产品名称
Phe-Ala,
SMILES string
C[C@H](NC(=O)[C@@H](N)Cc1ccccc1)C(O)=O
InChI
1S/C12H16N2O3/c1-8(12(16)17)14-11(15)10(13)7-9-5-3-2-4-6-9/h2-6,8,10H,7,13H2,1H3,(H,14,15)(H,16,17)/t8-,10-/m0/s1
InChI key
MIDZLCFIAINOQN-WPRPVWTQSA-N
assay
≥98.0% (TLC)
form
powder
color
white
storage temp.
−20°C
Quality Level
Gene Information
human ... SLC15A1(6564)
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
I Knütter et al.
Biochemistry, 40(14), 4454-4458 (2001-04-04)
This study was initiated to develop inhibitors of the intestinal H(+)/peptide symporter. We provide evidence that the dipeptide derivative Lys[Z(NO(2))]-Pro is an effective competitive inhibitor of mammalian PEPT1 with an apparent binding affinity of 5-10 microM. Characterization of the interaction
F Döring et al.
Biochemical and biophysical research communications, 232(3), 656-662 (1997-03-27)
The methylotrophic yeast Pichia pastoris was used for heterologous expression of the rabbit intestinal peptide transporter PepT1 and its functional characterization. PepT1 mediates the electrogenic transmembrane transport of di- and tripeptides and peptido-mimetics such as beta-lactam antibiotics and ACE-inhibitors. Functional
Shu-Hui Chen et al.
Bioorganic & medicinal chemistry letters, 14(1), 245-250 (2003-12-20)
With the aim of reducing molecular weight and adjusting log D value of BACE inhibitors to more favorable range for BBB penetration and better bioavailability, we synthesized and evaluated several series of P3 cap modified BACE inhibitors obtained via replacement
Jaeseung Kim et al.
The Journal of organic chemistry, 70(15), 5781-5789 (2005-07-16)
Four stereoisomers of a Phe-Ala silanediol dipeptide mimic have been evaluated as inhibitors of angiotensin-converting enzyme (ACE) and compared to ketone-based inhibitors reported by Almquist et al. One stereogenic center of the isomers was derived from the individual enantiomers of
D Meredith et al.
The American journal of physiology, 269(2 Pt 1), L137-L143 (1995-08-01)
The transport of a hydrolysis-resistant dipeptide, D-phenylalanyl-L-alanine (D-Phe-L-Ala), has been studied by high-performance liquid chromatography in rat lung epithelial cells and apical membrane vesicles. Time-dependent uptake of D-Phe-L-Ala into isolated type II pneumocytes was shown. Uptake was saturable, and Michaelis-Menten
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