Nelumbo nucifera leaf extracts inhibit the formation of advanced glycation end-products and mechanism revealed by Nano LC-Orbitrap-MS/MS

• Published in: Journal of functional foods Vol. 42; pp. 254 - 261
• Main Authors: Zhang, Lu, Zhang, Chong-ju, Tu, Zong-cai, Yang, Wen-hua, Zhao, Yi, Xin, Zheng-qi, Wang, Hui, Sha, Xiao-mei, Chen, Juan
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.03.2018; Elsevier
• Subjects: Advanced glycation end-products; Glycation degree; Glycation sites; Nano LC-Orbitrap-MS/MS; Nelumbo nucifera leaf; Structure; Advanced glycation end-products; CE; DCF; AG; Glycation degree; Fru; BF-CE; AGEs; EAF; Glycation sites; NNL; Nelumbo nucifera leaf; BF-EAF; WF; BSA; BF-DCF; MGO; BF-nBuF; nBuF; Arg; Nano LC-Orbitrap-MS/MS; BF-WF; Structure
• ISSN: 1756-4646; 2214-9414
• DOI: 10.1016/j.jff.2018.01.012

•The EAF of NNL shows superior inhibition on AGEs than aminoguanidine.•The inhibitory mechanism was elucidated by high resolution mass spectrometry.•NNL extracts attenuate the conformational change of BSA induced by glycation.•11 and 10 glycation sites were identified from glycated BSA with and without EAF, respectively.•EAF does not reduce the glycation sites, but decrease the DSP and alter the location. The inhibition of Nelumbo nucifera leaf (NNL) extract and its fractions on the formation of advanced glycation end-products (AGEs) was evaluated with different models. Changes in the conformational structure of bovine serum albumin (BSA) were analyzed by fluorescence spectrometry. Effect of ethyl acetate fraction (EAF) on the glycation sites and glycation degree of BSA was investigated by Nano LC-Orbitrap-MS/MS due to its strongest inhibitory ability. Results indicated that EAF could effectively inhibit the formation of AGEs by scavenging reactive radicals and attenuating the conformational change of BSA induced by glycation. Phenolics and flavonoids were the major contributors. Eleven (11 lysines) and ten (9 lysines and 1 arginine) glycation sites were identified from glycated BSA with and without EAF, respectively. Addition of EAF could not reduce the number of glycation sites of BSA, but could significantly decrease the glycation degree of most glycated peptides and alter the location of glycation.