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The selective adsorption of human serum albumin on N-isobutyryl-cysteine enantiomers modified chiral surfaces

Paper ID Volume ID Publish Year Pages File Format Full-Text
3549 174 2012 4 PDF Available
Title
The selective adsorption of human serum albumin on N-isobutyryl-cysteine enantiomers modified chiral surfaces
Abstract

The stereoselective interaction between human serum albumin (HSA) and N-isobutyryl-cysteine (NIBC) enantiomers was investigated by cyclic voltammetry and electrochemical impedance spectroscopy. The electrochemical responses of the NIBC enantiomers modified surfaces were varied along with the inserted time and the concentration of HSA. The results showed that HSA molecules displayed different adsorption behaviors on NIBC enantiomers modified surfaces and preferred to be adsorbed on the l-NIBC modified surface. That is to say, l-NIBC modified surface had stronger interaction with HSA molecules than d-NIBC modified surface, suggesting that the molecular configuration of l-NIBC had matched better with HSA than the case of d-NIBC. The investigation of the interaction between protein and chiral molecules may not only help to understand the high selectivity of chirality in biosystems, but also provide a reference for studying chiral drugs.

Graphical abstractThe schematic representation of l-NIBC-Au (a) and d-NIBC-Au (b) interact with HSA. The molecular configuration of l-NIBC had matched better with HSA than the case of d-NIBC.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Electrochemical methods were used to investigate the enantioselective interaction. ► HSA showed different behaviors on N-isobutyryl-cysteine enantiomers chiral surfaces. ► Larger electrochemical response signals were observed after HSA adsorbed on N-isobutyryl-l-cysteine-Au than N-isobutyryl-d-cysteine-Au. ► This work provides a reference for studying chiral drugs.

Keywords
N-isobutyryl-cysteine; Human serum albumin; Adsorption; Amino acids; Protein; Sensors
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The selective adsorption of human serum albumin on N-isobutyryl-cysteine enantiomers modified chiral surfaces
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 69, 15 December 2012, Pages 155–158
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
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