Gly-Pro-pNA, as a chromogenic substrate, can be cleaved by the circulating enzyme, dipeptidyl peptidase IV (DPP IV).[1]
In vitro, when Z-Gly-Pro-pNA was used as a substrate, SNA-8073-B inhibited prolyl endopeptidase of Flavobacterium non-competitively with IC50 of 8.9 µM.[2] In addition, when Z-Gly-Pro-pNA was used as a substrate, Propeptin inhibited prolyl endopeptidase of the genus Flavobacterium competitively with Ki of 0.70 µM.[3] In addition, using Gly-Pro-p-nitroanilide as substrate to determine the enzymatic activity of this molecule in serum. Using Gly-Pro-pNA as substrate can assess the enzymatic activity and biochemical status of dipeptidyl peptidase IV in patients with rheumatoid arthritis.[4] In vitro, using Gly-Pro-pNA as a substrate can determine DPP-IV inhibitory activities of quinoa protein hydrolysates. Twenty quinoa-derived peptides were determined with in vitro DPP-IV inhibitory activities with IC50 values less than 500 µM. [5]
[1] Fu P, et al. Identification of two isoforms of Pop in the domestic silkworm, Bombyx mori: Cloning, characterization and expression analysis. Gene. 2018 Aug 15;667:101-111.
Kimura K, et al. SNA-8073-B, a new isotetracenone antibiotic inhibits prolyl endopeptidase. I. Fermentation, isolation and biological properties. J Antibiot (Tokyo). 1997 Apr;50(4):291-6.
Kimura K, et al. Propeptin, a new inhibitor of prolyl endopeptidase produced by Microbispora. I. Fermentation, isolation and biological properties. J Antibiot (Tokyo). 1997 May;50(5):373-8.
Yeganeh F, et al. Association of CD26/dipeptidyl peptidase IV mRNA level in peripheral blood mononuclear cells with disease activity and bone erosion in rheumatoid arthritis. Clin Rheumatol. 2018 Dec;37(12):3183-3190.
You H, et al. Preparation and identification of dipeptidyl peptidase IV inhibitory peptides from quinoa protein. Food Res Int. 2022 Jun;156:111176.
References:
Z-Gly-Pro-pNA 作为显色底物，可被循环酶二肽基肽酶 IV (DPP IV) 裂解。[1]
在体外，当以Z-Gly-Pro-pNA为底物时，SNA-8073-B非竞争性抑制黄杆菌的脯氨酰内肽酶，IC50为8.9 µM.[2] 此外，当Z -以Gly-Pro-pNA为底物，Propeptin竞争性抑制黄杆菌属的脯氨酰内肽酶，Ki为0.70 µM.[3] 此外，使用Gly-Pro-p-nitroanilide作为底物来确定该分子在血清中的酶活性。以Gly-Pro-pNA为底物可评估类风湿性关节炎患者体内二肽基肽酶IV的酶活性和生化状态。[4] 在体外，以Gly-Pro-pNA为底物可测定藜麦蛋白水解物的 DPP-IV 抑制活性。二十种藜麦来源的肽经测定具有体外 DPP-IV 抑制活性，IC50 值小于 500 µM。 [5]