A study on modification of Human Albumin by proteomic technique

Bo Li; Waqar Ahmad; Bo Peng; Shengyuan Xiao; Yulin Deng

doi:10.1109/ICCME.2007.4382053

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

Beijing Institute of Technology

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-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 language	English
Title of host publication	2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007
Pages	1775-1781
Number of pages	7
DOIs	https://doi.org/10.1109/ICCME.2007.4382053
Publication status	Published - 2007
Event	2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007 - Beijing, China Duration: 23 May 2007 → 27 May 2007

Publication series

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

Conference

Conference	2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007
Country/Territory	China
City	Beijing
Period	23/05/07 → 27/05/07

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

AGEs
Biomarker
Glycation
LC/MS

Access to Document

10.1109/ICCME.2007.4382053

Cite this

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title = "A study on modification of Human Albumin by proteomic technique",

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.",

keywords = "AGEs, Biomarker, Glycation, LC/MS",

author = "Bo Li and Waqar Ahmad and Bo Peng and Shengyuan Xiao and Yulin Deng",

year = "2007",

doi = "10.1109/ICCME.2007.4382053",

language = "English",

isbn = "1424410789",

series = "2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007",

pages = "1775--1781",

booktitle = "2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007",

note = "2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007 ; Conference date: 23-05-2007 Through 27-05-2007",

}

Li, B, Ahmad, W, Peng, B, Xiao, S & Deng, Y 2007, A study on modification of Human Albumin by proteomic technique. in 2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007., 4382053, 2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007, pp. 1775-1781, 2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007, Beijing, China, 23/05/07. https://doi.org/10.1109/ICCME.2007.4382053

A study on modification of Human Albumin by proteomic technique. / Li, Bo; Ahmad, Waqar; Peng, Bo et al.
2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007. 2007. p. 1775-1781 4382053 (2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

TY - GEN

T1 - A study on modification of Human Albumin by proteomic technique

AU - Li, Bo

AU - Ahmad, Waqar

AU - Peng, Bo

AU - Xiao, Shengyuan

AU - Deng, Yulin

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

KW - AGEs

KW - Biomarker

KW - Glycation

KW - LC/MS

UR - https://www.scopus.com/pages/publications/48149093833

U2 - 10.1109/ICCME.2007.4382053

DO - 10.1109/ICCME.2007.4382053

M3 - Conference contribution

AN - SCOPUS:48149093833

SN - 1424410789

SN - 9781424410781

T3 - 2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007

SP - 1775

EP - 1781

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

T2 - 2007 IEEE/ICME International Conference on Complex Medical Engineering, CME 2007

Y2 - 23 May 2007 through 27 May 2007

ER -

A study on modification of Human Albumin by proteomic technique

Abstract

Publication series

Conference

UN SDGs

Keywords

Access to Document

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