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Method for Measuring Glycated Hemoglobin

IP.com Disclosure Number: IPCOM000201641D
Original Publication Date: 2010-Nov-17
Included in the Prior Art Database: 2010-Nov-17
Document File: 4 page(s) / 356K

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Juergen Carstens: CONTACT

Abstract

The measurement of GHb (Glycated Hemoglobin), also referred to as HbA1c, in human blood provides an accurate estimation of the efficacy of type II diabetes management in patients. Currently the methods used to quantify GHb can be classified into two groups based on the assay principle. The first group includes methods which quantify GHb based on charge differences between glycated and nonglycated components; examples for those methods are the cation-exchange chromatography and the agar gel electrophoresis. The second group includes methods which separate components based on structural differences between glycated and nonglycated components; examples for those methods are boronate affinity chromatography, immunoassays and enzymatic methods. Absorbance measurement, e. g., the turbidimetric or colorimetric measurement, can be used to sense changes in the GHb concentrations in immunoassays and enzymatic methods. Recently, sensing methods using detection principles with increased sensitivity and reliability have been identified for the detection of GHb. They include FRET (Fluorescence Resonance Energy Transfer) based sensing mechanisms, endopeptidase based agglutination inhibition methods and SERS (Surface Enhanced Raman Scattering) techniques. Those technologies however are label-based, e. g., by fluorescence, and hence they are sensitive to external light conditions in lieu of fluorescence decay with light, and not cost-effective. The surface plasmon resonance for example requires highly sensitive Raman lasers and detectors.

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Method for Measuring Glycated Hemoglobin

Idea: Dr. Venkatasubramaniam Kalambur, IN-Bangalore

The measurement of GHb (Glycated Hemoglobin), also referred to as HbA1c, in provides an accurate estimation of the efficacy of type II diabetes management in p

Currently the methods used to quantify GHb can be classified into two group
principle. The first group includes methods which quantify GHb based on charge dif
glycated and nonglycated components; examples for those methods are the cation-ex chromatography and the agar gel electrophoresis. The second group includes meth
separatecomponents based on structural differences between glycatedand non
examples for those methods are boronate affinity chromatography, immunoassay
methods. Absorbance measurement, e. g., the turbidimetric or colorimetric m
to sense changes in the GHb concentrations in immunoassays and enzymatic me
sensing methods using detection principles with increased sensitivity and reliability have been identified for the detection of GHb. They include FRET (Fluorescence Resonance Ene
based sensing mechanisms, endopeptidase based agglutination inhibition method
(Surface Enhanced Raman Scattering) techniques. Those technologies however a
e. g., by fluorescence, and hence they are sensitive to external light conditions in li decay with light, and not cost-effective. The surface plasmon resonance for exa sensitive Raman lasers and detectors.

In the following a novel mechanism for sensing hemoglobin is proposed which uses MagnetoResistance) effect. Magnetoresistance effects cause a change in the
due to an applied
chip, as depicted Figure 1. For measuring GHb using this mechanism, a GMR chi Figure 2 has to be constructed. The proposed GMR chip can be constructed by m similar to those present in a hard-disk drives read heads. The surface of the chip ca with polyethylene glycol or other biocompatible polymers for conjugating biomolecule magnetoresistance can be transduced into voltage or current changes whi
digitized and detected.

Figure 3 and Figure 4 show the assay and sensing method, for GHb and Hb res
chip is coated with primary binding antibodies or proteins. The sample is processe treated, and the antigen, GHb or Hb, binds to the chip due to the specificity of the
Then excess sample is removed. A second antibody or protein bound to a magne
bind to a different segment of the antigen. The presence of the magnetic particle causes the resistance on the GMR chip. The measured resistance is transduced into corresponds to the concentration of G

Multiplexing can be done as shown in Figure 5. Furthermore, the method can be use
levels of key diagnostic proteins, cells and nucleotides, e. g., DNA (DeoxyriboNucle (RiboNucleic Acid). Proteins include molecules like Troponin I, myocardial diseas
Protein), cardiac and inflammatory disease, thyroid hormones (T3, T4, TSH), PSA
Antigen) and cance...