Asparaginyl-proline
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Others |
| Catalog number | BBF-05580 |
| CAS | 78346-95-9 |
| Molecular Weight | 229.23 |
| Molecular Formula | C9H15N3O4 |
| Purity | ≥95% |
Online Inquiry
Description
Asparaginyl-proline is a dipeptide composed of asparagine and proline. It is an incomplete breakdown product of protein digestion or protein catabolism.
Specification
| Synonyms | L-Proline, 1-L-asparaginyl-; H-NP-OH; L-asparagyl-L-proline; Asn-Pro; L-Asn-L-Pro |
| Sequence | H-Asn-Pro-OH |
| IUPAC Name | (2S)-1-[(2S)-2,4-diamino-4-oxobutanoyl]pyrrolidine-2-carboxylic acid |
| Canonical SMILES | C1CC(N(C1)C(=O)C(CC(=O)N)N)C(=O)O |
| InChI | InChI=1S/C9H15N3O4/c10-5(4-7(11)13)8(14)12-3-1-2-6(12)9(15)16/h5-6H,1-4,10H2,(H2,11,13)(H,15,16)/t5-,6-/m0/s1 |
| InChI Key | GADKFYNESXNRLC-WDSKDSINSA-N |
Properties
| Appearance | Solid |
| Boiling Point | 586.2±50.0°C at 760 mmHg |
| Density | 1.4±0.1 g/cm3 |
| Solubility | Soluble in Water |
Reference Reading
1. Two-stage selective enzymatic hydrolysis generates protein hydrolysates rich in Asn-Pro and Ala-His for enhancing taste attributes of soy sauce
Yaqi Zhao, Xuan Zhao, Dongxiao Sun-Waterhouse, Geoffrey Ivan Neil Waterhouse, Mouming Zhao, Jiahui Zhang, Fang Wang, Guowan Su Food Chem. 2021 May 30;345:128803. doi: 10.1016/j.foodchem.2020.128803. Epub 2020 Dec 3.
This study demonstrated the contribution of peptides to umami soy sauce taste. Asn-Pro and Ala-His with remarkable umami taste and umami-enhancing capacity were found in original soy sauce, possessing umami thresholds of 175 and 160 mg/L and umami-enhancing thresholds of 10 and 13 mg/L, respectively. Firstly, an industrially viable two-stage hydrolysis at 55 °C (a 12-h hydrolysis with the neutral protease, then a 12-h hydrolysis with the aminopeptidase) was established to produce protein hydrolysates rich in umami-tasting and umami-enhancing peptides (e.g. Asn-Pro and Ala-His) from non-soy sauce protein preparations (soy protein isolate, rice proteins, wheat proteins, peanut proteins or pea proteins). The soy protein isolate hydrolysate produced via the two-stage hydrolysis had Asn-Pro and Ala-His contents 3.32 and 1.15 times higher than those produced via the one-stage hydrolysis using the neutral protease only. Adding the hydrolysate to original soy sauce at 5% w/v significantly increased umami and reduced bitterness.
2. Dual intra- and extracellular release of monomethyl auristatin E from a neutrophil elastase-sensitive antibody-drug conjugate
Imene Ait Mohamed Amar, Steve Huvelle, Emmanuel Douez, Stéphanie Letast, Sylvain Henrion, Marie-Claude Viaud-Massuard, Nicolas Aubrey, Emilie Allard-Vannier, Nicolas Joubert, Caroline Denevault-Sabourin Eur J Med Chem. 2022 Feb 5;229:114063. doi: 10.1016/j.ejmech.2021.114063. Epub 2021 Dec 24.
Antibody-drug conjugates (ADCs) are targeted therapies, mainly used in oncology, consisting in a three-component molecular architecture combining a highly potent drug conjugated via a linker onto a monoclonal antibody (mAb), designed for the selective delivery of the drug to the tumor site. The linker is a key component, defining the ADC stability and mechanism of action, and particularly the drug release strategy. In this study, we have developed and synthesized a cleavable linker, which possesses an Asn-Pro-Val (NPV) sequence sensitive to the human neutrophil elastase (HNE), overexpressed in the tumor microenvironment. This linker permitted the site-specific conjugation of the cell-permeable drug, monomethyl auristatin E (MMAE), onto trastuzumab, using a disulfide re-bridging technology. The resulting ADC was then evaluated in vitro. This conjugate demonstrated retained antigen (Ag) binding affinity and exhibited high subnanomolar potency against Ag-positive tumor cells after internalization, suggesting an intracellular mechanism of linker cleavage. While no internalization and cytotoxic activity of this ADC was observed on Ag-negative cells in classical conditions, the supplementation of exogenous HNE permitted to restore a nanomolar activity on these cells, suggesting an extracellular mechanism of drug release in these conditions. This in vitro proof of concept tends to prove that the NPV sequence could allow a dual intra- and extracellular mechanism of drug release. This work represents a first step in the design of original ADCs with a new dual intra- and extracellular drug delivery system and opens the way to further experimentations to evaluate their full potential in vivo.
3. Characterization of the distinct mechanism of agonist-induced canine platelet activation
Preeti K Chaudhary, Soochong Kim J Vet Sci. 2019 Jan 31;20(1):10-15. doi: 10.4142/jvs.2019.20.1.10.
Platelet activation has a major role in hemostasis and thrombosis. Various agonists including adenosine diphosphate (ADP) and thrombin interact with G protein-coupled receptors (GPCRs) which transduce signals through various G proteins. Recent studies have elucidated the role of GPCRs and their corresponding G proteins in the regulation of events involved in platelet activation. However, agonist-induced platelet activation in companion animals has not been elucidated. This study was designed to characterize the platelet response to various agonists in dog platelets. We found that 2-methylthio-ADP-induced dog platelet aggregation was blocked in the presence of either P2Y₁ receptor antagonist MRS2179 or P2Y₁₂ receptor antagonist AR-C69931MX, suggesting that co-activation of both the P2Y₁ and P2Y₁₂ receptors is required for ADP-induced platelet aggregation. Thrombin-induced dog platelet aggregation was inhibited in the presence of either AR-C69931MX or the PKC inhibitor GF109203X, suggesting that thrombin requires secreted ADP to induce platelet aggregation in dog platelets. In addition, thrombin-mediated Akt phosphorylation was inhibited in the presence of GF109203X or AR-C69931MX, indicating that thrombin causes Gi stimulation through the P2Y₁₂ receptor by secreted ADP in dog platelets. Unlike human and murine platelets, protease-activated receptor 4 (PAR4)-activating peptide AYPGKF failed to cause dog platelet aggregation. Moreover, PAR1-activating peptide SFLLRN or co-stimulation of SFLLRN and AYPGKF failed to induce dog platelet aggregation. We conclude that ADP induces platelet aggregation through the P2Y₁ and P2Y₁₂ receptors in dogs. Unlike human and murine platelets, selective activation of the PAR4 receptor may be insufficient to cause platelet aggregation in dog platelets.
Recommended Products
| BBF-01829 | Deoxynojirimycin | Inquiry |
| BBF-03754 | CASTANOSPERMINE | Inquiry |
| BBF-02642 | Lactonamycin | Inquiry |
| BBF-01825 | Loganin | Inquiry |
| BBF-05862 | Epirubicin | Inquiry |
| BBF-03755 | Actinomycin D | Inquiry |
Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
