D2293
N-(2,4-Dinitrophenyl)-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg amide
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About This Item
Formule empirique (notation de Hill):
C45H64N14O11
Numéro CAS:
Poids moléculaire :
977.08
Numéro MDL:
Code UNSPSC :
12352204
ID de substance PubChem :
Solubilité
H2O: 2 mg/mL
Température de stockage
−20°C
Chaîne SMILES
CC(C)C[C@H](NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CCCN1c2ccc(cc2N(=O)=O)N(=O)=O)C(=O)N[C@@H](Cc3c[nH]c4ccccc34)C(=O)N[C@@H](C)C(=O)N[C@H](CCCNC(N)=N)C(N)=O
Substrats
Fluorogenic substrate for matrix metalloproteinases (MMP-1 and MMP-9). The tryptophan fluorescence of the intact molecule is quenched by the dinitrophenyl moiety. Enzymatic cleavage of the substrate by collagenase or gelatinase results in an increased fluorescence.
Code de la classe de stockage
13 - Non Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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S Upadhye et al.
Biochemical and biophysical research communications, 215(2), 474-482 (1995-10-13)
To correlate structural data on substrates of human fibroblast collagenase with their interaction with the enzyme, we have studied: Ac-PLG-s-LLG-O-ethyl ester (I), Dnp-PLGLWA(d-Arg)-NH2 (II), AcGPEGLRVG-O-ethyl ester (III) and Succ-GPLGP-O-amidomethylcoumaryl ester (IV). Peptides I and II represent collagenase cleavage sequences in
M S Stack et al.
The Journal of biological chemistry, 264(8), 4277-4281 (1989-03-15)
A fluorogenic substrate for vertebrate collagenase and gelatinase, Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2, was designed using structure-activity data obtained from studies with synthetic inhibitors and other peptide substrates of collagenase. Tryptophan fluorescence was efficiently quenched by the NH2-terminal dinitrophenyl group, presumably through resonance energy
G M McGeehan et al.
The Journal of biological chemistry, 269(52), 32814-32820 (1994-12-30)
The peptide substrate specificities of two matrix metalloproteinases (MMPs), interstitial collagenase (MMP-1), and 92-kDa gelatinase (MMP-9), have been examined. Starting with the parent substrate, Dnp-Pro-Leu-Gly approximately Leu-Trp-Ala-D-Arg-NH2, four separate substrate mixtures were synthesized at subsites P2(Leu) through P2'(Trp). These mixtures
J Berman et al.
The Journal of biological chemistry, 267(3), 1434-1437 (1992-01-25)
A strategy is described for the rapid optimization of kcat/Km for protease substrates. Selected positions of a given peptide substrate sequence are varied through synthesis with mixtures of amino acids. Incubation of the resulting peptide mixture with the enzyme of
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