Thompson P E, Keah H H, Gomme P T, Stanton P G, Hearn M T
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
Int J Pept Protein Res. 1995 Aug;46(2):174-80. doi: 10.1111/j.1399-3011.1995.tb01333.x.
A two-step low-high protocol for the efficient synthesis of peptide amides is described. The protocol exploits the efficiency of Reagent K for side-chain deprotection with the capability of the hard acid trifluoromethane-sulfonic acid (TFSMA) for cleavage of the peptide from the benzhydrylamine resin. This procedure has proven to be an effective method for the synthesis of peptide amides. The formation of alpha-aminosuccinimide (Asu) derivatives were observed with aspartyl-containing peptides as a minor side reaction product of this procedure, but this Asp-->Asu rearrangement could be successfully suppressed by employing low temperature conditions. The N- to O-acyl rearrangement of threonine and/or serine residues also only occurred to a minor extent under these synthetic conditions.
描述了一种用于高效合成肽酰胺的两步低-高方案。该方案利用了试剂K进行侧链脱保护的效率以及硬酸三氟甲磺酸（TFSMA）从二苯甲基胺树脂上裂解肽的能力。该方法已被证明是合成肽酰胺的有效方法。观察到含天冬氨酰的肽形成α-氨基琥珀酰亚胺（Asu）衍生物，这是该方法的一种次要副反应产物，但通过采用低温条件可以成功抑制这种天冬氨酸向Asu的重排。在这些合成条件下，苏氨酸和/或丝氨酸残基的N-到O-酰基重排也仅在较小程度上发生。
