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N-Hippuryl-His-Leu (hydrate) Sale

(Synonyms: 马尿酰-组氨酰-亮氨酸水合物) 目录号 : GC44396

A synthetic ACE substrate

N-Hippuryl-His-Leu (hydrate) Chemical Structure

Cas No.:207386-83-2

规格 价格 库存 购买数量
25mg
¥442.00
现货
50mg
¥845.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

N-Hippuryl-His-Leu (hydrate) is a synthetic substrate for angiotensin-converting enzyme (ACE) that has been used in the in vitro identification of ACE inhibitors.,

Chemical Properties

Cas No. 207386-83-2 SDF
别名 马尿酰-组氨酰-亮氨酸水合物
Canonical SMILES O=C(CNC(C1=CC=CC=C1)=O)N[C@@H](CC2=CNC=N2)C(N[C@H](C(O)=O)CC(C)C)=O.O
分子式 C21H27N5O5•XH2O 分子量 429.5
溶解度 DMF: 16 mg/ml,DMSO: 14 mg/ml,Ethanol: 2 mg/ml,PBS (pH 7.2): 1 mg/ml 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 2.3283 mL 11.6414 mL 23.2829 mL
5 mM 0.4657 mL 2.3283 mL 4.6566 mL
10 mM 0.2328 mL 1.1641 mL 2.3283 mL
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Research Update

Structural characterization and functional properties of antihypertensive Cymodocea nodosa sulfated polysaccharide

Carbohydr Polym 2016 Oct 20;151:511-522.PMID:27474595DOI:10.1016/j.carbpol.2016.05.098.

A sulfated polysaccharide was successfully isolated from Cymodocea nodosa (CNSP). This is the first report that indicates the chemical composition, structural characterization, functional and antihypertensive properties of this polysaccharide. The CNSP consisted mainly of sulfate (23.17%), total sugars (54.90%), galactose (44.89%), mannose (17.30%), arabinose (12.05%), xylose (9.18%), maltose (1.07%) and uronic acid (11.03%) with low water activity (0.49). CNSP had an XRD pattern that was typical for a semi-crystalline polymer with homogeneous structure. It also displayed an important anti-hypertensive activity (IC50=0.43mgml) with a dose-dependent manner using a synthetic substrate, N-Hippuryl-His-Leu hydrate salt (HHL). Overall, the results indicate that CNSP have attractive chemical, functional and biological properties, with a preliminary structural may have a backbone of branched 6-O-sulfated (1→4) galactosidic linkages, which can be considered in the future as alternative additive in various foods, cosmetic and pharmaceutical preparations.

Measuring angiotensin-I converting enzyme inhibitory activity by micro plate assays: comparison using marine cryptides and tentative threshold determinations with captopril and losartan

J Agric Food Chem 2013 Nov 13;61(45):10685-90.PMID:24131339DOI:10.1021/jf403004e.

To determine the angiotensin-I converting enzyme (ACE) inhibitory activity of marine cryptides, different methods were tested. ACE inhibition was measured using two synthetic substrates, (N-[3-(2-furyl) acryloyl]-Phe-Gly-Gly (FAPGG) and N-Hippuryl-His-Leu hydrate salt (HHL)), and a natural one, angiotensin-I. The IC50 value (defined as the concentration of inhibitory molecule needed to inhibit 50% of the ACE activity) of the reference synthetic inhibitor captopril was in the nanomolar range (1.79-15.1 nM) when synthetic substrates were used, whereas it exhibited IC50 of micromolar range (16.71 μM) with angiotensin-I. We chose losartan, an antagonist of angiotensin-II receptor as negative control for the ACE inhibition. Losartan was also able to inhibit ACE whatever the substrate tested, with IC50 of micromolar range (17.13-146 μM). We defined this value as a limit above which molecules are not showing in vitro ACE inhibitory activity. Val-Trp (VW), Val-Tyr (VY), Lys-Tyr (KY), Lys-Trp (KW), Ile-Tyr (IY), Ala-Pro (AP), Val-Ile-Tyr (VIY), Leu-Lys-Pro (LKP), Gly-Pro-Leu (GPL), Ala-Lys-Lys (AKK), and Val-Ala-Pro (VAP) were tested as inhibitors of ACE with synthetic and natural substrates. IC50 displayed were substrate-dependent. With FAPGG as substrate, IW, VAP, KY, IY, AP, AKK, and VIY show IC50 values over the IC50 value of losartan and should not be considered as inhibitors of ACE. VY, VW, KW, and LKP exhibited IC50 value lower than the IC50 value of losartan for all substrates tested and were thus considered as good candidates for effectively decreasing hypertension. It appears that the comparison of IC50 is not consistent when IC50 values are obtained with different substrates and different methods. In vitro ACE inhibitory activity assays should always include various ACE substrates and references such as captopril and a negative control to obtain data reliable to discriminate ACE inhibitory peptides.