Analysis of Peptides and Proteins Affinity-Bound to lron Oxide Nanoparticles by MALDI MS

CNU IR > Pharmacy and Science > The 5rh Conference of Channel-bridge Chemistry, Biology and materal Science > Item 310902800/30495

Please use this identifier to cite or link to this item: https://ir.cnu.edu.tw/handle/310902800/30495

Title:	Analysis of Peptides and Proteins Affinity-Bound to lron Oxide Nanoparticles by MALDI MS
Authors:	Sarah Y. Chang Nan-Yan Zheng C. R. Chris Wang
Contributors:	Department of Chemistry,Tunghai University Department of Applied Chemistry, Chaoyang University of Technology Department of Chemistry and Biochemistry, National Chung Chung University
Keywords:	iron oxide nanoparticle peptides proteins
Date:	2008-07
Issue Date:	2017-12-04 15:56:09 (UTC+8)
Abstract:	Iron oxide nanoparticles modified with oleate have been employed to the extraction of peptides and proteins from aqueous solution prior to matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) analysis. Adsorption of peptides and proteins onto the nanoparticles were mainly through electrostatic attraction and hydrophobic interaction. The analyte-adsorbed iron oxide nanoparticles could be efficiently collected from solution using a magnet. No elution step was needed. With this preconcentration strategy, the lowest detectable concentration of angiotensin I, insulin and myoglobin in 500 μL of aqueous solution were 0.1 nM, 0.1 nM and 10.0 nM, respectively. In addition, the nanoparticles could extract the analytes from solution with a high content of salt and surfactant, thus eliminating suppression effect during MALDI MS analysis. This method was successfully applied to concentrate the tryptic digest products of cytochromec. In addition, the tryptic digestion of cytochrome c can be directly conducted on the iron oxide nanoparticles.
Relation:	第五屆海峽化學、生物及材料研討會，起迄日：2008/07/21-2008/07/22，地點：嘉南藥理科技大學
Appears in Collections:	[Pharmacy and Science] The 5rh Conference of Channel-bridge Chemistry, Biology and materal Science

Files in This Item:

File	Description	Size	Format
C15.pdf		326Kb	Adobe PDF	275	View/Open

Loading...