[1] Smith B J. Chemical cleavage of polypeptides. Methods Mol Biol,2003, 211:63~82 [2] Makino T, Matsumoto M, Suzuki Y, et al. Semisynthesis of human ghrelin: condensation of a Boc-protected recombinant peptide with a synthetic o-acylated fragment. Biopolymers, 2005, 79(5): 238~247 [3] Sharpe S, Yau W M, Tycko R. Expression and purification of a recombinant peptide from the Alzheimer's beta-amyloid protein for solid-state NMR. Protein Expr Purif,2005, 42 (1): 200~210 [4] Smith D B, Johnson K S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione s-transferase.Gene,1988, 67 (1): 31~40 [5] Su Z, Vinogradova A, Koutychenko A, et al. Rational design and selection of bivalent peptide ligands of thrombin incorporating P4-P1 tetrapeptide sequences: from good substrates to potent inhibitors. Protein Eng Des Sel,2004, 17 (8): 647~657 [6] Iltz J L,Baker D E,Setter S M,et al. Exenatide: An incretin mimetic for the treatment of type 2 diabetes mellitus. Clinical Therapeutics, 2006, 28 (5): 652~665 [7] Burcelin R.The EuCSGLP-1, what is known, new and controversial about GLP-1? Minutes of the 1st European GLP-1 Club Meeting, Marseille, 28-29 May 2008. Diabetes & Metabolism, 2008, 34(6):627~630 [8] Lindhout D A, Thiessen A, Schieve D, et al. High-yield expression of isotopically labeled peptides for use in NMR studies. Protein Sci,2003, 12(8): 1786~1791 [9] Li H,Zhou C X,Su J Z. Chemical ligation and cleavage on solid support facilitate recombinant peptide purification. Protein Expr Purif, 2006, 50 (2): 238~246 [10] Osborne M J,Su Z,Sridaran V, et al. Efficient expression of isotopically labeled peptides for high resolution NMR studies: application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans. J Biomol NMR, 2003, 26(4): 317~326 |