Chemical ligation and cleavage on solid support facilitate recombinant peptide purification.
Recombinant peptide technology offers a promising means alternative to chemical synthesis and natural extraction of peptides. The bottleneck in the process of recombinant peptide production is the paucity of efficient purification protocols to eliminate heterogeneity of the desired preparation. Here, we introduce a combination strategy to facilitate purification of recombinant therapeutic peptide via native chemical ligation and chemical cleavage on a solid support. In this study, one promising therapeutic peptide called for type-2 diabetes, GLP-1(7-37), was prepared with high yield and purity without an expensive HPLC purification. Furthermore, this method is also useful for the preparation of isotopically labeled NMR peptide samples. Hopefully, this strategy combining chemical ligation with chemical cleavage on a solid support will ameliorate the production of important recombinant pharmaceutical peptides.
Li
Hongjian
H
Department of Biotechnology, Jinan University, Guangzhou 510632, China.
Zhou
Cindy X
CX
Su
James Z
JZ
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000378:metabolism; D052216:Glucagon-Like Peptide 1 / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D007004:Hypoglycemic Agents / Q000737:chemistry / Q000302:isolation & purification*; D008863:Microspheres; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D021241:Spectrometry, Mass, Electrospray Ionization
D007004:Hypoglycemic Agents; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D052216:Glucagon-Like Peptide 1; C051322:glucagon-like peptide 1 (7-37)