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Chemical Structure| 61-90-5 Chemical Structure| 61-90-5

Structure of H-Leu-OH
CAS No.: 61-90-5

Chemical Structure| 61-90-5

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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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Heiser, Brittany J ; Lewis, Mae M ; Zerankeshi, Meysam Mohammadi ; Netemeyer, Emily K ; Hernandez, Ashlee M ; Marras, Alexander E , et al.

Abstract: Aerosolized lipid nanoparticles (LNPs) delivering mRNA are an attractive strategy for use in local, inhalable therapy to treat patients with lung diseases. However, a major barrier to delivering aerosolized mRNA LNPs is the shear forces encountered during aerosolization. These forces lead to significant morphology changes and subsequent decrease in efficacy of mRNA delivery. To best retain the physicochemical properties of mRNA LNPs during aerosolization, we took a formulation-based strategy to stabilize LNPs. We used a design-of-experiment (DOE) approach to comprehensively screen rationally chosen excipients at multiple concentrations. Excipients were carefully selected based on their use in clinically approved inhaled products or their ability to support lipid membrane properties. These excipients were added to the same mRNA LNP composition after formulation, were subsequently characterized, and used to transfect human lung cells at air–liquid interface. From this systematic screen, we identified that the addition of our lead candidate, poloxamer 188, best stabilizes LNP size throughout aerosolization and enhances mRNA expression after aerosolization. Additional morphological studies of the inclusion of poloxamer 188 in LNPs suggests that the excipient lowers aerosolization induced fusion or aggregation of particles without altering the internal structure. Our results indicate that poloxamer 188 can support aerosolized mRNA LNP delivery by maintaining LNP size and significantly enhancing therapeutic nucleic acid delivery to lung cells.

Purchased from AmBeed: ;

Martina Lioi ; Sara Tengattini ; Roberto Gotti ; Francesca Bagatin ; Stefano Galliani ; Gabriella Massolini , et al.

Abstract: During collagen biosynthesis, is post-translationally converted to 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. has four isomers, depending on whether 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 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 isomers. After the chiral derivatization of the 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 isomers and then applied to different collagen hydrolysates to gain insight and a deeper understanding of abundances in different species (human, chicken) and sources (native, recombinant).

Keywords: Collagen ; Amino acid analysis ; isomers ; Recombinant collagen ; Reverse phase chromatography ; Mass spectrometry

Purchased from AmBeed: ; ; ;

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.

Purchased from AmBeed: ; ; ; ; 56-40-6 ; 156-06-9 ; ; ; ; ; ; ; ; 828-01-3

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.

Purchased from AmBeed: ; ; ; 621-44-3

Alternative Products

Product Details of H-Leu-OH

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

Safety of H-Leu-OH

GHS Pictogram:
Signal Word:Warning
Hazard Statements:H315-H319-H335
Precautionary Statements:P261-P305+P351+P338

Related Pathways of H-Leu-OH

PI3K-AKT

Isoform Comparison

Biological Activity

In Vitro:

Cell Line
Concentration Treated Time Description References
human induced pluripotent stem cell-derived hypothalamic neurons 500 μM To characterize rapid neuronal responses to physiological changes in extracellular L-Leucine concentration. Results showed that 10.4% of neurons were activated and 15.6% were inhibited by leucine. Mol Metab. 2018 Apr;10:14-27
murine mediobasal hypothalamic neurons 500 μM 10 minutes To characterize rapid neuronal responses to physiological changes in extracellular L-Leucine concentration. Results showed that 9% of neurons were activated and 14% were inhibited by leucine. Mol Metab. 2018 Apr;10:14-27
C2C12 murine myotubes 10mM 24 hours Hyperammonemia significantly reduced protein synthesis J Hepatol. 2016 Nov;65(5):929-937
Brain microvascular endothelial cells (BMECs) 1 mM 45 minutes To evaluate the competitive relationship between L-leucine and kynurenine in blood-brain barrier transport, showing that L-leucine inhibits kynurenine influx via LAT1. Mol Psychiatry. 2019 Oct;24(10):1523-1532

In Vivo:

Species
Animal Model
Administration Dosage Frequency Description References
Mice Fasted mice Ex vivo slice culture 500 μM 45 minutes To investigate the effect of L-leucine on AGRP secretion in hypothalamic slices from fasted mice. Results showed that leucine significantly suppressed AGRP secretion. Mol Metab. 2018 Apr;10:14-27
C57BL/6J mice Resistance exercise model Oral gavage 0.4 g/kg body weight Administered acutely or 48 h after exercise cessation, with samples taken 30 min after administration To investigate the long-term enhanced sensitivity of mTORC1 to leucine following exercise. Results showed that leucine supplementation more potently activated mTORC1 and protein synthesis in acutely exercised muscle, and this effect was maintained at least 48 h after exercise. Mol Metab. 2022 Dec;66:101615

Protocol

Bio Calculators
Preparing Stock Solutions 1mg 5mg 10mg

1 mM

5 mM

10 mM

7.62mL

1.52mL

0.76mL

38.12mL

7.62mL

3.81mL

76.24mL

15.25mL

7.62mL

Dissolving Methods
The prepared working fluid is recommended to be prepared now and used up as soon as possible in a short period of time. The percentage shown in front of the following solvent refers to the volume ratio of the solvent in the final solution; If precipitation or precipitation occurs in the preparation process, it can be assisted by heating and/or ultrasound.
Protocol 1

References

 

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