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Atomic Absorption Spectroscopy: Interference

Atomic Absorption Spectroscopy: Interference

Interference leads to systematic error in atomic absorption (AA) measurements by enhancing or diminishing the analytical signal or the background. These interferences can be grouped into three main categories: spectral interference, chemical interference, and physical interference.
Spectral interference occurs when signals from other elements or molecules overlap with the analyte signal, falsely elevating or masking the analyte's absorbance. This interference can be corrected using Zeeman,...

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Updated: Apr 23, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Characterizing aptamer small molecule interactions with backscattering interferometry.

Michael N Kammer¹, Ian R Olmsted, Amanda K Kussrow

¹Department of Chemistry, Vanderbilt University, 2201 West End Avenue, Nashville, Tennessee, USA. darryl.bornhop@vanderbilt.edu.

|September 18, 2014

Summary

This summary is machine-generated.

Backscattering interferometry (BSI) offers a label-free method to characterize small molecule-aptamer interactions. This technique provides accurate binding affinity (Kd) values using minimal sample volumes and without requiring molecule labeling.

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Determining the Thermodynamic and Kinetic Association of a DNA Aptamer and Tetracycline Using Isothermal Titration Calorimetry

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Published on: August 23, 2022

Area of Science:

Biochemistry
Analytical Chemistry
Biotechnology

Background:

Aptamers, single-strand DNA or RNA, are versatile tools for sensors and therapeutics.
Aptamers offer high affinity and specificity for various targets, including small molecules (SM).
Current methods for characterizing SM-aptamer binding have limitations in sensitivity or require labeling.

Purpose of the Study:

To introduce and validate backscattering interferometry (BSI) as a label-free technique for quantifying SM-aptamer interactions.
To demonstrate BSI's capability in determining binding affinity (Kd) with high sensitivity and minimal sample volume.
To showcase BSI as an advantageous alternative to existing assay methodologies.

Main Methods:

Utilized backscattering interferometry (BSI), a free-solution sensing technique.
Measured aptamer affinity for previously characterized small molecules (bisphenol A, tenofovir, epirubicin).
Quantified Kd values for aptamers binding ampicillin, tetracycline, and norepinephrine.

Main Results:

BSI accurately determined Kd values for known SM-aptamer interactions, consistent with published data.
Achieved low nanomolar sensitivity with microliter sample quantities.
Demonstrated high signal-to-noise ratios (R(2) >0.95) without immobilization or labeling.

Conclusions:

Backscattering interferometry (BSI) is an effective, label-free method for characterizing small molecule-aptamer binding.
BSI offers a rapid and sensitive approach, overcoming limitations of mass-sensitive and label-dependent techniques.
This technique expedites assay development and is insensitive to mass differences between interacting molecules.