144120-54-7Relevant articles and documents
Fluorophore-labeled, peptide-based glycoclusters: Synthesis, binding properties for lectins, and detection of carbohydrate-binding proteins in cells
Tian, Xizhe,Pai, Jaeyoung,Baek, Kyung-Hwa,Ko, Sung-Kyun,Shin, Injae
, p. 2107 - 2113 (2011)
A facile and efficient solid-phase synthesis of linear peptide-based glycoclusters with various valences and different spatial arrangements of the sugar ligands is described. The synthetic strategy includes 1) solid-phase synthesis of fluorophore-labeled, alkyne-containing peptides, 2) coupling of azide-linked, unprotected mono-, di-, and trisaccharides to the alkyne-conjugated peptides on a solid support by click chemistry, and 3) release of the fluorophore-labeled glycoclusters from the solid support. By using this methodology, 32 fluorescent glycoclusters with a valence ranging from 1 to 4 and different spatial arrangements of the sugar ligands were prepared. Lectin-binding properties of the glycoclusters were initially examined by using microarrays immobilized by various lectins. These glycoclusters were then employed to detect the cell-surface carbohydrate-binding proteins in bacteria. Finally, the uptake of glycoclusters by mammalian cells through receptor-mediated endocytosis was evaluated. The results, obtained from the in vitro and in vivo studies, indicate that the binding affinities toward immobilized and cell-surface proteins are highly dependent on the valence and spatial arrangements of the sugar ligands in glycoclusters.
α-Selective Lysine Ligation and Application in Chemical Synthesis of Interferon Gamma
Dao, Yuankun,Han, Lin,Wang, Hanxuan,Dong, Suwei
, (2019)
A traceless β-mercaptan-assisted α-selective ligation of N-terminal lysine-containing peptides has been developed. In this ligation-desulfurization-based protocol, the ?-amine of lysine is free of protection, thus improving the overall synthetic efficiency and avoiding harsh reactions in preparing large peptides and proteins. The applicability of this methodology has been demonstrated in the synthesis of an acid-labile therapeutic protein, interferon gamma, and the anticancer activity of synthetic protein has also been evaluated.
Rhodium(I) and Iridium(I) N-Heterocyclic carbene complexes of imidazolium functionalized amino acids and peptides
Daubit, Isabelle Marie,Wolf, Jonas,Metzler-Nolte, Nils
, (2020/01/13)
The conjugation of organometallic complexes to peptides is generally achieved through covalent organic linkages of the metal's ligand to the peptide. Examples of direct coordination to metal centers by amino acid side chain residues remain rare. In one such example, side chain methylation of the natural amino acid histidine (His) resulted in an imidazolium functionalized amino acid which was used for the synthesis of rhodium(I), iridium(I), iridium(III), palladium(II) and ruthenium(III) N-heterocyclic carbene (NHC) complexes of the single amino acid and peptides containing this amino acid. Here, we have synthesized two new, non-natural imidazolium functionalized amino acid derivatives, which were used for solid phase peptide synthesis and for the synthesis of [M(COD)(NHC)Cl] (COD = 1,5 cyclooctadiene) complexes of Rh(I) and Ir(I). In total, six new complexes of the single amino acids and four complexes where the amino acids are present in a peptide environment were synthesized. Their characterization provides convincing evidence of conversion of the imidazolium moiety to an NHC ligand and thus the presence of a direct metal-carbon bond between the metal center and the amino acid side chain. Therefore, our compounds represent unique examples of peptide-conjugated complexes that bear the potential to be used for the synthesis of N-heterocyclic carbene complexes conjugated to cancer cell targeting peptides.
Solid-phase parallel synthesis of functionalised medium-to-large cyclic peptidomimetics through three-component coupling driven by aziridine aldehyde dimers
Treder, Adam P.,Hickey, Jennifer L.,Tremblay, Marie-Claude J.,Zaretsky, Serge,Scully, Conor C. G.,Mancuso, John,Doucet, Annie,Yudin, Andrei K.,Marsault, Eric
, p. 9249 - 9255 (2015/06/16)
The first solid-phase parallel synthesis of macrocyclic peptides using three-component coupling driven by aziridine aldehyde dimers is described. The method supports the synthesis of 9- to 18-membered aziridine-containing macrocycles, which are then functionalized by nucleophilic opening of the aziridine ring. This constitutes a robust approach for the rapid parallel synthesis of macrocyclic peptides. Solid-phase macrocycles: The first solid-phase parallel synthesis of macrocyclic peptides using three-component coupling driven by aziridine aldehyde dimers is described. The method supports the synthesis of 9- to 18-membered aziridine-containing macrocycles, which are then functionalised by nucleophilic opening of the aziridine ring (see scheme). This constitutes a robust approach for the rapid parallel synthesis of macrocyclic peptides.
Versatile selective α-carboxylic acid esterification of N-protected amino acids and peptides by alcalase
Nuijens, Timo,Cusan, Claudia,Kruijtzer, John A. W.,Rijkers, Dirk T. S.,Liskamp, Rob M. J.,Quaedflieg, Peter J. L. M.
experimental part, p. 809 - 814 (2009/07/11)
Under continuous removal of water, the industrial protease Alcalase allows selective synthesis of α-carboxylic acid methyl, ethyl, benzyl, allyl, 2-(trimethylsilyl)ethyl, and tert-butyl esters of amino acids and peptides under mild conditions in very high
Selective tert-butyl ester deprotection in the presence of acid labile protecting groups with use of ZnBr2
Kaul, Ramesh,Brouillette, Yann,Sajjadi, Zohreh,Hansford, Karl A.,Lubell, William D.
, p. 6131 - 6133 (2007/10/03)
Chemoselective hydrolysis of tert-butyl esters in the presence of other acid-labile groups has been explored by employing α-amino esters and ZnBr2 in DCM. Although N-Boc and N-trityl groups were found to the labile, PhF protected amines were compatible with these Lewis acid deprotection conditions such that a variety of N-(PhF)amino acids were prepared in good yields from their corresponding tert-butyl esters.
A novel, convenient, three-dimensional orthogonal strategy for solid-phase synthesis of cyclic peptides
Kates,Sole,Johnson,Hudson,Barany,Albericio
, p. 1549 - 1552 (2007/10/02)
Head-to-tail cyclic peptides are made by an efficient three-dimensional orthogonal solid-phase strategy (Fmoc/tBu/allyl), featuring side-chain anchoring to PAC or PAL supports, selective palladium (0)-catalyzed allyl removal, and resin-bound cyclization mediated by BOP/HOBt/DIEA.
Synthesis of 'head-to-tail' cyclized peptides on solid support by Fmoc chemistry
Trzeciak,Bannwarth
, p. 4557 - 4560 (2007/10/02)
Two cyclic peptides were synthesized directly on solid support by 'head-to-tail' cyclizations. Key features are side chain attachment of an Asp residue to an amide or a hydroxy linker and orthogonal protection of the α-carboxyl function of this amino acid as allyl ester. Cyclization was performed with TBTU as coupling reagent. Depending on the attachment the cyclic peptides contain either an Asp or an Asn residue. The method is also applicable to Glx-containing cyclic peptides.
