Filippova I Iu, Lysogorskaia E N
Faculty of Chemistry, Moscow State University, Vorob'evy gory, Moscow, 119992 Russia.
Bioorg Khim. 2003 Sep-Oct;29(5):544-50. doi: 10.1023/a:1026061828077.
We showed that modified proteases could catalyze synthesis of a wide variety of peptides of various lengths and structures both in solution and on solid phase in organic solvents. The following modified proteases were studied as catalysts for enzymatic peptide synthesis in polar organic solvents (acetonitrile, dimethylformamide, and ethanol): pepsin sorbed on celite, a noncovalent complex of subtilisin with sodium dodecylsulfate, and subtilisin or thermolysin covalently immobilized on a cryogel of polyvinyl alcohol. The use of the noncovalent complex of subtilisin with sodium dodecylsulfate and immobilized subtilisin is especially promising for the segment condensation of peptide fragments containing residues of trifunctional amino acids with unprotected ionogenic groups in side chains, such as Lys, Arg, His, Glu, and Asp.
我们发现，修饰后的蛋白酶能够在溶液以及有机溶剂中的固相中催化合成各种长度和结构的多种肽。我们研究了以下几种修饰后的蛋白酶作为极性有机溶剂（乙腈、二甲基甲酰胺和乙醇）中酶促肽合成的催化剂：吸附在硅藻土上的胃蛋白酶、枯草杆菌蛋白酶与十二烷基硫酸钠的非共价复合物，以及共价固定在聚乙烯醇冷冻凝胶上的枯草杆菌蛋白酶或嗜热菌蛋白酶。枯草杆菌蛋白酶与十二烷基硫酸钠的非共价复合物以及固定化枯草杆菌蛋白酶对于含三官能氨基酸残基且侧链上有未保护离子基团（如赖氨酸、精氨酸、组氨酸、谷氨酸和天冬氨酸）的肽片段的片段缩合尤其有前景。
