Quartz crystal biosensor for real-time monitoring of molecular recognition between protein and small molecular medicinal agents
A quartz crystal microbalance (QCM) biosensor integrated into a flow injection analysis (FIA) system was used for the real-time investigation of molecular recognition between a protein and small molecular medicinal agents. Two sulfa-drugs, sulfamethazine (SMZ) and sulfamethoxazole (SMO), were, respe...
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Published in | Biosensors & bioelectronics Vol. 19; no. 1; pp. 9 - 19 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Lausanne
Elsevier B.V
30.10.2003
Elsevier Science |
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Abstract | A quartz crystal microbalance (QCM) biosensor integrated into a flow injection analysis (FIA) system was used for the real-time investigation of molecular recognition between a protein and small molecular medicinal agents. Two sulfa-drugs, sulfamethazine (SMZ) and sulfamethoxazole (SMO), were, respectively, immobilized on the gold electrodes of the piezoelectric crystals using appropriate procedures based on self-assembly of the dithiothreitol (DTT). The binding interactions of the two immobilized drug ligands, with various proteins in solution, were followed as changes in the resonant frequency of the modified crystals. Results obtained from this rapid screen analysis clearly indicated that the two drug ligands appeared quite different in this molecular recognition procedure although their structures were similar. SMZ-immobilized sensor showed specific interaction only with IgG, while SMO-immobilized sensor showed negligible specific binding with IgG, but binding with trypsin and chymotrypsin. Further studies on the specific interaction between immobilized SMZ and three different species of IgG—human IgG, goat IgG and mouse IgG were carried out and the marked species-dependent difference was observed. The resultant sensorgrams were rapidly analyzed by using an in-house kinetic analysis software based on genetic algorithm (GA) to derive both the kinetic rate constants (k
ass and k
diss) and equilibrium association constants (K
A) for IgG–SMZ interactions. For the interactions, K
A were 5.48×l0
5, 2.75×l0
5 and 1.86×l0
5 M
−1 for human IgG, goat IgG and mouse IgG, respectively. The kinetic data provided further insight into the structural/functional relationships of different IgG on a molecular level. |
---|---|
AbstractList | A quartz crystal microbalance (QCM) biosensor integrated into a flow injection analysis (FIA) system was used for the real-time investigation of molecular recognition between a protein and small molecular medicinal agents. Two sulfa-drugs, sulfamethazine (SMZ) and sulfamethoxazole (SMO), were, respectively, immobilized on the gold electrodes of the piezoelectric crystals using appropriate procedures based on self-assembly of the dithiothreitol (DTT). The binding interactions of the two immobilized drug ligands, with various proteins in solution, were followed as changes in the resonant frequency of the modified crystals. Results obtained from this rapid screen analysis clearly indicated that the two drug ligands appeared quite different in this molecular recognition procedure although their structures were similar. SMZ-immobilized sensor showed specific interaction only with IgG, while SMO-immobilized sensor showed negligible specific binding with IgG, but binding with trypsin and chymotrypsin. Further studies on the specific interaction between immobilized SMZ and three different species of IgG--human IgG, goat IgG and mouse IgG were carried out and the marked species-dependent difference was observed. The resultant sensorgrams were rapidly analyzed by using an in-house kinetic analysis software based on genetic algorithm (GA) to derive both the kinetic rate constants (k sub(ass) and k sub(diss)) and equilibrium association constants (K sub(A)) for IgG-SMZ interactions. For the interactions, K sub(A) were 5.48xl0, 2.75xl0 and 1.86xl0 super(5) M super(-1) for human IgG, goat IgG and mouse IgG, respectively. The kinetic data provided further insight into the structural/functional relationships of different IgG on a molecular level. A quartz crystal microbalance (QCM) biosensor integrated into a flow injection analysis (FIA) system was used for the real-time investigation of molecular recognition between a protein and small molecular medicinal agents. Two sulfa-drugs, sulfamethazine (SMZ) and sulfamethoxazole (SMO), were, respectively, immobilized on the gold electrodes of the piezoelectric crystals using appropriate procedures based on self-assembly of the dithiothreitol (DTT). The binding interactions of the two immobilized drug ligands, with various proteins in solution, were followed as changes in the resonant frequency of the modified crystals. Results obtained from this rapid screen analysis clearly indicated that the two