Fmoc-(R)-3-amino-4-(4-methyl-phenyl)-butyric acid
95%
- Product Code: 188257
CAS:
269398-86-9
| Molecular Weight: | 415.481 g./mol | Molecular Formula: | C₂₆H₂₅NO₄ |
|---|---|---|---|
| EC Number: | MDL Number: | MFCD01860929 | |
| Melting Point: | Boiling Point: | 642.2 °C at 760 mmHg | |
| Density: | Storage Condition: | 2-8°C, dry, sealed |
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.
Sizes / Availability / Pricing:
| Size | Availability | Price | Quantity |
|---|---|---|---|
| 250mg | 10-20 days | $88.22 |
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| 1g | 10-20 days | $336.08 |
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Fmoc-(R)-3-amino-4-(4-methyl-phenyl)-butyric acid
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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