P4126
Phe-Phe
≥98% (TLC)
Synonym(s):
L-Phenylalanyl-L-phenylalanine, Di-L-phenylalanine
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About This Item
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Product Name
Phe-Phe,
Assay
≥98% (TLC)
Quality Level
form
powder
color
white
storage temp.
−20°C
SMILES string
N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc2ccccc2)C(O)=O
InChI
1S/C18H20N2O3/c19-15(11-13-7-3-1-4-8-13)17(21)20-16(18(22)23)12-14-9-5-2-6-10-14/h1-10,15-16H,11-12,19H2,(H,20,21)(H,22,23)/t15-,16-/m0/s1
InChI key
GKZIWHRNKRBEOH-HOTGVXAUSA-N
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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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Journal of colloid and interface science, 368(1), 226-230 (2011-12-02)
In this study, it was found that macroporous hydrogels were formed when self-assembly of fluorenyl-9-methoxycarbonyl (Fmoc)-diphenylalanine (Phe-Phe) peptides was induced using glucono-δ-lactone (GdL) in apparently frozen samples. Formed cryogels exhibited a heterogeneous structure with pore walls of densely packed fibres
Biophysical journal, 77(3), 1428-1444 (1999-08-31)
The interaction of three bioactive peptides, bombesin, beta-endorphin, and glucagon with a phosphatidylcholine monolayer that was immobilized to porous silica particles and packed into a stainless steel column cartridge, has been studied using dynamic elution techniques. This immobilized lipid monolayer
Journal of the American Chemical Society, 133(5), 1212-1215 (2011-01-05)
Chirality reversal of a residue in a peptide can change its mode of binding to a metal ion, as shown here experimentally by gas-phase IR spectroscopy of peptide-metal ion complexes. The binding conformations of Li(+), Na(+), and H(+) with the
Supramolecular nanofibers and hydrogels of nucleopeptides.
Angewandte Chemie (International ed. in English), 50(40), 9365-9369 (2011-09-29)
The FEBS journal, 277(21), 4549-4561 (2010-09-30)
Candida albicans exo-β-1,3-glucanase (Exg; EC 3.2.1.58) is implicated in cell wall β-D-glucan remodelling through its glucosyl hydrolase and/or transglucosylase activities. A pair of antiparallel phenylalanyl residues (F144 and F258) flank the entrance to the active site pocket. Various Exg mutants
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