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Mca-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Mca-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2, the FRET substrate, is hydrolyzed 60 times more rapidly by stromelysin 1 (MMP-3) (kcat/Km= 59400 M^-1s^-1) than by interstitial collagenase (MMP-1). However, it shows little discrimination between MMP-3, gelatinase A (MMP-2) (kcat/Km= 54000 M^-1s^-1), and gelatinase B (MMP-9) (kcat/Km = 55300 M^-1s^-1). This fluorogenic substrate is digested by Metalloelastase (MMP-12) with a kcat/Km of 243000 M^-1s^-1.

Category

Others

Catalog number

BAT-015173

CAS number

158584-08-8

Molecular Formula

C79H105N19O19S

Molecular Weight

1656.86

Mca-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2

Specification
Reference Reading

IUPAC Name

(2S)-1-[(2S)-6-amino-2-[[(2S)-1-[(2S)-5-carbamimidamido-2-[[2-(7-methoxy-2-oxochromen-4-yl)acetyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]-N-[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-6-(2,4-dinitroanilino)-1-oxohexan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]pyrrolidine-2-carboxamide

Synonyms

NFF-2; 7-Methoxycoumarin-4-acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-(2,4-dinitrophenyl)Lys amide; N2-[(7-Methoxy-2-oxo-2H-chromen-4-yl)acetyl]-L-arginyl-L-prolyl-L-lysyl-L-prolyl-L-tyrosyl-L-alanyl-L-norvalyl-L-tryptophyl-L-methionyl-N6-(2,4-dinitrophenyl)-L-lysinamide

Appearance

Yellow Powder

Purity

≥95%

Density

1.5±0.1 g/cm3

Sequence

Mca-RPKPYA-Nva-WMK(Dnp)-NH2

Storage

Store at -20°C

Solubility

Soluble in Acetic Acid, DMSO, Water

InChI

InChI=1S/C79H105N19O19S/c1-5-15-57(71(104)93-62(39-48-44-86-54-17-7-6-16-52(48)54)74(107)91-58(31-37-118-4)72(105)89-56(69(81)102)18-9-11-33-84-55-30-25-49(97(112)113)42-65(55)98(114)115)90-70(103)45(2)87-73(106)61(38-46-23-26-50(99)27-24-46)94-76(109)64-22-14-36-96(64)78(111)60(19-8-10-32-80)92-75(108)63-21-13-35-95(63)77(110)59(20-12-34-85-79(82)83)88-67(100)40-47-41-68(101)117-66-43-51(116-3)28-29-53(47)66/h6-7,16-17,23-30,41-45,56-64,84,86,99H,5,8-15,18-22,31-40,80H2,1-4H3,(H2,81,102)(H,87,106)(H,88,100)(H,89,105)(H,90,103)(H,91,107)(H,92,108)(H,93,104)(H,94,109)(H4,82,83,85)/t45-,56-,57-,58-,59-,60-,61-,62-,63-,64-/m0/s1

InChI Key

PMQNLFGGVGXOSM-BULAGXLTSA-N

Canonical SMILES

CCCC(C(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)NC(CCSC)C(=O)NC(CCCCNC3=C(C=C(C=C3)[N+](=O)[O-])[N+](=O)[O-])C(=O)N)NC(=O)C(C)NC(=O)C(CC4=CC=C(C=C4)O)NC(=O)C5CCCN5C(=O)C(CCCCN)NC(=O)C6CCCN6C(=O)C(CCCNC(=N)N)NC(=O)CC7=CC(=O)OC8=C7C=CC(=C8)OC

1. Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3)

H Nagase, C G Fields, G B Fields J Biol Chem . 1994 Aug 19;269(33):20952-7.

Members of the matrix metalloproteinase (MMP) family have been implicated in disease states such as arthritis, periodontal disease, and tumor cell invasion and metastasis. Stromelysin 1 (MMP-3) has a broad substrate specificity and participates in the activation of several MMP zymogens. We examined known sequences of MMP-3 cleavage sites in natural peptides and proteins and compared sequence specificities of MMP-3 and interstitial collagenase (MMP-1) in order to design fluorogenic substrates that (i) would be hydrolyzed rapidly by MMP-3, (ii) would discriminate between MMP-3 and MMP-1, and (iii) could be monitored continuously without interference from MMP amino acid residues. Designed substrates were then screened for activity toward MMP-1, gelatinase A (MMP-2), MMP-3, and gelatinase B (MMP-9). The first of these substrates, NFF-1 (Mca-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(Dnp)-Gly, where Mca is (7-methoxycoumarin-4-yl)acetyl and Dnp is 2,4-dinitrophenyl), was hydrolyzed equally well by MMP-3 and MMP-2 (kcat/Km approximately 11,000 s-1 M-1). MMP-1 had 25% of the activity of MMP-3 toward NFF-1. The second substrate, NFF-2 (Mca-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2, where Nva is norvaline), was hydrolyzed 60 times more rapidly by MMP-3 (kcat/Km = 59,400 s-1 M-1) than MMP-1. Unfortunately, NFF-2 showed little discrimination between MMP-3, MMP-2 (kcat/Km = 54,000 s-1 M-1), and MMP-9 (kcat/Km = 55,300 s-1 M-1). The third substrate, NFF-3 (Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2), was hydrolyzed rapidly by MMP-3 (kcat/Km = 218,000 s-1 M-1) and very slowly by MMP-9 (kcat/Km = 10,100 s-1 M-1), but there was no significant hydrolysis by MMP-1 and MMP-2. NFF-3 is the first documented synthetic substrate hydrolyzed by only certain members of the MMP family and thus has important application for the discrimination of MMP-3 activity from that of other MMPs. Although NFF-3 was designed by assuming that substrate subsites were independent and hence free energy changes derived from single mutation experiments were additive, we found discrepancies between predicted and experimental kcat/Km values, one on the order of 2000-5000. Thus, the design of additional discriminatory MMP substrates may require approaches other than assuming additive free energy changes, such as screening synthetic libraries and consideration of secondary and tertiary structures of substrates and the enzyme.