caa a22 4500 445326506 CHVBK 20180317142722.0 cr unu---uuuuu 170323e20111201xx s 000 0 eng 10.1007/s10989-011-9267-7 doi (NATIONALLICENCE)springer-10.1007/s10989-011-9267-7 Partially Folded Glycated State of Human Serum Albumin Tends to Aggregate [Elektronische Daten] [Taqi Khan, M. Saleemuddin, Aabgeena Naeem] The interaction of reducing carbohydrates with proteins leads to a cascade of reactions that are known as glycation or Maillard reactions that results in the formation of advanced glycation end products. We studied the impact of incubation with various sugars for 4weeks on the behaviour of human serum albumin incubation using CD, fluorescence, UV-Vis spectrophotometry and polyacrylamide gel electrophoresis. Three weeks of incubation of human serum albumin with sugars resulted in the formation of an intermediate state with negative CD peaks at 222 and 208nm characteristic of α-helix. The form also retained tertiary contacts but with altered tryptophan environment and high ANS binding indicative of molten globule state. Further incubation of human serum albumin for 4weeks resulted in the formation of an intermediate form with negative CD peak at 217nm, characteristic of β-sheet, decreased ANS fluorescence and increased thioflavin T fluorescence characteristic of an aggregated state. Prolonged exposure of human serum albumin to reducing sugars thus exerts greater deleterious effects on its structure and formation of aggregates. Springer Science+Business Media, LLC, 2011 AGEs nationallicence Aggregation nationallicence Circular dichorism nationallicence Fluorescence nationallicence HSA nationallicence Molten globule nationallicence K : Lysine nationallicence AGE : Advanced glycation end products nationallicence HSA : Human serum albumin nationallicence R : Arginine nationallicence CD : Circular dichorism nationallicence PAGE : Polyacrylamide gel electrophoresis nationallicence Th T : Thioflavin T nationallicence RAGE : Receptor for AGEs nationallicence TNBS : Trinitrobenzene sulphonate nationallicence Khan Taqi Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 202 002, Aligarh, India aut Saleemuddin M. Interdisciplinary Biotechnology Unit, Aligarh Muslim University, 202 002, Aligarh, India aut Naeem Aabgeena Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 202 002, Aligarh, India aut International Journal of Peptide Research and Therapeutics Springer Netherlands 17/4(2011-12-01), 271-279 1573-3149 17:4<271 2011 17 10989 https://doi.org/10.1007/s10989-011-9267-7 text/html Onlinezugriff via DOI 1 brief-communication jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10989-011-9267-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Khan Taqi Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 202 002, Aligarh, India aut NATIONALLICENCE 700 1- Saleemuddin M. Interdisciplinary Biotechnology Unit, Aligarh Muslim University, 202 002, Aligarh, India aut NATIONALLICENCE 700 1- Naeem Aabgeena Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 202 002, Aligarh, India aut NATIONALLICENCE 773 0- International Journal of Peptide Research and Therapeutics Springer Netherlands 17/4(2011-12-01), 271-279 1573-3149 17:4<271 2011 17 10989 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer