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The BI-3802 was designed by Boehringer Ingelheim and could be obtained free of charge through the Boehringer Ingelheim open innovation portal opnMe.com, associated with its negative control.
Leucine is one of nine essential amino acids in humans which is important for protein synthesis and many metabolic functions. It contributes to regulation of blood-sugar levels growth and repair of muscle and bone tissue growth hormone production and wound healing.
Synonyms: Leucine; Leu; AI3-08899
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Martina Lioi ; Sara Tengattini ; Roberto Gotti ; Francesca Bagatin ; Stefano Galliani ; Gabriella Massolini , et al.
Abstract: During collagen biosynthesis, proline is post-translationally converted to hydroxyproline by specific enzymes. This amino acid, unique to collagen, plays a crucial role in stabilizing the collagen triple helix structure and could serve as an important biomarker for collagen content and quality analysis. Hydroxyproline has four isomers, depending on whether proline is hydroxylated at position 4 or 3 and on whether the cis- or trans- conformation is formed. Moreover, as extensive hydrolysis of collagen is required for its amino acid analysis, epimerization may also occur, although to a lesser extent, giving a total of eight possible isomers. The aim of the present study was to develop a reversed-phase high-performance liquid chromatography-UV-mass spectrometry (RPLC-UV-MS) method for the separation and quantification of all eight hydroxyproline isomers. After the chiral derivatization of the hydroxyproline isomers with Nα-(2,4-dinitro-5-fluorophenyl)-L-valinamide (L-FDVA), to enable their UV detection, the derivatized diastereoisomers were separated by testing different C18 column technologies and morphologies and optimizing operative conditions such as the mobile phase composition (solvent, additives), elution mode, flow rate and temperature. Baseline resolution of all eight isomers was achieved on a HALO® ES-C18 reversed-phase column (150×1.5 mm, 2.7 μm, 160 Å) using isocratic elution and MS-compatible mobile phase. The optimized method was validated for the quantification of hydroxyproline isomers and then applied to different collagen hydrolysates to gain insight and a deeper understanding of hydroxyproline abundances in different species (human, chicken) and sources (native, recombinant).
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Keywords: Collagen ; Amino acid analysis ; Hydroxyproline isomers ; Recombinant collagen ; Reverse phase chromatography ; Mass spectrometry
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Electrosynthesis of amino acids from biomass-derived α-hydroxyl acids
Kaili Yan ; Morgan L. Huddleston ; Brett A. Gerdes ; Yujie Sun ;
Abstract: Electrochemical conversion of biomass-derived intermediate compounds to high-value products has emerged as a promising approach in the field of biorefinery. Biomass upgrading allows for the production of chemicals from non-fossil-based carbon sources and capitalization on electricity as a green energy input. Amino acids, as products of biomass upgrading, have received relatively little attention. Pharmaceutical and food industries will benefit from an alternative strategy for the production of amino acids that does not rely on inefficient fermentation processes. The use of renewable biomass resources as starting materials makes this proposed strategy more desirable. Herein, we report an electrochemical approach for the selective oxidation of biomass-derived α-hydroxyl acids to α-keto acids, followed by electrochemical reductive amination to yield amino acids as the final products. Such a strategy takes advantage of both reactions at the anode and cathode and produces amino acids under ambient conditions with high energy efficiency. A flow electrolyzer was also successfully employed for the conversion of α-hydroxyl acids to amino acids, highlighting its great potential for large-scale application.
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Antimycobacterial Rufomycin Analogues from Streptomyces atratus Strain MJM3502
Zhou, Bin ; Shetye, Gauri ; Yu, Yang ; Santarsiero, Bernard D. ; Klein, Larry L. ; Abad-Zapatero, Cele , et al.
Abstract: This study represents a systematic chem. and biol. study of the rufomycin (RUF) class of cyclic heptapeptides, which our anti-TB drug discovery efforts have identified as potentially promising anti-TB agents that newly target the caseinolytic protein C1, ClpC1. Eight new RUF analogs, rufomycins NBZ1-NBZ8, as well as 5 known peptides were isolated and characterized from the Streptomyces atratus strain MJM3502. Advanced Marfey's and X-ray crystallog. anal. led to the assignment of the absolute configuration of the RUFs. Several isolates exhibited potent activity against both pathogens M. tuberculosis H37Rv and M. abscessus, paired with favorable selectivity (selectivity index >60), which collectively underscores the promise of the rufomycins as potential anti-TB drug leads.
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CAS No. : | 61-90-5 |
Formula : | C6H13NO2 |
M.W : | 131.17 |
SMILES Code : | CC(C)C[C@H](N)C(O)=O |
Synonyms : |
Leucine; Leu; AI3-08899
|
MDL No. : | MFCD00002617 |
InChI Key : | ROHFNLRQFUQHCH-YFKPBYRVSA-N |
Pubchem ID : | 6106 |
GHS Pictogram: |
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Signal Word: | Warning |
Hazard Statements: | H315-H319-H335 |
Precautionary Statements: | P261-P305+P351+P338 |
* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With hydrogenchloride; In water; at 110℃; for 24h; | Urumamide (1) (0.7 mg) was treated with 9 N HCl (100 L) for 24 h at 110 C. The hydrolyzed product was evaporated to dryness and could be separated into each component by HPLC. [Cosmosil 5C18-PAQ (4.6 × 250 mm); flowrate, 1.0 mL/min; detection at 215 nm; solvent H2O. Retention times (min) of components: N-Me-Ala (tR = 3.0 min), Pro(tR = 3.2 min), Val (tR = 3.4 min), N-Me-Val (tR = 3.7 min), Leu (tR = 4.8 min), N-Me-Ile (tR = 5.3 min), N-Me-Leu (tR =6.0 min)]. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
In aq. buffer; at 37℃;pH 7.3; | General procedure: <strong>[1236199-60-2]NL-101</strong> (0.03 g) was incubated with amino acids (0.02 g) and peptides (0.03 g) at 37 oC in a buffer solution, which pH was 5.3,7.3 and 9.3 respectively as the experimental surroundings. The pH of the samples was determined by a pH-meter (FE 20, MettlerToledo). All samples were kept at -20 oC until further analysis. The desalting step of the <strong>[1236199-60-2]NL-101</strong> adducts obtained under theexperimental conditions was not carried out before MS analysis. |