title: [Peptide synthesis catalyzed by subtilisin-72 in organic solvents].
abstract: The solubility, stability, and activity of native subtilisin 72 and of its complex with SDS were comparatively studied in a number of polar organic solvents. Subtilisin was found to catalyze peptide bond formation when suspended in acetonitrile or solubilized as a complex with SDS in ethanol and isopropanol. Tripeptide Z-Ala-Ala-Leu-pNA, tetrapeptides A-Ala-Ala-P1-P1'-B, where A = Z or Abz; P1 = Leu, Phe, Met, Trp, Ile, Tyr, Phe(NO2), or Glu(OMe), P1' = Leu, Phe, Glu, Ala, Ile, Val, or Arg; B = NH2, pNA, or 2-(2,4-dinitrophenyl)aminoethylamine residue (Ded); pentapeptides Z-Ala-Ala-Leu-Ala-Ala-pNA and Z-Ala-Ala-Leu-Ala-Phe-pNA; and hexapeptide Abz-Val-Ala-Phe-Phe-Ala-Ala-Ded were synthesized using the SDS-subtilisin complex. The complex also efficiently catalyzed the oligomerization of tripeptide H-Phe-Ala-Leu-OCH3 in ethanol, which resulted in a 63:37 mixture of trioligomer and tetraoligomer. It was demonstrated that SDS-subtilisin is a much more efficient catalyst than the suspension of native enzyme.
authors.affiliation: Faculty of Chemistry, Moscow State University, Russia.
authors.forename: I V
authors.initials: IV
authors.lastname: Getun
authors.forename: I Iu
authors.initials: IIu
authors.lastname: Filippova
authors.forename: E N
authors.initials: EN
authors.lastname: Lysogorskaia
authors.forename: A V
authors.initials: AV
authors.lastname: Bacheva
authors.forename: E S
authors.initials: ES
authors.lastname: Oksenoĭt
mesh_terms: D002384:Catalysis; D004795:Enzyme Stability; D010455:Peptides / Q000138:chemical synthesis*; D012997:Solvents; D013381:Subtilisins / Q000378:metabolism*
chemical_list: D010455:Peptides; D012997:Solvents; D013381:Subtilisins
vernacular_title: Peptidnyĭ sintez, kataliziruemyĭ subtilizinom-72 v organicheskikh rastvoriteliakh.