C9405
Z-D-Phe-Phe-Gly
≥97% (TLC)
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About This Item
Fórmula empírica (notación de Hill):
C28H29N3O6
Número de CAS:
Peso molecular:
503.55
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
assay
≥97% (TLC)
storage temp.
−20°C
SMILES string
OC(=O)CNC(=O)C(Cc1ccccc1)NC(=O)C(Cc2ccccc2)NC(=O)OCc3ccccc3
Biochem/physiol Actions
Virus replication inhibitor.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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A R Dentino et al.
Biochimica et biophysica acta, 1235(2), 213-220 (1995-05-04)
The anti-viral and membrane fusion inhibitor, carbobenzoxy-D-phenylalanine-L-phenylalanine-glycine (ZfFG), was studied in phospholipid bilayers, where earlier studies had indicated this peptide functioned. Multinuclear magnetic resonance (NMR) studies were performed with isotopically labeled peptide. A peptide labeled in the glycine carboxyl with
R M Epand et al.
Biochimica et biophysica acta, 1152(1), 128-134 (1993-10-10)
The peptide ZfFG is known to inhibit non-bilayer phase formation as well as vesicle-vesicle and viral fusion. In order to ascertain some of the properties or structural features of this peptide which were important for the inhibition of membrane fusion
P L Yeagle et al.
Biochemistry, 31(12), 3177-3183 (1992-03-31)
The mechanism by which the hydrophobic peptide Z-D-Phe-L-PheGly inhibits membrane fusion was investigated. Differential scanning calorimetry, 2H nuclear magnetic resonance (NMR), and 13C NMR of phosphatidylcholine bilayers in the presence of Z-D-Phe-L-PheGly indicate that this hydrophobic peptide penetrates the phospholipid
P L Yeagle et al.
Biochemistry, 32(45), 12197-12202 (1993-11-16)
The influence of the antiviral peptide, carbobenzoxy-D-phenylalanyl-L-phenylalanylglycine (ZfFG), on the average conformation of phosphatidylcholine in hydrated bilayers was investigated with multinuclear solid state magnetic resonance (NMR). Phosphatidylcholine was specifically deuterated (separately) in the choline N-methyls, the alpha and beta positions
Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the F1 or HA2 viral polypeptides.
C D Richardson et al.
Virology, 105(1), 205-222 (1980-08-01)
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