Home > Research > Publications & Outputs > Rational Targeting of Subclasses of Intermolecu...

Links

Text available via DOI:

View graph of relations

Rational Targeting of Subclasses of Intermolecular Interactions: Elimination of Nonspecific Binding for Analyte Sensing

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Published

Standard

Rational Targeting of Subclasses of Intermolecular Interactions: Elimination of Nonspecific Binding for Analyte Sensing. / Lane, Jordan S.; Richens, Joanna L.; Vere, Kelly-Ann et al.
In: Langmuir, Vol. 30, No. 31, 12.08.2014, p. 9457-9465.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

APA

Vancouver

Lane JS, Richens JL, Vere KA, O'Shea P. Rational Targeting of Subclasses of Intermolecular Interactions: Elimination of Nonspecific Binding for Analyte Sensing. Langmuir. 2014 Aug 12;30(31):9457-9465. doi: 10.1021/la5016548

Author

Lane, Jordan S. ; Richens, Joanna L. ; Vere, Kelly-Ann et al. / Rational Targeting of Subclasses of Intermolecular Interactions : Elimination of Nonspecific Binding for Analyte Sensing. In: Langmuir. 2014 ; Vol. 30, No. 31. pp. 9457-9465.

Bibtex

@article{7ee6ee8d3a0f42298bdd3d7bcb025e0e,
title = "Rational Targeting of Subclasses of Intermolecular Interactions: Elimination of Nonspecific Binding for Analyte Sensing",
abstract = "The ability to target and control intermolecular interactions is crucial in the development of several different technologies. Here we offer a tool to rationally design liquid media systems that can modulate specific intermolecular interactions. This has broad implications in deciphering the nature of intermolecular forces in complex solutions and offers insight into the forces that govern both specific and nonspecific binding in a given system. Nonspecific binding still continues to be a problem when dealing with analyte detection across a range of different detection technologies. Here, we exemplify the problem of nonspecific binding on model membrane systems and when dealing with low-abundance protein detection on commercially available SPR technology. A range of different soluble reagents that target specific subclasses of intermolecular interactions have been tested and optimized to virtually eliminate nonspecific binding while leaving specific interactions unperturbed. Thiocyanate ions are used to target nonpolar interactions, and small reagents such as glycylglycylglycine are used to modulate the dielectric constant, which targets charge–charge and dipole interactions. We show that with rational design and careful modulation these reagents offer a step forward in dissecting the intermolecular forces that govern binding, alongside offering nonspecific binding elimination in detection systems.",
author = "Lane, {Jordan S.} and Richens, {Joanna L.} and Kelly-Ann Vere and Paul O'Shea",
year = "2014",
month = aug,
day = "12",
doi = "10.1021/la5016548",
language = "English",
volume = "30",
pages = "9457--9465",
journal = "Langmuir",
issn = "0743-7463",
publisher = "AMER CHEMICAL SOC",
number = "31",

}

RIS

TY - JOUR

T1 - Rational Targeting of Subclasses of Intermolecular Interactions

T2 - Elimination of Nonspecific Binding for Analyte Sensing

AU - Lane, Jordan S.

AU - Richens, Joanna L.

AU - Vere, Kelly-Ann

AU - O'Shea, Paul

PY - 2014/8/12

Y1 - 2014/8/12

N2 - The ability to target and control intermolecular interactions is crucial in the development of several different technologies. Here we offer a tool to rationally design liquid media systems that can modulate specific intermolecular interactions. This has broad implications in deciphering the nature of intermolecular forces in complex solutions and offers insight into the forces that govern both specific and nonspecific binding in a given system. Nonspecific binding still continues to be a problem when dealing with analyte detection across a range of different detection technologies. Here, we exemplify the problem of nonspecific binding on model membrane systems and when dealing with low-abundance protein detection on commercially available SPR technology. A range of different soluble reagents that target specific subclasses of intermolecular interactions have been tested and optimized to virtually eliminate nonspecific binding while leaving specific interactions unperturbed. Thiocyanate ions are used to target nonpolar interactions, and small reagents such as glycylglycylglycine are used to modulate the dielectric constant, which targets charge–charge and dipole interactions. We show that with rational design and careful modulation these reagents offer a step forward in dissecting the intermolecular forces that govern binding, alongside offering nonspecific binding elimination in detection systems.

AB - The ability to target and control intermolecular interactions is crucial in the development of several different technologies. Here we offer a tool to rationally design liquid media systems that can modulate specific intermolecular interactions. This has broad implications in deciphering the nature of intermolecular forces in complex solutions and offers insight into the forces that govern both specific and nonspecific binding in a given system. Nonspecific binding still continues to be a problem when dealing with analyte detection across a range of different detection technologies. Here, we exemplify the problem of nonspecific binding on model membrane systems and when dealing with low-abundance protein detection on commercially available SPR technology. A range of different soluble reagents that target specific subclasses of intermolecular interactions have been tested and optimized to virtually eliminate nonspecific binding while leaving specific interactions unperturbed. Thiocyanate ions are used to target nonpolar interactions, and small reagents such as glycylglycylglycine are used to modulate the dielectric constant, which targets charge–charge and dipole interactions. We show that with rational design and careful modulation these reagents offer a step forward in dissecting the intermolecular forces that govern binding, alongside offering nonspecific binding elimination in detection systems.

U2 - 10.1021/la5016548

DO - 10.1021/la5016548

M3 - Journal article

VL - 30

SP - 9457

EP - 9465

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 31

ER -