Novel biomimetic affinity ligands for human tissue plasminogen activator |
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Authors: | Wu Fang Yu Jing Li Rongxiu |
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Affiliation: | Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. fangwu@bioc.unizh.ch |
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Abstract: | Dyes-based biomimetic affinity chromatography has been used to purify therapeutically useful proteins. In order to design novel biomimetic affinity ligands for purification of tissue-type plasminogen activator (t-PA), small molecular fragments were achieved to fit in S3/4 binding site of t-PA by structure-based ligand design method (InsightII/Ludi). Three biomimetic affinity ligands A, B, and C were then designed, synthesized, and proved to bind the target protein (t-PA), exceeding the binding capacity of the commercial p-amino benzamidine affinity matrix. The designed affinity matrix A showed high efficiency to purify sc-tpa from the crude samples with 18-fold of purification. |
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Keywords: | t-PA, tissue-type plasminogen activator BBA, 2,7-bis-(4-amidino benzylidene) cycloheptanone AZT, 1-aminobenzamidine-3,5-chloro-2,4,6-sys-triazine sc-tpa, single chain t-PA |
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