کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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870288 | 1470993 | 2007 | 6 صفحه PDF | دانلود رایگان |

A novel fluorescent sensing system for α-glycated amino acids was created based on fructosyl amino acid binding protein (FABP) from Agrobacterium tumefaciens. The protein was found to bind specifically to the α-glycated amino acids fructosyl glutamine (Fru-Gln) and fructosyl valine (Fru-Val) while not binding to ɛ-fructosyl lysine. An Ile166Cys mutant of FABP was created by genetic engineering and modified with the environmentally sensitive fluorophore acrylodan. The acrylodan-conjugated mutant FABP showed eight-fold greater sensitivity to Fru-Val than the unconjugated protein and could detect concentrations as low as 17 nM, making it over 100-fold more sensitive than enzyme-based detection systems. Its high sensitivity and specificity for α-substituted fructosyl amino acids makes the new sensing system ideally suited for the measurement of hemoglobin A1c (HbA1c), a major marker of diabetes.
Journal: Biosensors and Bioelectronics - Volume 22, Issues 9–10, 15 April 2007, Pages 1933–1938