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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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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%
A Harjanne
Clinical chemistry, 30(6), 901-902 (1984-06-01)
In this automated kinetic modification of a previous method (Anal Biochem 95: 540-548, 1979) for determining angiotensin-converting enzyme (EC 3.4.15.1), 3-(2- furylacryloyl )-L- phenylalanylglycylglycine is used as the substrate. The change in absorbance at 340 nm is used to monitor
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.
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