Development of Biosensor Technology for Protein Interactions

蛋白质相互作用生物传感器技术的发展

• 批准号: 8340622
• 负责人: PETER SCHUCK
• 金额: $ 6.38万
• 依托单位: NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/8340622
• 关键词: Accounting; Affinity; Binding; Binding Sites; Biosensor; Carbohydrates; Chemicals; Collaborations; Computer software; Data; Development; Goals; Heterogeneity; Kinetics; Laboratories; Lectin; Length; Membrane Glycoproteins; Membrane Proteins; Methods; Microscopic; Modeling; Polymers; Process; Property; Proteins; Role; Site; Surface; Technology; Testing; Update; chemical property; macromolecule; new technology; sensor

In the last year, we have applied our method of computationally accounting for surface site heterogeneity to a study of a model protein immobilized with different chemical strategies and on different sensor surfaces. We found that the most uniform surface site distributions were achieved with linker layers of moderate length. We identified experimental conditions that impose increased mass transport limitations. As an additional result of these studies, we have released an updated version of our distributable SPR data anlaysis software. This now also includes a discrete conformational change model, which allows testing of how well the hypothesis of slow conformational changes after an initial binding step fits experimental multi-phasic surface binding data, in comparison with the alternative explanation of surface site distributions with polydisperse affinity and kinetic constants. This was applied to data from the laboratory of Dr. Birgit Helm. Finally, we have continued the collaboration with the laboratory of Dr. Michael Tarlov at NIST on the recognition of different carbohydrate moieties on glycoproteins by surface-immobilized lectins.

去年，我们将计算表面位点异质性的方法应用于用不同化学策略固定在不同传感器表面上的模型蛋白的研究。我们发现，中等长度的连接层实现了最均匀的表面位点分布。我们确定了增加质量输运限制的实验条件。