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Affinity characteristic of terminal sequence in vancomycin resistant Enterococcus (VRE) membrane peptides on nanobiosensor chip using localized surface plasmon resonance

Affinity characteristic of terminal sequence in vancomycin resistant Enterococcus (VRE) membrane... Abstract In this study, specific binding affinity between vancomycin (VAN) conjugated 40-50 nm gold nanoparticles (Au NPs) implemented on a sensor chip and pentapeptide mimicking pathogenic VAN resistant Enterococcus (VRE) wall membrane was employed as nanosensor format based on localized surface plasmon resonance (LSPR). Two pentapeptides, which were also anchored to 5 nm Au NPs, having two different terminal sequences of d-Ala-d-Ala and d-Ala-d-Lac respectively were compared in specific binding affinity toward the VAN conjugated nanosensor. Binding affinity difference identified by the LSPR characteristic in the nanosensor was shown in absorbance intensity and absorption wavelength shift between the two different terminal pentapeptides. The absorbance intensity clearly indicated that the pentapeptide having terminal d-Ala-d-Lac showed less affinity toward VAN conjugated nanosensor chip than that having terminal d-Ala-d-Ala. It indicates that the VRE itself has relatively weak binding strength towards the VAN, which may be used as a probe molecule for the VRE. Therefore, in order to design a VRE sensor using the VAN affinity, an indirect LSPR method can be devised instead of direct LSPR method. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png BioChip Journal Springer Journals

Affinity characteristic of terminal sequence in vancomycin resistant Enterococcus (VRE) membrane peptides on nanobiosensor chip using localized surface plasmon resonance

Lee, Kyungmin; Kim, Yo-Han; Jung, Hunsang; Lee, Hyun Ho
BioChip Journal , Volume 11 (2): 8 – Jun 1, 2017
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References (12)

Publisher
Springer Journals
Copyright
2017 The Korean BioChip Society and Springer-Verlag Berlin Heidelberg
ISSN
1976-0280
eISSN
2092-7843
DOI
10.1007/s13206-016-1206-4
Publisher site
See Article on Publisher Site

Abstract

Abstract In this study, specific binding affinity between vancomycin (VAN) conjugated 40-50 nm gold nanoparticles (Au NPs) implemented on a sensor chip and pentapeptide mimicking pathogenic VAN resistant Enterococcus (VRE) wall membrane was employed as nanosensor format based on localized surface plasmon resonance (LSPR). Two pentapeptides, which were also anchored to 5 nm Au NPs, having two different terminal sequences of d-Ala-d-Ala and d-Ala-d-Lac respectively were compared in specific binding affinity toward the VAN conjugated nanosensor. Binding affinity difference identified by the LSPR characteristic in the nanosensor was shown in absorbance intensity and absorption wavelength shift between the two different terminal pentapeptides. The absorbance intensity clearly indicated that the pentapeptide having terminal d-Ala-d-Lac showed less affinity toward VAN conjugated nanosensor chip than that having terminal d-Ala-d-Ala. It indicates that the VRE itself has relatively weak binding strength towards the VAN, which may be used as a probe molecule for the VRE. Therefore, in order to design a VRE sensor using the VAN affinity, an indirect LSPR method can be devised instead of direct LSPR method.

Journal

BioChip Journal – Springer Journals

Published: Jun 1, 2017

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