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The BI-3802 was designed by Boehringer Ingelheim and could be obtained free of charge through the Boehringer Ingelheim open innovation portal opnMe.com, associated with its negative control.
Fmoc-Lys(ivDde)-OH is a lysine derivative that serves as a standard structural unit for amino acid residues in peptide synthesis.
Synonyms: Fmoc-L-Lys(ivDde)-OH
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Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
Search for reports by entering the product batch number.
Batch number can be found on the product's label following the word 'Batch'.
CAS No. : | 204777-78-6 |
Formula : | C34H42N2O6 |
M.W : | 574.71 |
SMILES Code : | O=C(O)[C@H](CCCCN/C(CC(C)C)=C1C(CC(C)(C)CC\1=O)=O)NC(OCC2C3=C(C4=C2C=CC=C4)C=CC=C3)=O |
Synonyms : |
Fmoc-L-Lys(ivDde)-OH
|
MDL No. : | MFCD01631658 |
InChI Key : | LHJJUCZESVFWSO-MHZLTWQESA-N |
Pubchem ID : | 135443653 |
GHS Pictogram: |
![]() |
Signal Word: | Warning |
Hazard Statements: | H302-H315-H319-H335 |
Precautionary Statements: | P261-P305+P351+P338 |
* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
The solid phase synthesis as described in Methods was carried out on Novabiochem Rink-Amide resin (4-(2',4'-Dimethoxyphenyl-Fmoc-aminomethyl)-phenoxyacetamido- norleucylaminomethyl resin), 100-200 mesh, loading of 0.23 mmol/g. The Fmoc- synthesis strategy was applied with HBTU/DIPEA-activation. In position 14 Fmoc- Lys(ivDde)-OH and in position 1 Boc-His(Trt)-OH were used in the solid phase synthesis protocol. The ivDde-group was cleaved from the peptide on resin according to literature (S.R. Chhabra et al., Tetrahedron Lett. 39, (1998), 1603). Hereafter Palm- yGlu-yGlu-OSu was coupled to the liberated amino-group employing DIPEA as base. The peptide was cleaved from the resin with King's cocktail (D. S. King, C. G. Fields, G. B. Fields, Int. J. Peptide Protein Res. 36, 1990, 255-266). The crude product was purified via preparative HPLC on a Waters column (XBridge, BEH130, Prep C18 5muMu) using an acetonitrile/water gradient (both buffers with 0,1 percent TFA). The purified peptide was analysed by LCMS (Method A). Deconvolution of the mass signals found under the peak with retention time 12.61 min revealed the peptide mass 4581 ,5 which is in line with the expected value of 4581 ,1 . Peptide Synthesizer (Protein Technologies Inc) or similar automated synthesizer using standard Fmoc chemistry and HBTU/DIPEA activation. DMF was used as the solvent. Deprotection : 20percent piperidine/DMF for 2 x 2.5 min. Washes: 7 x DMF. Coupling 2:5:10 200 mM AA / 500 mM HBTU / 2M DIPEA in DMF 2 x for 20 min. Washes: 5 x DMF. In cases where a Lys-side-chain was modified, Fmoc-L-Lys(ivDde)-OH or Fmoc-L- Lys(Mmt)-OH was used in the corresponding position. After completion of the synthesis, the ivDde group was removed according to a modified literature procedure (S.R. Chhabra et al., Tetrahedron Lett. 39, (1998), 1603), using 4percent hydrazine hydrate in DMF. The Mmt group was removed by repeated treatment with 1 percent TFA in dichloromethane. The following acylations were carried out by treating the resin with the N-hydroxy succinimide esters of the desired acid or using coupling reagents like HBTU/DIPEA or HOBt/DIC. All the peptides that have been synthesized were cleaved from the resin with King's cleavage cocktail consisting of 82.5percent TFA, 5percent phenol, 5percent water, 5percent thioanisole, 2.5percent EDT The crude peptides were then precipitated in diethyl or diisopropyl ether, centrifuged, and lyophilized. Peptides were analyzed by analytical HPLC and checked by ESI mass spectrometry. Crude peptides were purified by a conventional preparative RP-HPLC purification procedure. |