Dunn B M, Pham C, Raney L, Abayasekara D, Gillespie W, Hsu A
Biochemistry. 1981 Dec 8;20(25):7206-11. doi: 10.1021/bi00528a023.
Peptide inhibitors, specifically labeled at the alpha-amino terminus by dansylation, have been prepared by utilizing solid-phase peptide synthesis. Changes in fluorescence have been observed upon mixing these peptides with porcine pepsin that can be attributed to the formation of at least two complexes. Energy transfer between tryptophan residues of the protein and the dansyl group of the inhibitors has been detected by the unique excitation spectra generated. The kinetics of formation of the second complex can be correlated with inhibition of the catalytic activity of pepsin. Evidence for complex formation has also been obtained from gel filtration experiments using the fluorescent peptides.
利用固相肽合成法制备了在α-氨基末端通过丹磺酰化特异性标记的肽抑制剂。将这些肽与猪胃蛋白酶混合后，观察到荧光变化，这可归因于至少两种复合物的形成。通过产生的独特激发光谱检测到了蛋白质色氨酸残基与抑制剂丹磺酰基团之间的能量转移。第二种复合物形成的动力学与胃蛋白酶催化活性的抑制相关。使用荧光肽的凝胶过滤实验也获得了复合物形成的证据。
