Fmoc-Lys(Dde)-OH: Advancing Peptide Synthesis
Unlock complex peptide structures with this essential building block for Fmoc SPPS.
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Fmoc-Lys(Dde)-OH
Fmoc-Lys(Dde)-OH is a vital protected amino acid derivative integral to Fmoc solid-phase peptide synthesis (SPPS). Its unique orthogonal protection scheme, featuring the acid-labile Dde group on the epsilon-amino position and the base-labile Fmoc group on the alpha-amino position, allows for precise and controlled peptide chain elongation.
- Explore the synthesis of branched peptides using Fmoc-Lys(Dde)-OH, offering advanced structural possibilities.
- Understand the selective deprotection of the Dde group in peptide synthesis, crucial for step-wise modifications.
- Learn about the orthogonality of Fmoc and Dde protecting groups, enabling sequential and independent deprotection steps.
- Discover how di-epitopic peptide synthesis strategies leverage this compound for creating peptides with multiple bioactive regions.
Key Advantages
Controlled Deprotection
Master the selective deprotection of Dde group in peptide synthesis, ensuring modified side chains are precisely altered without affecting the main chain.
Structural Versatility
Achieve branched peptide synthesis with Fmoc-Lys(Dde)-OH, creating complex architectures essential for advanced research and therapeutics.
Synthetic Efficiency
The orthogonality of Fmoc and Dde protecting groups streamlines complex peptide synthesis, reducing side reactions and improving yields.
Key Applications
Branched Peptides
Utilize Fmoc-Lys(Dde)-OH for the synthesis of branched peptides, enabling the attachment of multiple peptide chains to a single core lysine residue.
Di-epitopic Peptides
Facilitate di-epitopic peptide synthesis strategies by using Fmoc-Lys(Dde)-OH to introduce distinct epitopes at specific points in the peptide sequence.
Cyclic Peptides
Contribute to the cyclic peptide construction methods by allowing for controlled cyclization through selective side-chain functionalization.
Lysine Side-Chain Modification
Enable precise lysine side-chain modification in SPPS, crucial for developing peptides with enhanced stability, targeting, or signaling capabilities.