| Info. | Vol.4 - No.1 (2010.03.20) |
|---|---|
| Title | Determination of glycated hemoglobin on the basis of spectral shifting from protein-dye interaction |
| Authors | Eun Joong Kim1, Seung Yeon Song1, Bun Yeoul Lee1 & Hyun C. Yoon1 |
| Institutions | 1Department of Molecular Science & Technology, Ajou University, Suwon 443-749, Korea Correspondence and requests for materials should be addressed to H.C. Yoon (hcyoon@ajou.ac.kr) |
| Abstract | A method for the detection of glycated proteins was developed on the basis of spectral shifting observed for 1-(4-Boronophenylazo)-2-hydroxy-3,6-naphthalene-disulfonic acid (azo-BA) dye. Hemoglobin A1c, a type of glycated hemoglobin, is an important indicator of diabetes mellitus control and management. We have employed the azo-BA dye containing a boronic acid group linked to an aromatic chromophore. The boronic acid group of the dye specifically binds to the carbohydrate chain of HbA1c via cis-diol interaction, and its spectra exhibit a unique chromatic redshift. Because the reaction is spontaneous at neutral pH, this method provides an advantage of short detection time. After the azo-BA dye/HbA1c reaction commenced, the concentration of conjugate was measured by registering spectral shifts. The measurements revealed that the method has a dynamic detection range of 3-15% (HbA1c/total hemoglobin), which covers the required clinical reference range. This method has shown reproducible results; the coefficient of variation of the test was 3.60%. Thus, the proposed method was found suitable for measuring %HbA1c and would be applicable for diabetes mellitus control. |
| Keyword | Glycated hemoglobin, Glycated protein, Hemoglobin A1c, Optical sensing, Spectral shifting |
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