H-Gly-Arg-AMC is a fluorogenic substrate for cathepsin C, with maximum excitation/emission wavelengths of 340-360/440-460nm. When cleaved by cathepsin C, 7-amino-4-methylcoumarin (AMC) is liberated, and its fluorescence serves to measure the activity of cathepsin C[1]. H-Gly-Arg-AMC contains the AMC group and can be used to assess the activity of various proteases and peptidases. AMC has been widely used for monitoring the activity of aminopeptidases, dipeptidases, and carboxypeptidases. The H- can improve the water solubility of peptide substrates, optimize the kinetic parameters of the substrates (such as KM and kcat), enhance the specificity of the substrates, and improve their biocompatibility[2].
References:
[1] Rubach JK, Cui G, Schneck JL, et al. The amino-acid substituents of dipeptide substrates of cathepsin C can determine the rate-limiting steps of catalysis. Biochemistry. 2012;51(38):7551-7568.
[2] van Berkel SS, van der Lee B, van Delft FL, Wagenvoord R, Hemker HC, Rutjes FP. Fluorogenic peptide-based substrates for monitoring thrombin activity. ChemMedChem. 2012;7(4):606-617.
H-Gly-Arg-AMC 是组织蛋白酶 C 的一种荧光底物，其最大激发和发射波长分别为 340-360nm 和 440-460nm。当被组织蛋白酶 C 酶切时，会释放出7-氨基-4-甲基香豆素（AMC），其荧光可用于测量组织蛋白酶 C 的活性[1]。H-Gly-Arg-AMC 含有AMC基团，可用于评估各种蛋白酶和肽酶的活性，其中 AMC 已被广泛用于监测氨基肽酶、二肽酶和羧肽酶的活性。H-可以提高肽底物的水溶性，优化底物的动力学参数（如KM and kcat），增强底物的特异性，并提高其生物相容性[2]。