144-2319, USA: Inc., 1699 South Janley Road. Available at http://www.tripos.com
30. Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55, 29-32.
31. DeLano WL. The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific; 2002.
32. Alaña I, Hewage CM, Malthouse JP, Parker JC, Gault VA, O'Harte FP. NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide. Biochem Biophys Res Commun 2004;325:281-286.
33. Hewage CM, Jiang L, Parkinson JA, Ramage R, Sadler IH. Design of ET(B) receptor agonists: NMR spectroscopic and conformational studies of ET7-21[Leu7, Aib11, Cys(Acm)15]. Protein Eng 2002;15:161-167.
34. Chang X, Keller D, Bjorn S, Led JJ. Structure and folding of glucagon-like peptide-1-(7-36)-amide in aqueous trifluoroethanol studied by NMR spectroscopy. Magn Reson Chem 2001;39:477-483.
35. Alaña I, Parker JC, Gault VA, Flatt PR, O'Harte FPM, Malthouse JP, Hewage CM. NMR and alanine scan studies of glucose-dependent insulinotropic polypeptide in water. J Biol Chem 2006;281:16370-16376.
36. Sonnichsen FD, Van Eyk JE, Hodges RS, Sykes BD. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 1992;31:8790-8798.
37. Jasanoff A, Fersht AR. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 1994;33:2129-2135.
38. Povey JF, Smales CM, Hassard SJ, Howard MJ. Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function. J Struct Biol, in press.
39. Manhart S, Hinke SA, McIntosh CH, Pederson RA, Demuth HU. Structure-function analysis of a series of novel GIP analogues containing different helical length linkers. Biochemistry 2003;42:3081-3088.
40. Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 1996;8:477-486.
41. Tyndall JD, Pfeiffer B, Abbenante G, Fairlie DP. Over one hundred peptide-activated G protein-coupled receptors recognize ligands with turn structure. Chem Rev 2005;105:793-826.
42. Neidigh JW, Fesinmeyer RM, Prickett KS, Andersen NH. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry 2001;40:13188-13200.
43. Sasaki K, Dockerill S, Adamiak DA, Tickle IJ, Blundell T. X-ray analysis of glucagon and its relationship to receptor binding. Nature 1975;257:751-757.
44. Eng J, Kleinman WA, Singh L, Singh G, Raufman JP. Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas. J Biol Chem 1992;267:7402-7405.
45. Inooka H, Ohtaki T, Kitahara O, Ikegami T, Endo S, Kitada C, Ogi K, Onda H, Fujino M, Shirakawa M. Conformation of a peptide ligand bound to its G-protein coupled receptor. Nat Struct Biol 2001;8:161-165.
46. Tan YV, Couvineau A, Murail S, Ceraudo E, Neumann JM, Lacapere JJ, Laburthe M. Peptide agonist docking in the N-terminal ectodomain of a class II G protein-coupled receptor, the VPAC1 receptor. Photoaffinity, NMR, and molecular modeling. J Biol Chem 2006;281:12792-12798.
47. Alaña I, Hewage CM, Malthouse JP, Parker JC, Gault VA, O'Harte FPM. NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide. Biochem Biophys Res Commun 2004;325:281-286.
48. Hoare SR. Mechanisms of peptide and nonpeptide ligand binding to Class B G-protein-coupled receptors. Drug Discov Today 2005;10:417-427.
49. Perham M, Liao J, Wittung-Stafshede P. Differential effects of alcohols on conformational switchovers in α-helical and β-sheet protein models. Biochemistry 2006;45:7740-7749.