1059596-58-5

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 106-45-6 para-thiocresol 

Downstream Products

• 1059597-07-7 (S)-benzyl 3-oxo-1-phenylhex-5-en-2-ylcarbamate 
• 921793-46-6 (S)-benzyl 1-oxo-3-phenyl-1-p-tolylpropan-2-ylcarbamate 
• 1059597-15-7 (S)-benzyl 1-(4-chlorophenyl)-1-oxo-3-phenylpropan-2-ylcarbamate 
• 1059597-17-9 (S)-benzyl 1-oxo-3-phenyl-1-(pyridin-3-yl)propan-2-ylcarbamate 
• 1059597-20-4 (S,Z)-benzyl 3-oxo-1-phenylhex-4-en-2-ylcarbamate 
• 1059597-13-5 (S)-benzyl 1-(4-methoxyphenyl)-1-oxo-3-phenylpropan-2-ylcarbamate 
• 1059596-99-4 (S)-benzyl 1-oxo-3-phenyl-1-(thiophen-2-yl)propan-2-ylcarbamate 
• 1059597-01-1 (S)-benzyl 1-(1-methyl-1H-pyrrol-2-yl)-1-oxo-3-phenylpropan-2-ylcarbamate 
• 1059597-18-0 (S)-benzyl 1-(naphthalen-1-yl)-1-oxo-3-phenylpropan-2-ylcarbamate 
• 1059597-16-8 (S)-benzyl 1-oxo-3-phenyl-1-(pyridin-2-yl)propan-2-ylcarbamate 
• 1059597-03-3 (S)-benzyl 1-(1-methyl-1H-indol-2-yl)-1-oxo-3-phenylpropan-2-ylcarbamate 
• 34834-26-9 Cbz-L-Phe-L-Cys-OMe 
• 1346756-66-8 N-Cbz-L-Phe-L-Ser-OEt 
• 5276-63-1 Z-L-Phe-L-Phe-OEt 

Relevant academic research and scientific papers

Continuous-flow processes for the: S -alkynylation of cysteine-containing peptides and thioglycosides under catalyst-free, oxidant-free and mild conditions

Here we developed a novel method involving the use of continuous flow for the selective alkynylation of cysteine-containing peptides and 1-thioglycoside residues. This method was characterised by mild conditions (room temperature, metal-free, oxidant-free

Visible-Light-Mediated S?H Bond Insertion Reactions of Diazoalkanes with Cysteine Residues in Batch and Flow

We describe the application of S?H bond insertion reactions of aryl diazoacetates with cysteine residues that enabled metal-free, S?H functionalization under visible-light conditions. Moreover, this process could be intensified by a continuous-flow photomicroreactor on the acceleration of the reaction (6.5 min residence time). The batch and flow protocols described were applied to obtain a wide range of functionalized cysteine derivatives and cysteine-containing dipeptides, thus providing a straightforward and general platform for their functionalizations in mild conditions. (Figure presented.).

Facile Cu(ii)-mediated conjugation of thioesters and thioacids to peptides and proteins under mild conditions

The bioconjugation of peptide derivatives such as polypeptides, peptide-based probes and proteins is a vibrant area in many scientific fields. However, reports on metal-mediated chemical methods towards native peptides especially non-engineering protein modification under mild conditions are still limited. Herein, we describe a novel Cu(ii)-mediated strategy for the conjugation of thioesters/thioacids to peptides under mild conditions with high functional group tolerance. Based on this strategy, polypeptides, even peptide-based fluorescent probes, can be efficiently constructed. Finally, the selective modification of lysine residues of native Ub with thioesters could be realized and complete conjugation of Ub could be achieved even under equivalent Cu(ii). These promising results could greatly expand Cu(ii)-mediated reaction strategies on chemical biology and molecular imaging.

HMDO-promoted peptide and protein synthesis in ionic liquids

Hexamethyldisiloxane (HMDO) has been developed to efficiently promote the metal-free direct coupling of an amino function of one cysteine-free peptide or protein and a C-terminal thioester of the second peptide in ionic liquids. The amide-coupling reaction proceeds smoothly under mild conditions to afford the corresponding products in good to excellent yields (63-94%). Peptide couplings were also achieved using in-situ-generated thioesters by the thioesterification of oxo esters.

Metal-free direct amidation of peptidyl thiol esters with α-amino acid esters

Metal-free direct amidation of peptidyl thiol esters with α-amino acid esters in the presence of bis(trimethylsilyl) acetamide (BSA) has been developed. This general method provides convenient access to N-protected peptides in good yields under mild condi

Hexafluoro-2-propanol as a potent cosolvent for chemical ligation of membrane proteins

The study on membrane proteins is an important challenge mainly because of their very poor solubility in various solvents. The traditional recombinant expression strategy and the native chemical ligation method both have difficulty in generating sufficient amounts of desired proteins with high efficiency. Previous studies have shown that multiply fluorinated alcohols exhibit good ability to dissolve difficult peptide sequences, especially hexafluoro-2- propanol (HFIP). In the present study we systematically studied the capability of solvents containing different percentage of HFIP in dissolving transmembrane peptides. Through both HPLC and UV analyses we concluded that 60% HFIP/8 M urea constituted a good solvent system. In this solvent system we also optimized conditions to perform native chemical ligation (NCL). Under the optimized conditions we successfully achieved NCL's for both dipeptide formation and the synthesis of a model protein (Trifolitoxin). These results suggested that HFIP was a potential cosolvent that could be used in the ligation of poorly soluble peptides for the generation of membrane proteins.

Synthesis of high enantiopurity N-protected α-amino ketones by thiol ester-organostannane cross-coupling using pH-neutral conditions

(Chemical Equation Presented) An efficient synthesis of high enantiopurity N-protected α-amino ketones is described. Complementing other studies using boronic acids and thiol esters, this Cu(I) diphenylphosphinate (CuDPP)-mediated, palladium-catalyzed cou