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| Product Name | Fmoc-Phe-OH |
|---|---|
| Synonyms | Nα-Fmoc-L-phenylalanine; Fmoc-L-phenylalanine |
| Catalog No. | AS0305 |
| CAS Number | 35661-40-6 |
| Molecular Formula | C24H21NO4 |
| Molecular Weight | 387.43 g/mol |
| Appearance | White powder |
| Melting Point | 180–195°C |
| Specific Rotation | -38° ± 2.5° (C=1 in DMF) |
| Storage Temperature | Cool, dry place (≤25°C) |
| Side-Chain Protection | None required |
| Primary Application | Fmoc-SPPS |
Product Overview
Fmoc-Phe-OH is the Fmoc-protected form of L-phenylalanine, an aromatic hydrophobic amino acid widely used in peptide synthesis.
Its benzyl side chain requires no additional protection during conventional Fmoc-SPPS.
Phenylalanine is particularly important where aromatic hydrophobic interactions contribute to peptide folding, self-association or target binding.
Applications in Peptide Synthesis
| Application | Role of Fmoc-Phe-OH |
|---|---|
| Fmoc-SPPS | Standard L-phenylalanine building block |
| Aromatic Peptides | Introduces a phenyl side chain |
| Hydrophobic Binding Motifs | Supports hydrophobic and aromatic interactions |
| SAR Studies | Useful for probing aromatic recognition |
| Peptide Libraries | Standard proteinogenic residue |
| Self-Assembling Peptides | Frequently used in aromatic-rich peptide architectures |
Fmoc-Phe-OH in Fmoc-SPPS
No side-chain protection is necessary.
The α-carboxyl group is activated for peptide coupling, while the Fmoc-protected α-amino group is subsequently deprotected under standard basic conditions.
Aromaticity, π Interactions and Peptide Design
The phenyl side chain can contribute to:
hydrophobic packing
aromatic stacking
protein-binding interfaces
membrane interactions
peptide self-association
As a result, Phe→Ala, Phe→Leu or Phe→Tyr substitutions can produce effects that go beyond simple hydrophobicity changes.
Phe-Rich Sequences Can Become Difficult to Synthesize
Clusters of aromatic and hydrophobic residues can promote aggregation of the resin-bound peptide chain.
This can reduce solvent penetration and produce incomplete coupling or deletion impurities.
Phe-rich sequences may therefore require synthesis optimization even though Fmoc-Phe-OH itself is chemically straightforward.
Alan Scientific practical view: difficult peptide synthesis should be evaluated at the sequence level, not by assuming that a standard amino acid must always behave as a standard coupling step.
RP-HPLC Considerations
Phenylalanine generally increases peptide hydrophobicity and can contribute to stronger retention in reversed-phase chromatography.
For peptides containing multiple aromatic residues, purification behavior can therefore differ substantially from peptides of similar length but lower hydrophobicity.
Explore Peptide Purification & Quality Control for related technical resources.
Product Documents
A Safety Data Sheet (SDS / MSDS) is available for this product to support laboratory handling, storage and safety assessment.
Related Technical Resources
Browse Standard Fmoc-Amino Acids.
Read Amino Acids & Peptide Building Blocks.
For difficult aromatic sequences, see Custom Peptide Synthesis.
Why Source Peptide Building Blocks from Alan Scientific?
Alan Scientific supplies protected amino acids and specialized peptide building blocks for research and peptide synthesis applications.
Research Use Only