Diprotin B
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| Category | Enzyme inhibitors |
| Catalog number | BBF-01765 |
| CAS | 90614-49-6 |
| Molecular Weight | 327.42 |
| Molecular Formula | C16H29N3O4 |
| Purity | ≥95% |
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Description
It is produced by the strain of Bacillus cereus BMF 657-RF1. It can inhibit Dipeptidyl amino peptidase IV and immune enhancement effect.
Specification
| Synonyms | H-Val-Pro-Leu-OH; valyl-prolyl-leucine; Val-Pro-Leu; N-(1-L-Valyl-L-prolyl)-L-leucine; L-valyl-L-prolyl-L-leucine; L-Leucine, N-(1-L-valyl-L-prolyl)-; N-[Hydroxy(1-valylpyrrolidin-2-yl)methylidene]leucine |
| Storage | -20 °C |
| IUPAC Name | (2S)-2-[[(2S)-1-[(2S)-2-amino-3-methylbutanoyl]pyrrolidine-2-carbonyl]amino]-4-methylpentanoic acid |
| Canonical SMILES | CC(C)CC(C(=O)O)NC(=O)C1CCCN1C(=O)C(C(C)C)N |
| InChI | InChI=1S/C16H29N3O4/c1-9(2)8-11(16(22)23)18-14(20)12-6-5-7-19(12)15(21)13(17)10(3)4/h9-13H,5-8,17H2,1-4H3,(H,18,20)(H,22,23)/t11-,12-,13-/m0/s1 |
| InChI Key | NHXZRXLFOBFMDM-AVGNSLFASA-N |
Properties
| Appearance | White Lyophilized Powder |
| Boiling Point | 575.9 °C at 760 mmHg |
| Melting Point | 158-160 °C (dec.) |
| Density | 1.157 g/cm3 |
| Solubility | Soluble in Hydrochloric acid |
Reference Reading
1. Identification and primary characterization of specific proteases in the digestive juice of Archachatina ventricosa
Olivier Guionie, Claire Moallic, Sébastien Niamké, Gaël Placier, Jean Pierre Sine, Bernard Colas Comp Biochem Physiol B Biochem Mol Biol. 2003 Jul;135(3):503-10. doi: 10.1016/s1096-4959(03)00115-5.
The profile of sedimentation on a 4-20% (w/v) linear sucrose gradient of the digestive juice of the mollusk Archachatina ventricosa revealed the presence of at least four specific proteases. A first peak, corresponding to a sedimentation coefficient of 3.9 S, contained two endoproteases that could be assayed, one with Leu-pNA and the other with Met-pNA. Their activity was maximal at pH 8.0 and increased in the presence of Ca(2+) ions. Both enzymes were inhibited by the chelating agent 1,10-phenanthroline but their thermal inactivation kinetics were different. A second protease peak was observed at 6.8 S and corresponded to a metallo-endoprotease that hydrolyzed with a maximal activity at pH 8.0 only the amide bonds of peptide substrates having a threonine residue at the P1' position. A last protease peak identified at 9.0 S contained a protease that preferentially acted on tripeptides, such as Val-Pro-Leu (diprotin B) and Thr-Val-Leu, releasing the C-terminal residue. Unlike the proteases identified in the two other peaks, its activity was maximal at acid pH (5.0) and was inhibited by the serine protease inhibitors. Together these results show the potential of A. ventricosa as a source of specific proteases.
2. Computational study of matrix-peptide interactions in MALDI mass spectrometry: Interactions of 2,5- and 3,5-dihydroxybenzoic acid with the tripeptide valine-proline-leucine
Faten H Yassin, Dennis S Marynick J Phys Chem A. 2006 Mar 16;110(10):3820-5. doi: 10.1021/jp058257c.
The mechanism of matrix-to-analyte proton transfer in matrix-assisted laser desorption and ionization mass spectrometry (MALDI-MS) has been investigated computationally by modeling the matrix-analyte interaction of potential MALDI matrixes such as 2,5-dihydroxybenzoic acid (2,5-DHB) and 3,5-DHB with the tripeptide valine-proline-leucine (VPL). A combination of molecular dynamics/simulated annealing calculations followed by density functional theory geometry optimization using a reasonably large basis set has been done on a large number of clusters in an attempt to study the ionization energy of each matrix in the cluster environment and the intracluster proton transfer from the matrix to the tripeptide. The calculations show a substantial reduction in the IP for both matrixes in their cluster environments. In the 2,5-system, proton transfer can sometimes occur in the neutral clusters (preformed ions), whereas proton transfer in the cationic clusters, which is actually a double proton transfer, is spontaneous and exoergic. Even though it is more acidic from a thermodynamic perspective, the radical cation of 3,5-DHB is a less efficient proton donor to VPL. The thermodynamics of proton transfer in the cationic clusters is discussed in detail.
3. Crystal structures of human dipeptidyl peptidase IV in its apo and diprotin B-complexed forms
Hajime Hiramatsu, Kiyoshi Kyono, Atsushi Yamamoto, Kazuhiko Saeki, Hideaki Shima, Shigeru Sugiyama, Koji Inaka, Ryo Shimizu Acta Biochim Biophys Sin (Shanghai). 2007 May;39(5):335-43. doi: 10.1111/j.1745-7270.2007.00289.x.
Dipeptidyl peptidase IV (DPPIV), which belongs to the prolyl oligopeptidase family of serine proteases, is known to have a variety of regulatory biological functions and has been shown to be implicated in type 2 diabetes. It is therefore important to develop selective human DPPIV (hDPPIV) inhibitors. In this study, we determined the crystal structure of apo hDPPIV at 1.9 A resolution. Our high-resolution crystal structure of apo hDPPIV revealed the presence of sodium ion and glycerol molecules at the active site. In order to elucidate the hDPPIV binding mode and substrate specificity, we determined the crystal structure of hDPPIV-diprotin B (Val-Pro-Leu) complex at 2.1 A resolution, and clarified the difference in binding mode between diprotin B and diprotin A (Ile-Pro-Ile) into the active site of hDPPIV. Comparison between our crystal structures and the reported apo hDPPIV structures revealed that positively charged functional groups and conserved water molecules contributed to the interaction of ligands with hDPPIV. These results are useful for the design of potent hDPPIV inhibitors.
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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 ╳
