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L-Lysine hydrate Sale

目录号 : GC66490

L-Lysine hydrate 是一种必需氨基酸。L-Lysine hydrate 可用于血管钙化 (VC) 和急性胰腺炎的研究。

L-Lysine hydrate Chemical Structure

Cas No.:39665-12-8

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产品描述

L-Lysine hydrate is an essential amino acid. L-Lysine hydrate can be research for vascular calcification (VC) and acute pancreatitis[1][2].

L-Lysine hydrate (VSMCs) suppresses plasma iPTH and elevates plasma alanine, proline, plasma arginine, and homo arginine, thereby inhibiting apoptosis of VSMCs and mineral precipitation[1].

L-Lysine hydrate (40 μg/kg; p.o.) ameliorates arterial calcification in adenine rats and protects the femora from osteoporotic changes in adenine rats[1].
L-Lysine hydrate (10 and 400 mg/kg; i.g. and p.o.; Male mice) inhibits pancreatic tissue damage[2].

Animal Model: Male mice[2]
Dosage: 10 and 400 mg/kg
Administration: Intraperitoneal injection and oral administration; for 15 days
Result: Inhibited the release of the inflammatory cytokine IL-6 and enhance antioxidant activity.

[1]. Shimomura A, et, al. Dietary L-lysine prevents arterial calcification in adenine-induced uremic rats. J Am Soc Nephrol. 2014 Sep;25(9):1954-65.
[2]. Al-Malki AL. Suppression of acute pancreatitis by L-lysine in mice. BMC Complement Altern Med. 2015 Jun 23;15:193.

Chemical Properties

Cas No. 39665-12-8 SDF Download SDF
分子式 C6H16N2O3 分子量 164.2
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1 mg 5 mg 10 mg
1 mM 6.0901 mL 30.4507 mL 60.9013 mL
5 mM 1.218 mL 6.0901 mL 12.1803 mL
10 mM 0.609 mL 3.0451 mL 6.0901 mL
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Research Update

L-Lysine and l-arginine inhibit myosin aggregation and interact with acidic amino acid residues of myosin: The role in increasing myosin solubility

Food Chem 2018 Mar 1;242:22-28.PMID:29037682DOI:10.1016/j.foodchem.2017.09.033.

The objective of this paper is to investigate the potential affecting mechanisms of L-Lysine (Lys)/l-arginine (Arg) on myosin solubility. The results showed that both Lys and Arg increased the solubility of myosin at the examined pH values. Additionally, both Lys and Arg decreased the hydrodynamic size of myosin but increased the hydration capacity (HC), the surface aromatic hydrophobicity of myosin, the surface tension of the myosin solution and the absolute transfer free energy (TFE) of the major amino acids that constitute myosin. The results indicate that the properties of Lys or Arg that result in an inhibition of myosin aggregation and an interaction with hydrophobic amino acid residues may play important roles in increasing the myosin solubility. The results are attractive to the meat industry.

Poly(L-proline) II helix propensities in poly(L-Lysine) dendrigraft generations from vibrational Raman optical activity

Biomacromolecules 2009 Jun 8;10(6):1662-4.PMID:19499952DOI:10.1021/bm9002249.

Vibrational Raman optical activity (ROA), measured as small circularly polarized components in Raman scattering from chiral molecules, was applied to study the backbone conformations of the first five generations of poly(L-Lysine) dendrigrafts (DGLs) in water. Generation 1 was found to support predominantly the poly(L-proline) II (PPII) conformation, the amount of which steadily decreased with increasing generation, with a concomitant increase in other backbone conformations. This behavior may be due to increasing crowding of the lysine side chains, together with suppression of backbone hydration, with increasing branching. In contrast, the ROA spectra of a series of linear poly(L-Lysine)s in water show little change with increasing molecular weight. Our results may have implications for the nonimmunogenic properties of DGLs.

L-Lysine: exploiting powder X-ray diffraction to complete the set of crystal structures of the 20 directly encoded proteinogenic amino acids

Angew Chem Int Ed Engl 2015 Mar 23;54(13):3973-7.PMID:25651303DOI:10.1002/anie.201411520.

During the last 75 years, crystal structures have been reported for 19 of the 20 directly encoded proteinogenic amino acids in their natural (enantiomerically pure) form. The crystal structure is now reported for the final member of this set: L-Lysine. As crystalline L-Lysine has a strong propensity to incorporate water under ambient atmospheric conditions to form a hydrate phase, the pure (non-hydrate) crystalline phase can be obtained only by dehydration under rigorously anhydrous conditions, resulting in a microcrystalline powder sample. For this reason, modern powder X-ray diffraction methods have been exploited to determine the crystal structure in this final, elusive case.

Molecular modeling of interactions between L-Lysine and functionalized quartz surfaces

J Phys Chem B 2006 Mar 16;110(10):4836-45.PMID:16526721DOI:10.1021/jp0508610.

Molecular modeling techniques have been used to investigate the interaction of L-Lysine in aqueous medium with silanol and methyl sites onto quartz substrates. The substrate effect has been studied for partially hydrophilic surfaces formed by silanol and methyl groups with a ratio of 1:5 and hydrophobic fully methylated surfaces. Molecular dynamics and static calculations indicate that L-Lysine does not show any significant interaction with fully methylated surfaces, while its interaction with hydroxylated/methylated surfaces is dominated by electrostatic and H-bond terms. Accordingly, on fully methylated surfaces there is no preferential orientation of L-Lysine with respect to the surface, while for hydroxylated/methylated surfaces the L-lysine-surface interaction mainly depends on the molecular orientation, with a preferred geometry involving the ammonium group pointing toward the silanol site. The structure of water shells around L-Lysine molecules was shown to be strongly affected by the relative hydrophilic/hydrophobic character of the surfaces. In particular, the order is almost completely lost for partially hydrophilic surfaces, while well-defined hydration shells around L-Lysine are obtained for hydrophobic surfaces.

Volumetric characterization of homopolymeric amino acids

Biopolymers 2003 Dec;70(4):563-74.PMID:14648766DOI:10.1002/bip.10526.

We have determined the partial molar volumes, expansibilities, and adiabatic compressibilities for poly(L-alanine), poly(L-proline), and poly(L-threonine) within the temperature range of 18-55 degrees C. In addition, we have determined at 25 degrees C changes in volume, DeltaV, and adiabatic compressibility, DeltaK(S), associated with the coil-to-helix transitions of poly(L-Lysine) and poly(L-glutamic acid) and the alpha-to-beta transition of poly(L-Lysine). We have interpreted our volumetric data as suggesting that poly(L-alanine) and poly(L-proline) are not fully unfolded and, probably, retain some solvent-inaccessible core. Further, we propose that poly(L-threonine) is fully unfolded with the majority of its atomic groups being solvent-exposed. Near zero changes in volume and compressibility accompanying the coil-to-helix transitions of poly(L-Lysine) and poly(L-glutamic acid) suggest that, in the absence of fortuitous compensations, the coil-to-helix transitions of the polypeptides do not result in any significant enhancement of solute hydration. By contrast, the alpha-to-beta transition of poly(L-Lysine) causes slight but statistically significant increases in volume and compressibility, an observation that may suggest that the beta-sheet conformation of poly(L-Lysine) is slightly less hydrated than its alpha-helical conformation. In general, our results provide a quantitative volumetric description of the hydration properties of the homopolymeric polypeptides investigated. Such characterizations should prove useful in developing an understanding of the role that solvent plays in the stabilization/destabilization of folded protein structures and protein complexes.