PMID- 29133088 OWN - NLM STAT- MEDLINE DCOM- 20180809 LR - 20180809 IS - 1879-0003 (Electronic) IS - 0141-8130 (Linking) VI - 109 DP - 2018 Apr 1 TI - Fructose-human serum albumin interaction undergoes numerous biophysical and biochemical changes before forming AGEs and aggregates. PG - 896-906 LID - S0141-8130(17)33517-1 [pii] LID - 10.1016/j.ijbiomac.2017.11.069 [doi] AB - Fructose is a reducing and highly lipogenic sugar that has unique metabolic effects in the liver. Non-enzymatic fructosylation of proteins generates advanced glycation end products (AGEs). Human serum albumin (HSA) may undergo fructosylation vis-a-vis AGEs formation. High fructose consumption may lead to structurally altered and functionally compromised fructosylated-HSA-AGEs, which can cause damage to hepatocytes resulting in hepatic macro- and microvesicular steatosis. In this study, HSA was incubated with varying concentrations of fructose for 10days and the induced changes were studied. Fructosylated-HSA exhibited hyperchromicity, increased AGE-specific fluorescence, quenching of tryptophan fluorescence and increased melting temperature. Nepsilon-[carboxymethyl]-lysine (CML), was detected by liquid chromatography mass spectrometry (LC-MS). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results showed decreased mobility in fructosylated-HSA. Perturbations in secondary and tertiary structure were revealed by fourier transform-infrared spectroscopy (FT-IR), supported by far- and near-UV circular dichroism (CD). Dynamic light scattering (DLS) and Matrix-Assisted Laser Desorption Ionization-Time of Flight (MALDI-TOF) mass spectrometry studies suggested increase in molecular mass of fructosylated-HSA. Amyloidogenic aggregates were confirmed from Congo red, Thioflavin T assay and Scanning electron microscope (SEM). These investigations confirmed the structural alterations in fructosylated-HSA and warrants further study to probe the role of fructosylated-HSA-AGEs in hepatopathy vis-a-vis fatty liver diseases. CI - Copyright (c) 2017 Elsevier B.V. All rights reserved. FAU - Zaman, Asif AU - Zaman A AD - Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, Aligarh, India. FAU - Arif, Zarina AU - Arif Z AD - Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, Aligarh, India. FAU - Moinuddin AU - Moinuddin AD - Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, Aligarh, India. FAU - Alam, Khursheed AU - Alam K AD - Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, Aligarh, India. Electronic address: kalam786@rediffmail.com. LA - eng PT - Journal Article DEP - 20171111 PL - Netherlands TA - Int J Biol Macromol JT - International journal of biological macromolecules JID - 7909578 RN - 0 (Glycation End Products, Advanced) RN - 0 (Protein Aggregates) RN - 30237-26-4 (Fructose) RN - ZIF514RVZR (Serum Albumin, Human) SB - IM MH - Chromatography, Liquid MH - Circular Dichroism MH - Dynamic Light Scattering MH - Fructose/*chemistry/*metabolism MH - Glycation End Products, Advanced/*chemistry/*metabolism MH - Humans MH - Mass Spectrometry MH - *Protein Aggregates MH - Serum Albumin, Human/*chemistry/*metabolism MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MH - Spectroscopy, Fourier Transform Infrared OTO - NOTNLM OT - AGEs OT - Fructose OT - Human serum albumin EDAT- 2017/11/15 06:00 MHDA- 2018/08/10 06:00 CRDT- 2017/11/15 06:00 PHST- 2017/09/12 00:00 [received] PHST- 2017/11/08 00:00 [revised] PHST- 2017/11/10 00:00 [accepted] PHST- 2017/11/15 06:00 [pubmed] PHST- 2018/08/10 06:00 [medline] PHST- 2017/11/15 06:00 [entrez] AID - S0141-8130(17)33517-1 [pii] AID - 10.1016/j.ijbiomac.2017.11.069 [doi] PST - ppublish SO - Int J Biol Macromol. 2018 Apr 1;109:896-906. doi: 10.1016/j.ijbiomac.2017.11.069. Epub 2017 Nov 11.