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Leucyl-phenylalanine Sale

目录号 : GC30131

Leucyl-phenylalanine是二肽的有机化合物。

Leucyl-phenylalanine Chemical Structure

Cas No.:3063-05-6

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50mg
¥446.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

Leucyl-phenylalanine belongs to the class of organic compounds known as dipeptides.

Chemical Properties

Cas No. 3063-05-6 SDF
Canonical SMILES O=C(O)[C@H](CC1=CC=CC=C1)NC([C@H](CC(C)C)N)=O
分子式 C15H22N2O3 分子量 278.35
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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1 mM 3.5926 mL 17.963 mL 35.926 mL
5 mM 0.7185 mL 3.5926 mL 7.1852 mL
10 mM 0.3593 mL 1.7963 mL 3.5926 mL
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Research Update

Formyl-methionyl-leucyl-phenylalanine-induced intestinal inflammation

The main functions and structural modifications of tripeptide N-formyl-methionyl-leucyl-phenylalanine (fMLP) as a chemotactic factor

Gram negative bacteria-derived and synthetic N-formyl peptides play a key role in host defense as chemotactic factors for phagocytic leukocytes. The first compound to be identified was N-formylmethionyl-leucyl-phenylalanine (fMLP) which contains highly potent leukocyte chemoattractant. Natural fMLP was subsequently purified and identified in supernatants of gram negative bacteria. Recently, much more attention has been focused on the human formyl peptide receptor (FPR) and its variant formyl peptide receptor-like 1 (FPRL1) and formyl peptide receptor-like 2 (FPRL2). Chemotactic factors such as fMLP interact with their specific cell surface receptors, which results in multiple biological responses through a G protein-coupled signal pathway. In this review, the functions and structural modifications of fMLP are discussed in view of future drug development.

Formyl-methionyl-leucyl-phenylalanine induces prostaglandin E2 release from human amnion-derived WISH cells by phospholipase C-mediated [Ca+]i rise

The presence of binding sites for formyl-methionyl-leucyl-phenylalanine (fMLP), its effect on prostaglandin E (PGE) release, and the signal transduction pathway activated by the peptide were investigated in human amnion-derived WISH cells. Our results demonstrate that specific binding sites for fMLP are present on WISH cells and that the peptide induces a significant increase of prostaglandin (PG)E2 release. The kinetic properties of binding are similar to those previously found in amnion tissue prior to the onset of labor, i.e., only one population of binding sites with low affinity for the peptide is present. Binding of 3H-fMLP in WISH cells is inhibited by N-t-butoxycarbonyl-methionyl-leucyl-phenylalanine, an fMLP receptor antagonist, with an IC50 value very close to that shown by nonlaboring amnion. The fMLP-induced PGE2 output is inhibited by indomethacin, quinacrine, and U-73122, inhibitors of cyclooxygenase, phospholipase A2, and phospholipase C, respectively. As regards the transduction pathway activated by fMLP, we demonstrate that phospholipase C activation, followed by an increase of intracellular calcium concentration ([Ca2+]i), is involved in response to the peptide. Our results add further evidence to the role of proinflammatory agents in the determination of labor. Furthermore, because WISH cells appear to behave like nonlaboring amnion tissue, they represent the ideal candidate for in vitro investigation of the events triggering the mechanism of delivery.

Effect of N-formylated methionyl-phenylalanine (FMP) and methionyl-leucyl-phenylalanine (FMLP) on gut permeability. A model of local inflammatory process

With the aim of elucidating inflammatory reactions in intestinal mucosa evoked by agents of microbial origin, the effect was assessed on intestinal permeability in the rat of two known chemoattractants for granulocytes and macrophages, N-formyl-methionyl-phenylalanine (FMP) and N-formyl-methionyl-leucyl-phenylalanine (FMLP). Fluoresceinated dextran (mol wt 3000 daltons) was used as a permeability marker. It was found that increasing concentrations of FMP enhanced the transmural passage up to a maximum at 2 X 10(-7)-2 X 10(-6)M. With FMLP the effect was greater than with FMP and measurable at 2 X 10(-9)-2 X 10(-8)M. The increased permeability was apparent 1-5 min after introduction of the peptides and prevailed during the 45-min measuring period. The bimodal response to the peptides is discussed in relation to different potential target-effector cells in the intestinal wall.

Anti-formyl peptide antibodies

Antibodies that selectively bind to N-formylmethionyl leucyl phenylalanine (fMLF, also known as fMLP) have been generated. These antibodies bound to fMLF with higher affinity than to non-formylated peptide MLF: the differences in the binding energies between fMLF and MLF were 1.4->2.1 kcal/mol.