N-(2,4-Dinitrophenyl)-L-proline
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N-(2,4-Dinitrophenyl)-L-proline

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Category
Cyclic Amino Acids
Catalog number
BAT-005895
CAS number
1655-55-6
Molecular Formula
C11H11N3O6
Molecular Weight
281.22
N-(2,4-Dinitrophenyl)-L-proline
IUPAC Name
(2S)-1-(2,4-dinitrophenyl)pyrrolidine-2-carboxylic acid
Synonyms
Dnp-Pro-OH; (S)-1-(2,4-Dinitrophenyl)pyrrolidine-2-carboxylic acid
Density
1.563±0.06 g/cm3
Melting Point
140 °C
Boiling Point
531.0±50.0 °C
Storage
Store at -20°C
InChI
InChI=1S/C11H11N3O6/c15-11(16)9-2-1-5-12(9)8-4-3-7(13(17)18)6-10(8)14(19)20/h3-4,6,9H,1-2,5H2,(H,15,16)/t9-/m0/s1
InChI Key
MVZXUWLTGGBNHL-VIFPVBQESA-N
Canonical SMILES
C1CC(N(C1)C2=C(C=C(C=C2)[N+](=O)[O-])[N+](=O)[O-])C(=O)O
1. Effect of chromatographic conditions on enantioseparation of bovine serum albumin chiral stationary phase in HPLC and thermodynamic studies
Qiu-Yun Wang, Ya-Jin Xiong, Bao-Zhu Lu, Jun Fan, Sheng-Run Zheng, Wei-Guang Zhang Chirality. 2013 Sep;25(9):487-92. doi: 10.1002/chir.22163. Epub 2013 Aug 2.
Twelve chiral compounds were enantiomerically resolved on bovine serum albumin chiral stationary phase (BSA-CSP) by high-performance liquid chromatography (HPLC) in reversed-phase modes. Chromatographic conditions such as mobile phase pH, the percentage of organic modifier, and concentration of analyte were optimized for separation of enantiomers. For N-(2, 4-dinitrophenyl)-serine (DNP-ser), the retention factors (k) greatly increase from 0.81 to 6.23 as the pH decreasing from 7.21 to 5.14, and the resolution factor (R(s)) exhibited a similar increasing trend (from 0 to 1.34). More interestingly, the retention factors for N-(2, 4-dinitrophenyl)-proline (DNP-pro) decrease along with increasing 1-propanol in mobile phase (3%, 5%, 7% and 9% by volume), whereas the resolution factor shows an upward trend (from 0.96 to 2.04). Moreover, chiral recognition mechanisms for chiral analytes were further investigated through thermodynamic methods.
2. Reversal of elution order of N-(2,4-dinitrophenyl)-proline and N-(2,4-dinitrophenyl)-serine in HPLC by BSA chiral stationary phase
Qiuyun Wang, Yajin Xiong, Baozhu Lu, Jun Fan, Sheng Zhang, Shengrun Zheng, Weiguang Zhang J Sep Sci. 2013 Apr;36(8):1343-8. doi: 10.1002/jssc.201201165. Epub 2013 Mar 18.
N-(2,4-dinitrophenyl)-proline and N-(2,4-dinitrophenyl)-serine were enantiomerically resolved on the BSA chiral stationary phase by HPLC in reversed-phase mode. Effects of chromatographic conditions on enantioseparation and elution order have been investigated in detail. For these two samples, reversal of enantiomer elution order was observed by changing buffer pH, the content of acetonitrile, or alcohol modifiers in mobile phase, which is firstly reported in the BSA chiral stationary phase studies. More interestingly, combined effect between buffer pH and the content of acetonitrile was also observed. In addition, coelution range of enantiomers varied along with the content of acetonitrile in mobile phase.
3. Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein
Marcelo Campos, Constance Couture, Izaura Y Hirata, Maria A Juliano, Thomas P Loisel, Philippe Crine, Luiz Juliano, Guy Boileau, Adriana K Carmona Biochem J. 2003 Jul 1;373(Pt 1):271-9. doi: 10.1042/BJ20030287.
The PHEX gene (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) encodes a protein (PHEX) with structural homologies to members of the M13 family of zinc metallo-endopeptidases. Mutations in the PHEX gene are responsible for X-linked hypophosphataemia in humans. However, the mechanism by which loss of PHEX function results in the disease phenotype, and the endogenous PHEX substrate(s) remain unknown. In order to study PHEX substrate specificity, combinatorial fluorescent-quenched peptide libraries containing o -aminobenzoic acid (Abz) and 2,4-dinitrophenyl (Dnp) as the donor-acceptor pair were synthesized and tested as PHEX substrates. PHEX showed a strict requirement for acidic amino acid residues (aspartate or glutamate) in S(1)' subsite, with a strong preference for aspartate. Subsites S(2)', S(1) and S(2) exhibited less defined specificity requirements, but the presence of leucine, proline or glycine in P(2)', or valine, isoleucine or histidine in P(1) precluded hydrolysis of the substrate by the enzyme. The peptide Abz-GFSDYK(Dnp)-OH, which contains the most favourable residues in the P(2) to P(2)' positions, was hydrolysed by PHEX at the N-terminus of aspartate with a k(cat)/ K(m) of 167 mM(-1) x s(-1). In addition, using quenched fluorescence peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein sequences flanked by Abz and N -(2,4-dinitrophenyl)ethylenediamine, we showed that these physiologically relevant proteins are potential PHEX substrates. Finally, our results clearly indicate that PHEX does not have neprilysin-like substrate specificity.
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