Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 | 150956-93-7
Catalog Number | A18-0037 |
Category | Fluorescent Enzyme Substrates |
Molecular Formula | C51H72N14O12S |
Molecular Weight | 1105.3 |
Catalog Number | Size | Price | Quantity |
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A18-0037 | -- | $-- |
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Product Introduction
Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-9. It is cleaved by MMP-1 and MMP-9 to release N-methylanthranilic acid (Nma), which is unquenched and its fluorescence can be used to quantify MMP activity.
Chemical Information |
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Synonyms | Matrix Metalloproteinase-1 Fluorogenic Substrate III; MMP-1 Fluorogenic Substrate III; (S)-N-((7S,10S,13S,16R,19S,22S)-13-((1H-imidazol-5-yl)methyl)-7-carbamoyl-23-cyclohexyl-19-ethyl-10-methyl-1-(2-(methylamino)phenyl)-16-((methylthio)methyl)-1,9,12,15,18,21-hexaoxo-2,8,11,14,17,20-hexaazatricosan-22-yl)-1-(2,4-dinitrophenyl)pyrrolidine-2-carboxamide |
Purity | ≥95% |
Canonical SMILES | CCC(C(=O)NC(CSC)C(=O)NC(CC1=CN=CN1)C(=O)NC(C)C(=O)NC(CCCCNC(=O)C2=CC=CC=C2NC)C(=O)N)NC(=O)C(CC3CCCCC3)NC(=O)C4CCCN4C5=C(C=C(C=C5)[N+](=O)[O-])[N+](=O)[O-] |
InChI | InChI=1S/C51H72N14O12S/c1-5-35(58-49(71)38(24-31-14-7-6-8-15-31)61-51(73)42-19-13-23-63(42)41-21-20-33(64(74)75)26-43(41)65(76)77)47(69)62-40(28-78-4)50(72)60-39(25-32-27-54-29-56-32)48(70)57-30(2)45(67)59-37(44(52)66)18-11-12-22-55-46(68)34-16-9-10-17-36(34)53-3/h9-10,16-17,20-21,26-27,29-31,35,37-40,42,53H,5-8,11-15,18-19,22-25,28H2,1-4H3,(H2,52,66)(H,54,56)(H,55,68)(H,57,70)(H,58,71)(H,59,67)(H,60,72)(H,61,73)(H,62,69)/t30-,35-,37-,38-,39-,40-,42-/m0/s1 |
InChI Key | ZXWDGVAWRUKOAR-IHGWQQAUSA-N |
- Product Specification
- Application
Storage | Store at -20°C |
Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 is a synthetic peptide compound characterized by its unique sequence and specialized functional groups. The sequence begins with Dnp (2,4-dinitrophenyl), which is often used as a protecting group in peptide synthesis, providing stability during the synthesis process. P-Cha refers to the phenylcyclohexylalanine, a modified amino acid that can alter the peptide’s structural conformation, thereby affecting its binding properties and biological activity. Abu stands for 2-aminobutyric acid, a non-standard amino acid contributing to the peptide’s hydrophobic character. Cys(Me) denotes methyl-cysteine, which incorporates a methyl group into the cysteine residue, impacting the peptide’s reactivity, particularly in forming disulfide bridges. HA is histidine (His), but in this notation, it implies some alteration potentially associated with the sequence’s unique framework. K(Nma) represents lysine modified with N-methylalanine, adding to the structural diversity and functional specificity. The -NH2 ending indicates an amidated C-terminus, often found in peptides to enhance biological activity and stability. Together, the specific sequence design of Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 underscores its specialized nature and potential for diverse applications.
One key application of Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 is in the field of pharmaceutical research, specifically in the development of novel therapeutic agents. Given its complex structure and customizable nature, this peptide can be tailored for targeting specific biological pathways or interactions, making it a valuable candidate for drug design. Its sequence allows for significant interactions with various biological targets, providing opportunities to develop inhibitors or modulators for proteins associated with diseases such as cancer, metabolic disorders, or inflammatory conditions. By modulating these proteins or pathways, this peptide has the potential to lead to new treatments with improved efficacy and reduced side effects compared to conventional small-molecule drugs.
In biochemical research, Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 serves a critical role in studying protein-peptide interactions. Its unique sequence can be employed as a probe to elucidate the binding mechanisms of proteins that are difficult to study using traditional methods. By studying the interactions between this peptide and various proteins, researchers can gain insights into the dynamic processes of protein function and regulation. This understanding is crucial for discovering how proteins operate in different biological contexts, potentially leading to breakthroughs in knowledge that could inform future research directions and therapeutic interventions.
Additionally, Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 can be utilized in the field of diagnostic assay development. The specificity of its sequence allows it to be used as a biomarker or as a component in assays designed to detect specific biological molecules or changes within a biological system. For instance, its high specificity and affinity for particular targets could be harnessed in assays to diagnose diseases at an early stage, monitor disease progression, or evaluate the effectiveness of treatments. The peptide’s ability to bind selectively to certain molecules makes it a powerful tool in creating highly sensitive and specific diagnostic tests.
Finally, in the field of material science, Dnp-P-Cha-Abu-Cys(Me)-HA-K(Nma)-NH2 offers potential for use in the creation of novel biomaterials. The peptide’s structural properties can be exploited to construct materials with specific mechanical or chemical properties, useful in bioengineering and biotechnology applications. For instance, it could be used to create scaffolds that promote cell growth and differentiation in tissue engineering or as a coating material that offers anti-bacterial or anti-fouling properties. The adaptability and functional diversity of this peptide make it a strong candidate for the development of innovative materials that meet specific scientific and industrial needs.
Applications of Fluorescent Probes & Dyes
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