38678-59-0

Upstream product

• 687-51-4 H-L-Leu-NH₂ 
• 3081-24-1 H-Phe-OEt 
• 69193-13-1 Cbz-L-Phe-L-Leu-NH₂ 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 108395-58-0 acetyl L-phenylalanine chloroethyl ester 
• 2666-93-5 (S)-Leu-OMe 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 74257-73-1 tert-butyl ((S)-1-(((S)-1-amino-4-methyl-1-oxopentan-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 32909-56-1 Nα-pivaloyl-L-phenylalanine 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 65118-58-3 N-Ac-L-Phe-L-Leu-NH₂ 

Downstream Products

• 71591-21-4 Z-Tyr-Gly-Gly-Phe-Leu-NH₂ 
• 81638-88-2 amide of N-t-butyloxycarbonyl-O-benzyl-L-tyrosylglycylglycyl-L-phenylalanyl-L-leucine 
• 138850-05-2 Boc-Met-Leu-Phe-Phe-Leu-NH₂ 
• 132910-39-5 (S)-2-[(S)-2-(2-{2-[(S)-2-Acetylamino-3-(4-hydroxy-phenyl)-propionylamino]-acetylamino}-acetylamino)-3-phenyl-propionylamino]-4-methyl-pentanoic acid amide 
• 85574-42-1 Z-Tyr(Z)-(D)Ala-Gly-Phe-Leu-NH₂ 
• 3303-55-7 L-Phe-Leu 
• 69193-15-3 N-(benzyloxycarbonyl)-glycyl-L-phenylalanyl-L-leucine amide 
• 126028-19-1 N-cbz-L-Phe-L-Phe-L-Leu-NH₂ 
• 65189-64-2 H-Tyr-D-Ala-Gly-Phe-Leu-NH₂ 
• 95852-51-0 Aib-Phe-Leu-NH₂ 
• 95852-52-1 Acc⁵-Phe-Leu-NH₂ 
• 95852-70-3 Tyr-Gly-Aib-Phe-Leu-NH₂ 
• 95852-71-4 H-Tyr-Aib-Aib-Phe-Leu-NH₂ 
• 95878-03-8 Tyr-Gly-Acc⁵-Phe-Leu-NH₂ 

Relevant academic research and scientific papers

Mapping the s1 and s1’ subsites of cysteine proteases with new dipeptidyl nitrile inhibitors as trypanocidal agents

The cysteine protease cruzipain is considered to be a validated target for therapeutic intervention in the treatment of Chagas disease. A series of 26 new compounds were designed, synthesized, and tested against the recombinant cruzain (Cz) to map its S1/S1′ subsites. The same series was evaluated on a panel of four human cysteine proteases (CatB, CatK, CatL, CatS) and Leishmania mexicana CPB, which is a potential target for the treatment of cutaneous leishmaniasis. The synthesized compounds are dipeptidyl nitriles designed based on the most promising combinations of different moieties in P1 (ten), P2 (six), and P3 (four different building blocks). Eight compounds exhibited a Ki smaller than 20.0 nM for Cz, whereas three compounds met these criteria for LmCPB. Three inhibitors had an EC50 value of ca. 4.0 μM, thus being equipotent to benznidazole according to the antitrypanosomal effects. Our mapping approach and the respective structure-activity relationships provide insights into the specific ligand-target interactions for therapeutically relevant cysteine proteases.

NEW XANTHENE PROTECTIVE AGENT

To develop a protecting group that facilitates separation and purification, after reaction, of a compound including a protected functional group, without solidifying or insolubilizing the compound. A xanthene compound of by General Formula (1) (wherein Y is —OR17 (R17 is a hydrogen atom or an active ester-protecting group), —NHR18 (R18 is a hydrogen atom, or a linear or branched C1-C6 alkyl group or aralkyl group), an azide, a halogen atom, or a carbonyl group formed together with a methylene group; at least one of R1 to R8 is represented by Formula (2); [in-line-formulae]—O—R9—X-A??(2)[/in-line-formulae]and a residue is a hydrogen atom, a halogen atom, a C1-C4 alkyl group, or a C1-C4 alkoxy group,wherein R9 is a linear or branched C1-C16 alkylene group;X is O or CONR19 (R19 is a hydrogen atom or a C1-C4 alkyl group); andA is represented by Formula (3) or the like (wherein R10, R11, and R12, the same or different, are a linear or branched C1-C6 alkyl group or an aryl group optionally including a substituent; R13 is a single bond or a linear or branched C1-C3 alkylene group; and R14, R15, and R16 are a linear or branched C1-C3 alkylene group)).

Enzymatic peptide synthesis in frozen aqueous systems: Use of N(α)-unprotected unusual acyl donors

α-Chymotrypsin (EC 3.4.21.1) was used for catalyzing the reaction of various N(α)-unprotected non-coded phenylalanine ester derivatives with H-Leu-NH2 and H-Arg-NH2 in frozen aqueous solution at -15°C. Compared with reactions at room temperature, a significant yield increasing effect could be established. The kinetic parameters of ester hydrolysis show that most of the unusual acyl donors (compared with the coded phenylalanine methyl ester) are well accepted substrates for α-chymotrypsin.

Facile Enzymatic Synthesis of N-Acyl-enkephalin Amides

A novel three step protease catalysed synthesis of enkephalin precursors from simple readily available substrates is described.

Papain Catalysed Peptide Synthesis: Control of Amidase Activity and the Introduction of Unusual Amino Acids

Procedures for the papain catalysed synthesis of peptides containing D-amino acids and derivatives with control of the enzyme's amidase activity have been developed.

Synthesis and Conformations of Stereochemically Restricted Analogs of Leu5-Enkephalinamide: Substitution of α-Aminoisobutyric Acid and 1-Aminocyclopentane-1-carboxylic Acid at Positions 2 and 3

Six analogs of Leu-enkephalinamide containing α-aminoisobutyric acid (Aib) or 1-amino-cyclopentane-1-carboxylic acid (Acc5) at positions 2 and 3 have been synthesized.The peptides Tyr-Aib-Gly-Phe-Leu-NH2 (1), Tyr-Gly-Aib-Phe-Leu-NH2 (2), Tyr-Ai