50300-49-7

Upstream product

• 64504-35-4 N-carbobenzyloxy-L-alanyl-L-alanyl-L-phenylalanine methylester 
• 16012-70-7 benzyloxycarbonyl-L-alanyl-L-alanine 
• 17585-69-2 L-phenylalanine hydrochloride 

Downstream Products

• 159141-68-1 Cbz-alanyl-alanyl-phenylalanyl bromomethane 
• 90427-63-7 Z-Ala₂-Phe-AlaCH₃ 

Relevant academic research and scientific papers

Resin-to-resin acyl- and aminoacyl-transfer reactions using oxime supports

We describe a convergent approach to solid-phase synthesis in which two fragments of a molecule are synthesized on independent supports and then condensed in a key resin-to-resin transfer reaction. This approach has been utilized for the synthesis of amides and ureas by transferring acyl groups and aminoacyl groups from p-nitrophenyl(polystyrene)ketoxime resin to amino acid-functionalized Wang resins. Oxime resinderived esters of peptides undergo transacylation to a solution-phase nucleophilic activator which then transfers the peptide to another resin bearing a nucleophilic amine terminus, resulting in amide bond formation. Likewise, oxime resin-derived carbamates, prepared from phosgenated p-nitrophenyl(polystyrene)ketoxime resin, undergo thermolytic isocyanate liberation in solution, which reacts with a second resin bearing a nucleophilic amino terminus resulting in urea bond formation.

Stereocontrolled synthesis of erythro N-protected α-amino epoxides and peptidyl epoxides

N-protected α-amino epoxides of erythro configuration, derived from α-amino acids, were synthesized in a stereoselective manner. The erythro (2S,3S), configuration was achieved by the synthetic sequence: amino acid -> haloketone -> halohydrin -> epoxide. A mechanistic explanation for the observed stereoselectivity is presented. This stereoselective synthetic approach was applied to the synthesis of a variety of short peptidyl epoxides, bearing a predefined absolute configuration of the chiral epoxide moiety.

Thermitase - A Thermostable Serine Protease. II. Synthesis of Substrate Analogous Peptide Chloromethyl Ketones as Irreversibly Acting Inhibitors

The preparation of dipeptide to pentapeptide chloromethyl ketones of alanine with variation of the amino acid in the P1 and P2 position of the peptides is described.The synthesis is performed by fragment condensation of N-acylated amino acids or peptides with the unprotected chloromethyl ketone derivatives of amino acids and peptides, respectively.Some examples of enzyme inactivation by peptide chloromethyl ketones are discussed.