Fmoc-(R)-3-amino-4-(4-methyl-phenyl)-butyric acid

95%

Reagent Code: #188257
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CAS Number 269398-86-9

science Other reagents with same CAS 269398-86-9

blur_circular Chemical Specifications

scatter_plot Molecular Information
Weight 415.481 g/mol
Formula C₂₆H₂₅NO₄
badge Registry Numbers
MDL Number MFCD01860929
thermostat Physical Properties
Boiling Point 642.2 °C at 760 mmHg
inventory_2 Storage & Handling
Storage 2-8°C, dry, sealed

description Product Description

Used in peptide synthesis as a chiral building block for constructing structurally modified peptides with enhanced stability and biological activity. The Fmoc group enables solid-phase synthesis by allowing stepwise addition of amino acids under mild conditions. The (R)-3-amino-4-(4-methylphenyl)butyric acid moiety introduces a sterically hindered, hydrophobic side chain that can influence peptide conformation, receptor selectivity, and metabolic resistance. Commonly applied in the development of peptidomimetic drugs, especially in oncology and CNS-targeted therapeutics where aromatic and chiral elements improve target binding. Its structure supports beta-turn formation in peptides, making it valuable in designing foldamers and constrained peptides.

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Size Availability Unit Price Quantity
inventory 250mg
10-20 days ฿2,050.00
inventory 1g
10-20 days ฿7,810.00

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Fmoc-(R)-3-amino-4-(4-methyl-phenyl)-butyric acid
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Used in peptide synthesis as a chiral building block for constructing structurally modified peptides with enhanced stability and biological activity. The Fmoc group enables solid-phase synthesis by allowing stepwise addition of amino acids under mild conditions. The (R)-3-amino-4-(4-methylphenyl)butyric acid moiety introduces a sterically hindered, hydrophobic side chain that can influence peptide conformation, receptor selectivity, and metabolic resistance. Commonly applied in the development of peptidomimetic drugs, especially in oncology and CNS-targeted therapeutics where aromatic and chiral elements improve target binding. Its structure supports beta-turn formation in peptides, making it valuable in designing foldamers and constrained peptides.
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