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Bioaffinity Assays Using UV One-Dimensional Photonic Crystals (1DPC)

使用紫外一维光子晶体 (1DPC) 进行生物亲和力测定

基本信息

批准号：
9098709
负责人：
Joseph R. LAKOWICZ
金额：
$ 19.3万
依托单位：
UNIVERSITY OF MARYLAND BALTIMORE
依托单位国家：
美国
项目类别：
财政年份：
2015
资助国家：
美国
起止时间：
2015-07-01 至 2018-06-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/9098709
关键词：
Affect Albumins Antibodies Area Basic Science Binding Binding Proteins Biological Biological Assay Biological Models Biological Testing Biomedical Research Bovine Serum Albumin Bypass CD4 Antigens Capsid Proteins Chemicals Collaborations Complex Coupled Coupling DC-specific ICAM-3 grabbing nonintegrin Deposition Detection Devices Dimensions Dyes Film Fluorescence Future Generations Generic Drugs HIV HIV Antibodies HIV Envelope Protein gp120 Health Immunoglobulin G Kinetics Label Lighting Link MDM2 gene Measurement Measures Metals Methods Modeling Optics Performance Plasma Protein Array Protein p53 Proteins Proteomics Radiation Reaction Reader Refractive Indices Reporting Research Sampling Signal Transduction Silicon Dioxide Spatial Distribution Streptavidin Structure Surface Surface Plasmon Resonance System TP53 gene Tantalum Temperature Testing Tryptophan Tumor Suppressor Proteins Utah Work anti-IgG base biological systems cost design drug discovery fluorophore instrument instrumentation monolayer novel strategies photonics prevent protein protein interaction receptor research clinical testing screening sensor silicon nitride simulation transmission process vapor

项目摘要

DESCRIPTION (provided by applicant): Measurements of biomolecule interactions are increasingly important for proteomics and protein-protein interactions (the Interactome). With the exception of surface plasmon resonance (SPR) most of the alternative methods rely on the use of extrinsic fluorophores or probes which are covalently linked to one or more of the interacting species. These labeling steps become increasingly costly and complex as the number of biomolecules is increased. We propose a new approach to label-free measurements using one-dimensional photonic crystals (1DPCs) and intrinsic protein fluorescence. Since most proteins contain tryptophan these residues provide a type of mass sensor for proteins, analogous to SPR which also senses mass by changes in the refractive index. We will use Bloch surface waves (BSWs) on the 1DPCs. BSWs provide opportunities for highly localized excitation and observation of surface-bound proteins. The BSW substrates will be composed of multiple layers of UV-transmitting dielectrics. These structures will not contain metals so there is no quenching at short distances. Specific Aim 1. Design BSW structures for use at UV wavelengths. Not all 1DPCs display BSW. We will use the transfer matrix method to simulate the optical modes and select the dielectrics and dimensions. More complex numerical simulations will be used to predict the efficiency of trp coupling and directionality of the emission. Specific Aim 2. Fabricae and test 1DPCs for use with UV wavelengths. Suitable structures must display good UV transmission, a BSW and low autofluorescence. We will test combinations of three dielectrics, silica (SiO2), silicon nitride (Si3N4) and tantalum pentoxide (Ta2O5). Substrates will be tested wih model systems of albumin, streptavidin and antibodies. Specific Aim 3. Biological testing of the BSW structures. The structures will be tested with two important biological systems. The first is binding between the p53 tumor suppressor protein and its negative effectors. The second is binding of the HIV gp120 protein with its CD4 receptor and with potential HIV antibodies. Impact. This project will result in a new generic method to measure protein-protein interactions. The substrates will be simple and inexpensive. The method can be used with existing or modified plate readers. The simplicity of the optics will permit the extension to high-throughput measurements.