2131-01-3

Upstream product

• 2018-66-8 Z-Leu-OH 
• 4510-08-1 L-methioninamide 
• 51021-87-5 N-benzyloxycarbonyl-L-leucine methyl ester 
• 84890-95-9 C₁₅H₂₇NO₆S 
• 2488-15-5 N-tert-butoxycarbonyl-L-methionine 
• 68359-92-2 (S)-methionine amide trifluoroacetate 
• 34805-23-7 (S)-N-(tert-butoxycarbonyl)methionine amide 

Downstream Products

• 40297-96-9 H-Gly-Leu-Met-NH₂ hydrochloride 

Relevant academic research and scientific papers

Synthesis of N-Protected Eledoisin (6-11)-hexapeptide Using Proteases as Biocatalysts

Papain and α-chymotrypsin were used for the protease-catalyzed assembly of Boc-protected eledoisin (6-11)-hexapeptide by (2+4)- and (3+3)-segment condensation, respectively, in aqueous-organic solvent systems.As C-components, chemically synthesized Boc-pr

Active Site Mapping of Human CathepsinF with Dipeptide Nitrile Inhibitors

Cleavage of the invariant chain is the key event in the trafficking pathway of major histocompatibility complex classII. CathepsinS is the major processing enzyme of the invariant chain, but cathepsinF acts in macrophages as its functional synergist which is as potent as cathepsinS in invariant chain cleavage. Dedicated low-molecular-weight inhibitors for cathepsinF have not yet been developed. An active site mapping with 52 dipeptide nitriles, reacting as covalent-reversible inhibitors, was performed to draw structure-activity relationships for the non-primed binding region of human cathepsinF. In a stepwise process, new compounds with optimized fragment combinations were designed and synthesized. These dipeptide nitriles were evaluated on human cysteine cathepsinsF, B, L, K and S. Compounds 10 (N-(4-phenylbenzoyl)-leucylglycine nitrile) and 12 (N-(4-phenylbenzoyl)leucylmethionine nitrile) were found to be potent inhibitors of human cathepsinF, with Ki values 10nM. With all dipeptide nitriles from our study, a 3D activity landscape was generated to visualize structure-activity relationships for this series of cathepsinF inhibitors. Mapping with nitriles: For human cathepsinF, low-molecular-weight inhibitors have not been developed so far. Therefore, a library of 52 dipeptide nitriles, known to interact in a covalent but reversible manner with the active site cysteine, was evaluated for cathepsinF inhibition. With the kinetic data in hand, optimized candidates were designed, synthesized, and tested to improve the activity profile as cathepsinF inhibitors.