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| Product Name | Fmoc-Pro-OH |
|---|---|
| Synonyms | N-Fmoc-L-proline; Fmoc-L-proline |
| Catalog No. | AS0808 |
| CAS Number | 71989-31-6 |
| Molecular Formula | C20H19NO4 |
| Molecular Weight | 337.37 g/mol |
| Appearance | White powder |
| Melting Point | 100–118°C |
| Specific Rotation | -32° ± 2° (C=1 in DMF) |
| Storage Temperature | Cool, dry place (≤25°C) |
| Side-Chain Protection | None required |
| Primary Application | Fmoc-SPPS |
Product Overview
Fmoc-Pro-OH is the Fmoc-protected form of L-proline.
Proline differs structurally from most amino acids because its side chain connects back to the backbone nitrogen, forming a five-membered pyrrolidine ring.
This cyclic architecture restricts backbone conformational freedom and gives proline a distinctive role in peptide structure.
Applications in Peptide Synthesis
| Application | Role of Fmoc-Pro-OH |
|---|---|
| Fmoc-SPPS | Standard L-proline building block |
| Turn Formation | Introduces local conformational restriction |
| Proline-Rich Peptides | Used in signaling and protein-interaction motifs |
| Cyclic Peptides | Supports conformationally constrained architectures |
| SAR Studies | Useful for probing backbone geometry |
| Peptide Design | Can reduce local backbone flexibility |
Fmoc-Pro-OH in Fmoc-SPPS
Proline requires no side-chain protecting group.
However, its secondary amine makes its peptide chemistry structurally different from that of ordinary primary α-amino groups.
Coupling to proline and coupling the residue after proline can therefore show different kinetics depending on sequence context.
Proline as a Conformational Constraint
The pyrrolidine ring restricts rotation around the peptide backbone.
This property makes proline useful for:
stabilizing turns
disrupting or terminating α-helices
controlling local geometry
reducing conformational flexibility
designing constrained peptide analogs
Replacing another amino acid with Pro is therefore a much larger structural intervention than a simple side-chain substitution.
Cis/Trans Peptide-Bond Isomerization
Peptide bonds preceding proline show a greater tendency to populate both cis and trans conformations than most peptide bonds.
This can influence:
peptide folding
conformational heterogeneity
biological recognition
chromatographic behavior
In some peptide systems, proline isomerization can even produce multiple conformational peaks without representing different molecular formulas.
Alan Scientific practical view: unusual HPLC behavior in a Pro-containing peptide should not automatically be interpreted as a chemical impurity; conformational isomerism may also need consideration.
Product Documents
A Safety Data Sheet (SDS / MSDS) is available for this product to support laboratory handling, storage and safety assessment.
Related Technical Resources
Explore Standard Fmoc-Amino Acids.
Read Amino Acids & Peptide Building Blocks.
For conformationally constrained peptides, see Custom Peptide Synthesis.
Why Source Peptide Building Blocks from Alan Scientific?
Alan Scientific provides Fmoc-protected amino acids and specialized building blocks for conventional and conformationally complex peptide synthesis.
Research Use Only