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Product Name
Phe-Ala,
Assay
≥98.0% (TLC)
Quality Level
form
powder
color
white
storage temp.
−20°C
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
Gene Information
human ... SLC15A1(6564)
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Bioorganic & medicinal chemistry letters, 14(1), 239-243 (2003-12-20)
We describe herein the syntheses and evaluation of a series of C-termini pyridyl containing Phe*-Ala-based BACE inhibitors (5-19). In conjunction with four fixed residues at the P1 (Phe), P1' (Ala), P2' (Val), and P2' cap (Pyr.), rather detailed SAR modifications
The Journal of organic chemistry, 76(3), 833-839 (2011-01-13)
The synthesis of a novel Phe-Ala dipeptide mimic, built up on a diazaspirocyclic lactam core, is presented. This new scaffold was evaluated for conformational mimicry of reverse turn by combining molecular modeling, IR, NMR, and X-ray diffraction experiments. All these
Journal of cellular physiology, 178(3), 341-348 (1999-02-16)
Di- and tripeptides and peptide mimetics such as beta-lactam antibiotics are efficiently reabsorbed from the tubular lumen by a high-affinity peptide transporter. We have recently identified and characterized this H+-coupled high-affinity peptide transport system in the porcine proximal tubular cell
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
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
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