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F7131

Sigma-Aldrich

N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly

chromogenic, ≥99% (HPLC)

Synonym(s):

FAPGG, N-[3-(2-Furyl)acryloyl]-L-phenylalanyl-glycyl-glycine

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About This Item

Empirical Formula (Hill Notation):
C20H21N3O6
CAS Number:
64967-39-1
Molecular Weight:
399.40
MDL number:
MFCD00036816
UNSPSC Code:
12352202
PubChem Substance ID:
24894929
NACRES:
NA.32

product name

N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly,

storage temp.

−20°C

SMILES string

OC(=O)CNC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)\C=C\c2ccco2

InChI

1S/C20H21N3O6/c24-17(9-8-15-7-4-10-29-15)23-16(11-14-5-2-1-3-6-14)20(28)22-12-18(25)21-13-19(26)27/h1-10,16H,11-13H2,(H,21,25)(H,22,28)(H,23,24)(H,26,27)/b9-8+/t16-/m0/s1

InChI key

ZDLZKMDMBBMJLI-FDMDGMSGSA-N

Gene Information

human ... ACE(1636) , ACE2(59272)
mouse ... ACE3(217246)
rat ... ACE(11421) , ACE2(70008) , ACE3(498012)

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Amino Acid Sequence

FA-Phe-Gly-Gly

General description

N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly acts as a substrate for angiotensin converting enzyme (ACE), and is used in inhibitory assays of ACE.

Application

N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly has been used for kinetic spectrophotometric assay of ACE (angiotensin converting enzyme) inhibitory activity.

Substrates

A substrate for continuous spectrophotometric assay of angiotensin converting enzyme (ACE).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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Zhen-Hao Li et al.
Scientific reports, 7(1), 12243-12243 (2017-09-28)
Quality control is critical for ensuring the safety and effectiveness of drugs. Current quality control method for botanical drugs is mainly based on chemical testing. However, chemical testing alone may not be sufficient as it may not capture all constituents
Wen-Chi Hou et al.
Journal of agricultural and food chemistry, 51(6), 1706-1709 (2003-03-06)
Five commercial peptides, namely, reduced glutathione (GSH), oxidized glutathione (GSSG), carnosine, homocarnosine, and anserine, were used to test angiotensin converting enzyme inhibitory (ACEI) activities using N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly (FAPGG) as a substrate. All of these peptides showed dose-dependent ACEI activities. Using 50%
J E Buttery et al.
Clinical chemistry, 39(2), 312-316 (1993-02-01)
In the kinetic angiotensin-converting enzyme (ACE) method, a practical and optimal buffer is 80 mmol/L borate buffer at pH 8.2 (37 degrees C). A lag phase is detected in the reaction, and a 5-min incubation of substrate and plasma is
Siqi Sun et al.
Marine drugs, 17(3) (2019-03-22)
Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis.
Phadke Girija Gajanan et al.
Environmental science and pollution research international, 23(24), 24901-24911 (2016-09-25)
Enzymatic conversion of fish frame waste of threadfin breams (Nemipterus japonicus) to protein hydrolysate could be a solution for minimizing the pollution issues related to seafood processing operations and a way for the value addition to processing by-products. Protein hydrolysates
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