drug ligands appeared quite different in this molecular recognition procedure although their structures were similar. SMZ-immobilized sensor showed specific interaction only with IgG, while SMO-immobilized sensor showed negligible specific binding with IgG, but binding with trypsin and chymotrypsin. Further studies on the specific interaction between immobilized SMZ and three different species of IgG--human IgG, goat IgG and mouse IgG were carried out and the marked species-dependent difference was observed. The resultant sensorgrams were rapidly analyzed by using an in-house kinetic analysis software based on genetic algorithm (GA) to derive both the kinetic rate constants (kass and kdiss) and equilibrium association constants (KA) for IgG-SMZ interactions. For the interactions, KA were 5.48 x 10(5), 2.75 x 10(5) and 1.86 x 10(5) M(-1) for human IgG, goat IgG and mouse IgG, respectively. The kinetic data provided further insight into the structural/functional relationships of different IgG on a molecular level. A quartz crystal microbalance (QCM) biosensor integrated into a flow injection analysis (FIA) system was used for the real-time investigation of molecular recognition between a protein and small molecular medicinal agents. Two sulfa-drugs, sulfamethazine (SMZ) and sulfamethoxazole (SMO), were, respectively, immobilized on the gold electrodes of the piezoelectric crystals using appropriate procedures based on self-assembly of the dithiothreitol (DTT). The binding interactions of the two immobilized drug ligands, with various proteins in solution, were followed as changes in the resonant frequency of the modified crystals. Results obtained from this rapid screen analysis clearly indicated that the two drug ligands appeared quite different in this molecular recognition procedure although their structures were similar. SMZ-immobilized sensor showed specific interaction only with IgG, while SMO-immobilized sensor showed negligible specific binding with IgG, but binding with trypsin and chymotrypsin. Further studies on the specific interaction between immobilized SMZ and three different species of IgG—human IgG, goat IgG and mouse IgG were carried out and the marked species-dependent difference was observed. The resultant sensorgrams were rapidly analyzed by using an in-house kinetic analysis software based on genetic algorithm (GA) to derive both the kinetic rate constants (k ass and k diss) and equilibrium association constants (K A) for IgG–SMZ interactions. For the interactions, K A were 5.48×l0 5, 2.75×l0 5 and 1.86×l0 5 M −1 for human IgG, goat IgG and mouse IgG, respectively. The kinetic data provided further insight into the structural/functional relationships of different IgG on a molecular level. |
Author | Liu, Guoquan Bo, Zuyi Shangguan, Di-Hua Liu, Yang Yu, Xiao Zhao, Rui |
Author_xml | – sequence: 1 givenname: Yang surname: Liu fullname: Liu, Yang – sequence: 2 givenname: Xiao surname: Yu fullname: Yu, Xiao – sequence: 3 givenname: Rui surname: Zhao fullname: Zhao, Rui – sequence: 4 givenname: Di-Hua surname: Shangguan fullname: Shangguan, Di-Hua – sequence: 5 givenname: Zuyi surname: Bo fullname: Bo, Zuyi – sequence: 6 givenname: Guoquan surname: Liu fullname: Liu, Guoquan email: liugq@infoc3.icas.ac.cn |
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Keywords | Sulfamethoxazole Sulfamethazine Genetic algorithm Immunoglobulin G Molecular recognition Kinetic analysis Quartz crystal biosensor Drug Ligand Quartz crystal biosensor: Kinetic analysis Piezoelectric crystals Real time Protein Biosensor Kinetics Monitoring Quartz microbalance |
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SubjectTerms | Adsorption Algorithms Animals Biological and medical sciences Biosensing Techniques - instrumentation Biosensing Techniques - methods Biosensors Biotechnology Coated Materials, Biocompatible - chemical synthesis Crystallization - methods dithiothreitol Equipment Design Equipment Failure Analysis Flow Injection Analysis - instrumentation Flow Injection Analysis - methods Fundamental and applied biological sciences. Psychology Genetic algorithm Goats Humans Immunoglobulin G Kinetic analysis Methods. Procedures. Technologies Mice Molecular recognition Online Systems Pharmaceutical Preparations - analysis Pharmaceutical Preparations - chemistry Protein Interaction Mapping - instrumentation Protein Interaction Mapping - methods Proteins - analysis Proteins - chemistry Quartz quartz crystal Quartz crystal biosensor Reproducibility of Results Sensitivity and Specificity Sulfamethazine Sulfamethazine - analysis Sulfamethazine - chemistry Sulfamethoxazole Sulfamethoxazole - analysis Sulfamethoxazole - chemistry Transducers Various methods and equipments |
Title | Quartz crystal biosensor for real-time monitoring of molecular recognition between protein and small molecular medicinal agents |
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