Surface immobilization of a protease through an inhibitor-derived affinity ligand: a bioactive surface with defensive properties against an inhibitor
The concept of enzyme immobilization via an inhibitor-derived peptide was developed. This method of immobilization was shown to be advantageous over physical adsorption and covalent bonding in retaining the enzymatic activity. Moreover, the surface-immobilized enzyme exhibited resistance against its...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2015-09, Vol.51 (75), p.14263-14266 |
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creator | Tang, Zengchao Luan, Yafei Li, Dan Du, Hui Haddleton, David M Chen, Hong |
description | The concept of enzyme immobilization via an inhibitor-derived peptide was developed. This method of immobilization was shown to be advantageous over physical adsorption and covalent bonding in retaining the enzymatic activity. Moreover, the surface-immobilized enzyme exhibited resistance against its inhibitor due to the occupation of an inhibitor binding site on the enzyme. |
doi_str_mv | 10.1039/c5cc05652g |
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source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
subjects | Affinity Binding Sites Bonding Covalence Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Immobilization Inhibitors Ligands Models, Molecular Molecular Structure Occupation Plasminogen Inactivators - chemistry Structure-Activity Relationship Surface chemistry Surface Properties Tissue Plasminogen Activator - chemistry Tissue Plasminogen Activator - metabolism |
title | Surface immobilization of a protease through an inhibitor-derived affinity ligand: a bioactive surface with defensive properties against an inhibitor |
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