A study on modification of Human Albumin by proteomic technique

Bo Li, Waqar Ahmad, Bo Peng, Shengyuan Xiao, Yulin Deng*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

Abstract

Advanced glycation end products (AGEs) are a heterogeneous group of complex compounds which may play a role in the pathogenesis of chronic complications associated with diabetes and aging. Glucose has the ability to crosslink proteins through creation of AGEs. This study was carried out on glycated human albumin (HA) by glucose which were analyzed by LC/MS with the aim of identifying specific peptides from glycated HA. Our objective was to find typical peptides as biomarker for clinical diagnose of diabetes and aging. This method was in vitro incubation of HA with glucose of different concentrations. Glycated and unglycated HA were digested by trypsin. AGE-peptides originated by enzymatic digestion were analysed by LC/MS. Analysis of the LC/MS data show that there were differences between peptides of glycated and unglycated HA. Some peptides detected in unglycated HA cannot be found in glycated HA. These typical peptides were considered as important markers for glycated HA.

Original languageEnglish
Title of host publication2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007
Pages1775-1781
Number of pages7
DOIs
Publication statusPublished - 2007
Event2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007 - Beijing, China
Duration: 23 May 200727 May 2007

Publication series

Name2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007

Conference

Conference2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007
Country/TerritoryChina
CityBeijing
Period23/05/0727/05/07

Keywords

  • AGEs
  • Biomarker
  • Glycation
  • LC/MS

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