A Single Pseudoproline and Microwave Solid Phase Peptide Synthesis Facilitates an Efficient Synthesis of Human Amylin 1-37

被引：21

作者：

Harris, Paul W. R. ^{[1
,2
,3
,4
]}

Kowalczyk, Renata ^{[1
,2
,3
]}

Hay, Debbie L. ^{[2
,5
]}

Brimble, Margaret A. ^{[1
,2
,3
,4
]}

机构：

[1] Univ Auckland, Sch Chem Sci, Auckland 1010, New Zealand

[2] Univ Auckland, Maurice Wilkins Ctr Mol Biodiscovery, Auckland 1010, New Zealand

[3] Univ Auckland, Inst Innovat Biotechnol, Auckland 1010, New Zealand

[4] Univ Auckland, Sch Chem Sci, Auckland 1142, New Zealand

[5] Univ Auckland, Sch Biol Sci, Auckland 1010, New Zealand

来源：

INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS | 2013年 / 19卷 / 02期

关键词：

Amylin; Microwave solid phase synthesis; Pseudoproline; 2,2 '-Dipyridyl disulfide; ISLET AMYLOID POLYPEPTIDE; DIET-INDUCED OBESITY; O-ACYL ISOPEPTIDE; DIABETES-MELLITUS; LEPTIN RESPONSIVENESS; DISULFIDE FORMATION; PSEUDO-PROLINES; RESIN; PURIFICATION; PRAMLINTIDE;

D O I：

10.1007/s10989-012-9325-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A chemical synthesis of the 37 residue polypeptide human amylin using microwave enhanced solid phase peptide chemistry is described. An optimised protocol used only a single pseudoproline derivative, a chemically pure resin and single couplings of all amino acids to deliver non-oxidised amylin in high yield. Oxidation of the crude peptide to form the disulfide bond was accomplished in 20 min using 2,2'-dipyridyl disulfide in dimethyl sulphoxide giving human amylin that was fully functional in a cAMP assay.

引用

页码：147 / 155

页数：9

共 42 条

[1] Recovery and purification of highly aggregation-prone disulfide-containing peptides: Application to islet amyloid polypeptide [J].

Abedini, A ;

Singh, G ;

Raleigh, DP .

ANALYTICAL BIOCHEMISTRY, 2006, 351 (02) :181-186

[2] Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide [J].

Abedini, A ;

Raleigh, DP .

ORGANIC LETTERS, 2005, 7 (04) :693-696

[3]

[Anonymous], WIEN KLEIN WOCHENSCH

[4] Solid-phase synthesis of difficult peptide sequences at elevated temperatures:: A critical comparison of microwave and conventional heating technologies [J].

Bacsa, Bernadett ;

Horvati, Kata ;

Bosze, Szilvia ;

Andreae, Fritz ;

Kappe, C. Oliver .

JOURNAL OF ORGANIC CHEMISTRY, 2008, 73 (19) :7532-7542

[5] Resins with Identical Specifications Are Not Identical. Identifying a Useful Solid-Phase Resin [J].

Bouillon, Isabelle ;

Soural, Miroslav ;

Miller, Marvin J. ;

Krchnak, Viktor .

JOURNAL OF COMBINATORIAL CHEMISTRY, 2009, 11 (02) :213-215

[6] 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].

Cao, Ping ;

Raleigh, Daniel P. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2010, 132 (12) :4052-+

[7] General method for facile intramolecular disulfide formation in synthetic peptides [J].

Cline, DJ ;

Thorpe, C ;

Schneider, JP .

ANALYTICAL BIOCHEMISTRY, 2004, 335 (01) :168-170

[8] The depsipeptide method for solid-phase synthesis of difficult peptides [J].

Coin, Irene .

JOURNAL OF PEPTIDE SCIENCE, 2010, 16 (05) :223-230

[9] Microwave energy: a versatile tool for the biosciences [J].

Collins, Jonathan M. ;

Leadbeater, Nicholas E. .

ORGANIC & BIOMOLECULAR CHEMISTRY, 2007, 5 (08) :1141-1150

[10] AMYLIN AND THE AMYLIN GENE - STRUCTURE, FUNCTION AND RELATIONSHIP TO ISLET AMYLOID AND TO DIABETES-MELLITUS [J].

COOPER, GJS ;

DAY, AJ ;

WILLIS, AC ;

ROBERTS, AN ;

REID, KBM ;

LEIGHTON, B .

BIOCHIMICA ET BIOPHYSICA ACTA, 1989, 1014 (03) :247-258

← 1 2 3 4 5 →