Lambda Theta Reflectometry: A New Technique for Measuring Optical Film Thickness in Planar Protein Arrays.
Gespeichert in:
| Titel: | Lambda Theta Reflectometry: A New Technique for Measuring Optical Film Thickness in Planar Protein Arrays. |
|---|---|
| Autoren: | Klose AM; Department of Dermatology, University of Rochester, Rochester, New York 14627, United States.; Materials Science Program, University of Rochester, Rochester, New York 14627, United States., Katz JD; Laboratory for Laser Energetics, University of Rochester, Rochester, New York 14627, United States., Boni R; Laboratory for Laser Energetics, University of Rochester, Rochester, New York 14627, United States., Nelson D; Laboratory for Laser Energetics, University of Rochester, Rochester, New York 14627, United States., Hassard B; Institute of Optics, University of Rochester, Rochester, New York 14627, United States., Miller BL; Department of Dermatology, University of Rochester, Rochester, New York 14627, United States.; Materials Science Program, University of Rochester, Rochester, New York 14627, United States.; Department of Biomedical Engineering, University of Rochester, Rochester, New York 14627, United States.; Institute of Optics, University of Rochester, Rochester, New York 14627, United States. |
| Quelle: | ACS sensors [ACS Sens] 2025 Jul 25; Vol. 10 (7), pp. 5097-5107. Date of Electronic Publication: 2025 Jul 02. |
| Publikationsart: | Journal Article |
| Sprache: | English |
| Info zur Zeitschrift: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101669031 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2379-3694 (Electronic) Linking ISSN: 23793694 NLM ISO Abbreviation: ACS Sens Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Washington, DC : American Chemical Society, [2016]- |
| MeSH-Schlagworte: | Protein Array Analysis*/methods , Protein Array Analysis*/instrumentation , Biosensing Techniques*/methods, Silicon Dioxide/chemistry |
| Abstract: | Quantitative protein measurements provide valuable information about biological pathways, immune system functionality, and the mechanisms of disease. The most accurate methods for detecting proteins are label-free and preserve native protein-binding interactions. Label-free biomolecular interaction analysis includes reflectometry, a group of techniques that detect proteins by measuring the reflectance properties of a thin film on a substrate. Most of these techniques are limited in some way by instrument complexity, sensitivity, or consumable manufacturing requirements. To address these issues, we introduce Lambda Theta Reflectometry (LTR), a new reflectometric technique that measures changes in film thickness by determining the point of null reflectivity as a function of wavelength (lambda) and angle of incidence (theta). The substrate is simultaneously illuminated with a range of angles and wavelengths, and reflected light is resolved both angularly and spectrally. Our prototype LTR reflectometer can measure SiO |
| Kommentare: | Update of: bioRxiv. 2025 Mar 29:2025.03.26.645463. doi: 10.1101/2025.03.26.645463.. (PMID: 40196501) |
| References: | AAPS J. 2007 Jun 29;9(2):E260-7. (PMID: 17907767) Cold Spring Harb Perspect Biol. 2014 Sep 04;6(10):a016295. (PMID: 25190079) Anal Chem. 2006 Aug 1;78(15):5578-83. (PMID: 16878898) Dermatol Ther (Heidelb). 2023 Oct;13(10):2417-2429. (PMID: 37615834) Biointerphases. 2017 Mar 16;12(2):02D301. (PMID: 28301944) Front Mol Neurosci. 2018 May 16;11:164. (PMID: 29867354) Biophys Rev. 2021 Oct 13;13(6):1179-1190. (PMID: 35059036) Protein Expr Purif. 2008 Aug;60(2):147-50. (PMID: 18538581) Anal Chem. 2011 May 15;83(10):3750-7. (PMID: 21517019) Biosensors (Basel). 2021 Dec 13;11(12):. (PMID: 34940269) Biosensors (Basel). 2023 Sep 05;13(9):. (PMID: 37754104) Anal Chem. 2015 Oct 6;87(19):9795-801. (PMID: 26376354) Hum Vaccin Immunother. 2013 Sep;9(9):1857-64. (PMID: 23778314) Anal Chem. 2021 Oct 12;93(40):13580-13588. (PMID: 34596381) Clin Orthop Relat Res. 2015 Sep;473(9):2735-49. (PMID: 26013151) Appl Opt. 2007 Apr 1;46(10):1890-5. (PMID: 17356635) World J Surg Oncol. 2023 Dec 14;21(1):384. (PMID: 38098074) Proc Natl Acad Sci U S A. 2008 Jun 10;105(23):7988-92. (PMID: 18523019) Nat Rev Microbiol. 2005 Dec;3(12):948-58. (PMID: 16322743) Essays Biochem. 2016 Jun 30;60(1):91-100. (PMID: 27365039) |
| Grant Information: | P50 AR072000 United States AR NIAMS NIH HHS |
| Contributed Indexing: | Keywords: immunoassay; optical thickness measurement; reflectometry; spectroscopy; thin film |
| Substance Nomenclature: | 7631-86-9 (Silicon Dioxide) |
| Entry Date(s): | Date Created: 20250702 Date Completed: 20250725 Latest Revision: 20250801 |
| Update Code: | 20250801 |
| PubMed Central ID: | PMC12305664 |
| DOI: | 10.1021/acssensors.5c01108 |
| PMID: | 40600954 |
| Datenbank: | MEDLINE |
| Abstract: | Quantitative protein measurements provide valuable information about biological pathways, immune system functionality, and the mechanisms of disease. The most accurate methods for detecting proteins are label-free and preserve native protein-binding interactions. Label-free biomolecular interaction analysis includes reflectometry, a group of techniques that detect proteins by measuring the reflectance properties of a thin film on a substrate. Most of these techniques are limited in some way by instrument complexity, sensitivity, or consumable manufacturing requirements. To address these issues, we introduce Lambda Theta Reflectometry (LTR), a new reflectometric technique that measures changes in film thickness by determining the point of null reflectivity as a function of wavelength (lambda) and angle of incidence (theta). The substrate is simultaneously illuminated with a range of angles and wavelengths, and reflected light is resolved both angularly and spectrally. Our prototype LTR reflectometer can measure SiO <subscript>2</subscript> layer thickness with milli-Ångström precision. LTR measurements of Si/SiO <subscript>2</subscript> oxide films are in excellent agreement with spectroscopic ellipsometry for film thicknesses ranging from 1390 to 1465 Å. This technique enables label-free biosensing measurements across a range of biological analyte concentrations (0.5 ng/mL to μg/mL) without requiring stringent control over probe deposition thickness or substrate manufacturing. |
|---|---|
| ISSN: | 2379-3694 |
| DOI: | 10.1021/acssensors.5c01108 |
Nájsť tento článok vo Web of Science