Madder A, Farcy N, Pérez-Payán MN, Öhberg LM, Davis AP
Laboratory for Organic Synthesis Department of Organic Chemistry, University of Gent Krijgslaan 281, 9000 Gent (Belgium).
Angew Chem Int Ed Engl. 2000 Jan;39(1):145-148. doi: 10.1002/(sici)1521-3773(20000103)39:1<145::aid-anie145>3.0.co;2-j.
Recursive deconvolution of a 729-membered peptide library has identified three active sequences, in which both Ser and His are present in one of the two tripeptidic chains generated on a steroidal scaffold (see structural formula), for the cleavage of an activated p-nitrophenyl ester. This combinatorial approach aims at searching for serine-protease-like activity.
对一个由729个成员组成的肽库进行递归去卷积,已鉴定出三个活性序列,其中丝氨酸(Ser)和组氨酸(His)都存在于甾体支架上产生的两条三肽链之一中(见结构式),用于切割活化的对硝基苯酯。这种组合方法旨在寻找类丝氨酸蛋白酶活性。