Dunn B M, Lewitt M, Pham C
Biochem J. 1983 Feb 1;209(2):355-62. doi: 10.1042/bj2090355.
Derivatives of the 1-12 sequence of pig pepsinogen were prepared by solid-phase peptide synthesis. The three derivatives contain substitutions in the 4-7 region of the 1-12 sequence. Glycine was used to replace the hydrophobic residues -Val-Pro-Leu-Val- in pairs. After cleavage and purification, the synthetic peptides were compared with a synthetic peptide of the native sequence, prepared at the same time, with respect to their ability to inhibit the pepsin-catalysed clotting of milk. Inhibitory potency, determined from plots of percentage inhibition versus concentration of synthetic peptide, is inversely correlated with the substitution of glycine residues for the hydrophobic residues. Therefore the equilibrium inhibition of pepsin by these peptides is dominated by the hydrophobic nature of the 4-7 sequence region.
通过固相肽合成制备了猪胃蛋白酶原1 - 12序列的衍生物。这三种衍生物在1 - 12序列的4 - 7区域含有取代基。用甘氨酸成对取代疏水残基-Val-Pro-Leu-Val-。切割和纯化后，将合成肽与同时制备的天然序列合成肽在抑制胃蛋白酶催化的牛奶凝固能力方面进行比较。根据抑制百分比与合成肽浓度的关系图确定的抑制效力与甘氨酸残基取代疏水残基呈负相关。因此，这些肽对胃蛋白酶的平衡抑制作用主要由4 - 7序列区域的疏水性决定。
