天花粉胰蛋白酶抑制剂(Trichosanthes trypsin inhibitor, TTI)是一含27个氨基酸残基的多肽,其中包括三对硫硫键。本文报道了它的化学全合成及其分子内二硫键重组,合成产物纯化后其氨基酸序列以及与胰蛋白酶的抑制当量比均与天然抑制剂相一致。并合成了此抑制剂的类似物,其N端第6位Met残基由Ala所取代,合成产物纯化后,其抑制活力也与天然抑制剂相同。此结果为今后天花粉胰蛋白酶抑制剂作为融合蛋白用基因工程表达以及产物的后处理提供了依据。 Trichosanthes trypsin inhibitor (TTI) is a polypeptide of 27 amino acid residues, including three pairs of sulfur and sulfur bonds. In this paper, its chemical synthesis and its intramolecular disulfide bond recombination were reported. The amino acid sequence of the purified product and its inhibitory equivalent ratio to trypsin were the same as those of the natural inhibitor. The analogs of this inhibitor were synthesized, and the Met residue at the N-terminal 6 was replaced by Ala. After the purified product was synthesized, its inhibitory activity was also the same as that of the natural inhibitor. The results provide the basis for future use of TCS inhibitor as a fusion protein in gene engineering and product post-treatment.