A single pseudoproline and microwave solid phase peptide synthesis facilitates an efficient synthesis of human amylin 1-37

International Journal of Peptide Research and Therapeutics

Volumn 19, Issue 2, 2013, Pages 147-155

  Harris, Paul W R ^a   Kowalczyk, Renata ^a   Hay, Debbie L ^a,b   Brimble, Margaret A ^a  

^a UNIVERSITY OF AUCKLAND   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

2,2 Dipyridyl disulfide; Amylin; Microwave solid phase synthesis; Pseudoproline

Indexed keywords

2,2' DITHIODIPYRIDINE; AMYLIN; AMYLIN[1-37]; CYCLIC AMP; DIMETHYL SULFOXIDE; PROLINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; DISULFIDE BOND; MICROWAVE RADIATION; PEPTIDE SYNTHESIS; PROCESS OPTIMIZATION; SOLID PHASE SYNTHESIS;

EID: 84877980753     PISSN: 15733149     EISSN: 15733904     Source Type: Journal    
DOI: 10.1007/s10989-012-9325-9     Document Type: Article

References (41)

1. Abedini A, Raleigh DP (2005) Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Org Lett 7(4):693-696. doi: 10.1021/ol047480+
2. Abedini A, Singh G, Raleigh DP (2006) Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Anal Biochem 351(2):181-186. doi: 10.1016/J.Ab.2005.11.029
3. Bacsa B, Horvati K, Bosze S, Andreae F, Kappe CO (2008) Solid-phase synthesis of difficult peptide sequences at elevated temperatures: a critical comparison of microwave and conventional heating technologies. J Org Chem 73(19):7532-7542. doi: 10.1021/Jo8013897
4. Bouillon I, Soural M, Miller MJ, Krchnak V (2009) Resins with identical specifications are not identical. Identifying a useful solid-phase resin. J Comb Chem 11(2):213-215. doi: 10.1021/Cc800143e
5. Cao P, Raleigh DP (2010) Ester to amide switch peptides provide a simple method for preparing monomeric islet amyloid polypeptide under physiologically relevant conditions and facilitate investigations of amyloid formation. J Am Chem Soc 132(12):4052-4053. doi: 10.1021/Ja910763m
6. Cline DJ, Thorpe C, Schneider JP (2004) General method for facile intramolecular disulfide formation in synthetic peptides. Anal Biochem 335(1):168-170. doi: 10.1016/J.Ab.2004.07.015
7. Coin I (2010) The depsipeptide method for solid-phase synthesis of difficult peptides. J Pept Sci 16(5):223-230. doi: 10.1002/Psc.1224
8. Collins JM, Leadbeater NE (2007) Microwave energy: a versatile tool for the biosciences. Org Biomol Chem 5(8):1141-1150. doi: 10.1039/B617084f
9. Cooper GJS, Willis AC, Clark A, Turner RC, Sim RB, Reid KBM (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type-2 diabetic-patients. Proc Natl Acad Sci USA 84(23):8628-8632
10. Cooper GJS, Day AJ, Willis AC, Roberts AN, Reid KBM, Leighton B (1989) Amylin and the amylin gene - structure, function and relationship to islet amyloid and to diabetes-mellitus. Biochim Biophys Acta 1014(3):247-258
11. Deng FK, Mandal K, Luisier S, Kent SBH (2010) Synthesis and comparative properties of two amide-generating resin linkers for use in solid phase peptide synthesis. J Pept Sci 16(10):545-550. doi: 10.1002/Psc.1279
12. Gingell JJ, Qi T, Bailey RJ, Hay DL (2010) A key role for tryptophan 84 in receptor activity-modifying protein 1 in the amylin 1 receptor. Peptides 31(7):1400-1404. doi: 10.1016/j.peptides.2010.03.027
13. Harris PWR, Brimble MA (2009) Synthesis of an Arginine Tagged [Cys(155)-Arg(180)] Fragment of NY-ESO-1: elimination of an undesired by-product using 'in house' resins. Synthesis-Stuttgart 20:3460-3466. doi: 10.1055/s-0029-1216952
14. Harris PWR, Yang SH, Brimble MA (2011) An improved procedure for the preparation of aminomethyl polystyrene resin and its use in solid phase (peptide) synthesis. Tetrahedron Lett 52(45):6024-6026. doi: 10.1016/j.tetlet.2011.09.010
15. Hood CA, Fuentes G, Patel H, Page K, Menakuru M, Park JH (2008) Fast conventional Fmoc solid-phase peptide synthesis with HCTU. J Pept Sci 14(1):97-101. doi: 10.1002/Psc.921
16. Ludvik B, KautzkyWiller A, Prager R, Thomaseth K, Pacini G (1997) Amylin: history and overview. Diabet Med 14(6):S9-S13
17. Lutz TA (2012) Effects of amylin on eating and adiposity. In: Joost H-G (ed) Appetite control, vol 209. Handbook of experimental pharmacology. Springer-Berlin, Heidelberg, pp 231-250. doi: 10.1007/978-3-642-24716-3-10
18. Marek P, Woys AM, Sutton K, Zanni MT, Raleigh DP (2010) Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Org Lett 12(21):4848-4851. doi: 10.1021/Ol101981b
