Surface plasmon resonance: A useful technique for cell biologists to characterize biomolecular interactions

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein-protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid-protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid-protein interactions and highlights the unique lipid-protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid-protein interactions.

Original languageEnglish
Pages (from-to)883-886
Number of pages4
JournalMolecular Biology of the Cell
Volume24
Issue number7
DOIs
StatePublished - Apr 1 2013

Fingerprint

Surface Plasmon Resonance
Lipids
Proteins
Ligands
Membrane Lipids
Membranes
Research

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

@article{e07db9b58abe4338aace947121c9c11a,
title = "Surface plasmon resonance: A useful technique for cell biologists to characterize biomolecular interactions",
abstract = "Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein-protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid-protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid-protein interactions and highlights the unique lipid-protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid-protein interactions.",
author = "Robert Stahelin",
year = "2013",
month = "4",
day = "1",
doi = "10.1091/mbc.E12-10-0713",
language = "English",
volume = "24",
pages = "883--886",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "7",

}

TY - JOUR

T1 - Surface plasmon resonance

T2 - A useful technique for cell biologists to characterize biomolecular interactions

AU - Stahelin, Robert

PY - 2013/4/1

Y1 - 2013/4/1

N2 - Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein-protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid-protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid-protein interactions and highlights the unique lipid-protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid-protein interactions.

AB - Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein-protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid-protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid-protein interactions and highlights the unique lipid-protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid-protein interactions.

UR - http://www.scopus.com/inward/record.url?scp=84875459950&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84875459950&partnerID=8YFLogxK

U2 - 10.1091/mbc.E12-10-0713

DO - 10.1091/mbc.E12-10-0713

M3 - Article

C2 - 23533209

AN - SCOPUS:84875459950

VL - 24

SP - 883

EP - 886

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 7

ER -