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Merck

D2293

N-(2,4-Dinitrophenyl)-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg amide

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Fórmula empírica (notación de Hill):
C45H64N14O11
Número CAS:
Peso molecular:
977.08
UNSPSC Code:
12352204
PubChem Substance ID:
MDL number:
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solubility

H2O: 2 mg/mL

storage temp.

−20°C

SMILES string

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

General description

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.


Clase de almacenamiento

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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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
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
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