| Synonym: | Fmoc-Nε-1-(4,4-dimethyl-2,6-dioxocyclohex-1-ylidene)-3-methylbutyl-L-lysine |
| CAS #: | 204777-78-6 |
| Molecular Formula: | C34H42N2O6 |
| Molecular Weight: | 574.7 |
| Fmoc-Lys(ivDde)-OH is especially useful for preparing peptides selectively modified on the Lys sidechain, such as peptides labeled peptides, PEGylated peptides or peptides cyclized through the Lys sidechain. The ivDde protective group possesses higher orthogonality regarding Boc and Fmoc in comparison to Dde. The ivDde group can be selectively removed with hydrazine in the presence of acid labile groups such as t-butyl and trityl based protecting groups. Pros: 1. Selective ε-amino protection: The ivDde group provides excellent stability under standard Fmoc-SPPS conditions and can be selectively removed using hydrazine or hydrazine-based reagents without affecting the Fmoc group. 2. High Purity & Compatibility: It integrates well with automated and manual peptide synthesis techniques. 3. Ideal for Side-Chain Functionalization: Since ivDde is removable under mild conditions, this compound is perfect for introducing modifications like fluorophores, biotin, or PEGylation at the lysine side chain after the peptide sequence is assembled. Cons: 1. Slow ivDde Removal: Compared to other protecting groups like Boc or Alloc, ivDde removal requires excess hydrazine and prolonged reaction times, sometimes leading to incomplete deprotection. 2. Potential Side Reactions: Under harsh conditions, ivDde removal can cause partial peptide degradation or unwanted side reactions. 3. Limited Compatibility with Certain Resins: In some cases, specific resin-bound peptides may show reduced efficiency in deprotection, requiring careful optimization. Fmoc-Lys(ivDde)-OH is an excellent choice for peptide synthesis where selective modification of the lysine side chain is required. It is a must-have reagent for researchers working on multi- functional peptides, cyclic peptides, or labeled peptides. However, careful handling is necessary to optimize ivDde deprotection conditions. References: 1. Chhabra, S. R., et al. (1998). “A Novel Orthogonal Protection Scheme for Solid-Phase Peptide Synthesis Using the ivDde Group.” Tetrahedron Letters, 39(10), 1603-1606. 2. Chandra, K., et al. (2014). “A Tandem In Situ Peptide Cyclization through Trifluoroacetic Acid Cleavage.” Angewandte Chemie International Edition, 53(36), 9450-9455. 3. Fmoc Solid Phase Peptide Synthesis 4. Boc Solid Phase Peptide Synthesis |
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