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D2293

Sigma-Aldrich

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

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About This Item

Fórmula empírica (notación de Hill):
C45H64N14O11
Número de CAS:
121282-17-5
Peso molecular:
977.08
MDL number:
MFCD00133551
UNSPSC Code:
12352204
PubChem Substance ID:
24893676

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

Substrates

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.

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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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