19. Maruyama K, Nagasawa H, Suzuki A (1999) 2,2′-Bispyridyl disulfide rapidly induces intramolecular disulfide bonds in peptides. Peptides 20(7):881-884
20. Muthusamy K, Albericio F, Arvidsson PI, Govender P, Kruger HG, Maguire GEM, Govender T (2010) Microwave assisted SPPS of amylin and its toxicity of the pure product to RIN-5F cells. Biopolymers 94(3):323-330. doi: 10.1002/Bip.21370
21. Mutter M, Nefzi A, Sato T, Sun X, Wahl F, Wohr T (1995) Pseudo-Prolines (Psi-Pro) for accessing inaccessible peptides. Pept Res 8(3):145-153
22. NovaBiochem (2004) NovaBiochem innovations 1/4 guidelines for the use of pseudoproline dipeptides. http://www.emdmillipore.com/life-science-research/ novabiochem-innovations/c-nZGb.s1OBzUAAAEj2WxumA4O. Accessed Aug 2012
23. Opie EL (1901) The relation of diabetes mellitus to lesions of the pancreas. Hyaline degeneration of the islands of Langerhans. J Exp Med 5(5):527-540
24. Page K, Hood CA, Patel H, Fuentes G, Menakuru M, Park JH (2007) Fast Fmoc synthesis of hAMYLIN(1-37) with pseudoproline assisted on-resin disulfide formation. J Pept Sci 13(12):833-838
25. Pedersen SL, Tofteng AP, Malik L, Jensen KJ (2012) Microwave heating in solid-phase peptide synthesis. Chem Soc Rev 41(5):1826-1844
26. Reda TK, Geliebter A, Pi-Sunyer FX (2002) Amylin, food intake, and obesity. Obes Res 10(10):1087-1091
27. Roth JD, Roland BL, Cole RL, Trevaskis JL, Weyer C, Koda JE, Anderson CM, Parkes DG, Baron AD (2008) Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies. Proc Natl Acad Sci USA 105(20):7257-7262. doi: 10.1073/pnas.0706473105
28. Roth JD, Erickson MR, Chen S, Parkes DG (2012) GLP-1R and amylin agonism in metabolic disease: complementary mechanisms and future opportunities. Br J Pharmacol 166(1):121-136. doi: 10.1111/j.1476-5381.2011.01537.x
29. Smith SR, Aronne LJ, Burns CM, Kesty NC, Halseth AL, Weyer C (2008) Sustained weight loss following 12-month pramlintide treatment as an adjunct to lifestyle intervention in obesity. Diabetes Care 31(9):1816-1823. doi: 10.2337/Dc08-0029
30. Sohma Y, Sasaki M, Hayashi Y, Kimura T, Kiso Y (2004) Novel and efficient synthesis of difficult sequence-containing peptides through O-N intramolecular acyl migration reaction of O-acyl E isopeptides. Chem Commun (Camb) 1:124-125. doi: 10.1039/B312129a
31. Sohma Y, Yoshiya T, Taniguchi A, Kimura T, Hayashi Y, Kiso Y (2007) Development of O-acyl isopeptide method. Biopolymers 88(2):253-262. doi: 10.1002/Bip.20683
32. Tam JP, Wu CR, Liu W, Zhang JW (1991) Disulfide bond formation in peptides by dimethyl-sulfoxide - scope and applications. J Am Chem Soc 113(17):6657-6662
33. Trevaskis JL, Coffey T, Cole R, Lei C, Wittmer C, Walsh B, Weyer C, Koda J, Baron AD, Parkes DG, Roth JD (2008) Amylin-mediated restoration of leptin responsiveness in diet-induced obesity: magnitude and mechanisms. Endocrinology 149(11):5679-5687. doi: 10.1210/En.2008-0770
34. Weichselbaum A, Stangl E (1901) Zur Kenntnis der feineren Veranderungen des Pankreas bie Diabetes Mellitus. Wein Klin Wochenschr 14:968-972
35. Westermark P, Wernstedt C, Obrien TD, Hayden DW, Johnson KH (1987) Islet amyloid in type-2 human diabetes-mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am J Pathol 127(3):414-417
36. Westermark P, Engstrom U, Johnson KH, Westermark GT, Betsholtz C (1990) Islet amyloid polypeptide - pinpointing amino-acid-residues linked to amyloid fibril formation. Proc Natl Acad Sci USA 87(13):5036-5040
37. Wohr T, Wahl F, Nefzi A, Rohwedder B, Sato T, Sun XC, Mutter M (1996) Pseudo-prolines as a solubilizing, structure-disrupting protection technique in peptide synthesis. J Am Chem Soc 118(39):9218-9227
38. Yonemoto IT, Kroon GJA, Dyson HJ, Balch WE, Kelly JW (2008) Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state†. Biochemistry 47(37):9900-9910. doi: 10.1021/bi800828u
39. Yoshiya T, Higa A, Abe N, Fukao F, Kuruma T, Toda Y, Sohma Y, Kiso Y (2011) Click peptide concept: O-acyl isopeptide of islet amyloid polypeptide as a nonaggregative precursor molecule. ChemBioChem 12(8):1216-1222. doi: 10.1002/cbic.201100025
40. Young A (2005) Amylin and the integrated control of nutrient influx. In: Andrew Y (ed) Advances in pharmacology, vol 52. Academic Press, New York, pp 67-77. doi: 10.1016/s1054-3589(05)52004-0
41. Younk LM, Mikeladze M, Davis SN (2011) Pramlintide and the treatment of diabetes: a review of the data since its introduction. Expert Opin Pharmacother 12(9):1439-1451. doi: 10(1517/14656566),2011,581663