52845-15-5

Upstream product

• 1948-31-8 di-L-alanine 
• 70-34-8 2,4-Dinitrofluorobenzene 

Downstream Products

• 56-41-7 L-alanin 
• 4615-69-4 2-methyl-5-nitro-1H-benzimidazole-3-oxide 
• 166535-26-8 Dnp-Ala-Ala-Phe-Arg-NH₂ 
• 166535-24-6 Dnp-Ala-Ala-Leu-Arg-NH₂ 
• 166535-25-7 Dnp-Ala-Ala-Val-Arg-NH₂ 
• 166535-27-9 Dnp-Ala-Ala-Ile-Arg-NH₂ 
• 223271-87-2 (S)-2-{(S)-2-[(S)-2-(2,4-Dinitro-phenylamino)-propionylamino]-propionylamino}-3-phenyl-propionic acid 
• 223271-86-1 (S)-2-{(S)-2-[(S)-2-(2,4-Dinitro-phenylamino)-propionylamino]-propionylamino}-3-phenyl-propionic acid methyl ester 
• 185699-13-2 Dnp-Ala-Ala-Ile-OCH₃ 
• 166535-23-5 Dnp-Ala-Ala-Val-OCH₃ 

Relevant academic research and scientific papers

Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties

A metallocarboxypeptidase produced by Streptomyces bikiniensis 27 strain (VKPM Ac-1783) (CPSb) was purified and characterized. The enzyme cleaves both basic and hydrophobic C-terminal amino acid residues from synthetic peptides, that is, it possesses specificity of mammalian carboxypeptidases A and B. The enzyme also hydrolyzes peptides bearing glutamic acid at the C-end. CPSb exhibits its maximal activity at pH 7.0-7.6 and 55°C. The nucleotide sequence encoding the mature CPSb in S. bikiniensis 27 (VKPM Ac-1783) genome (Accession No. GU362077) was determined. It is shown that the primary structure of the mature enzyme has a moderate degree of identity with orthologs from Streptomyces griseus (79% identity) and Streptomyces avermitilis (85% identity).

Method for photolysis of amido bonds

The invention discloses a method for photo-splitting amido bonds, wherein the method is mild in reaction condition and can realize splitting of amido bonds by using illumination. The method for photo-splitting the amido bonds comprises the following steps: reacting 2,4-dinitrofluorobenzene with an amino group of a substance which contains alpha amino acid at the tail end and is shown as a structural formula I to generate a compound 1 represented by a structural formula II; and under light irradiation, carrying out amido bond cleavage reaction on the compound 1, wherein R1 is a side chain group of alpha-amino acid, and R2 is aryl, aliphatic hydrocarbon, -CH(R)-COOH or polypeptide.

Synthesis of new chromogenic substrates for aspartyl proteases

A general method was developed for the synthesis of new chromogenic substrates of aspartyl proteases: Dnp-Ala-Xaa-Phe-Phe-Ala-Arg-NH2, where Xaa was Ala or Ser. The synthetic scheme involved both chemical and enzymic stages, the condensation of tripeptides in an organic medium by means of pepsin immobilized on Celite being among the latters. The influence of organic solvents, reaction time, and the composition and ionic strength of the buffers used in the reaction mixture and at the pepsin immobilization step on the efficacy of the pepsin-catalyzed synthesis was studied.