Flow linear dichroism of protein–membrane systems

Matthew R. Hicks, Sarah R. Dennison, Adewale Olamoyesan, Alison Rodger

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Linear dichroism (LD) is the differential absorbance of light polarized parallel and perpendicular to an orientation direction. Any oriented sample will show a signal in its electronic as well as vibrational transitions. Model membrane small unilamellar vesicles or liposomes provide an oriented system when they are subject to shear flow in a Couette or other type of flow cell. Anything, including peptides and proteins, that is bound to the liposome also gives an LD signal whereas unbound analytes are invisible. Flow LD is the ideal technique for determining the orientation of different chromophores with respect to the membrane normal. To illustrate the power of the method, data for diphenyl hexatriene, fluorene, antimicrobial peptides (aurein 2.5 and gramicidin), are considered as well as another common chromophore, fluorene, often used to increase the hydrophobicity and hence membrane binding of peptides. How LD can be used both for geometry, structure analysis and probing kinetic processes is considered. Kinetic analysis usually involves identifying binding (appearance of an LD signal), insertion (sign change), often followed by loss of signal, if the inserted protein or peptide disrupts the membrane.
Original languageEnglish
Title of host publicationProtein-ligand interactions
Subtitle of host publicationmethods and applications
EditorsTina Daviter, Christopher M. Johnson, Stephen H. McLaughlin, Mark A. Williams
PublisherSpringer, Springer Nature
Chapter21
Pages449-463
Number of pages15
Edition3rd
ISBN (Electronic)9781071677975
ISBN (Print)9781071611968
DOIs
Publication statusPublished - 2021

Publication series

NameMethods in Molecular Biology
PublisherSpringer
Volume2263
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • Linear dichroism
  • Membrane bilayers
  • Liposomes
  • Electronic spectroscopy
  • Infrared spectroscopy

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