Conformational photoswitching of a synthetic peptide foldamer bound within a phospholipid bilayer
- 29 April 2016
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 352 (6285), 575-580
- https://doi.org/10.1126/science.aad8352
Abstract
Synthetic twists among lipids: Proteins embedded in cell membranes perform a wide variety of signaling and transport functions through conformational shifts. De Poli et al. examined how a much smaller, simpler construct might begin to achieve similar aims (see the Perspective by Thiele and Ulrich). Specifically, they designed an artificial peptide with a photosensitive group at one end and embedded it in a phospholipid bilayer akin to a membrane. Nuclear magnetic resonance spectroscopy revealed how light-induced isomerization influenced conformational dynamics at the other end. The results point the way toward development of small-molecule–based switches in membrane environments. Science , this issue p. 575 ; see also p. 520Funding Information
- European Research Council
- UK Engineering and Physical Sciences Research Council (EP/K039547/1, EP/N009134/1)
This publication has 55 references indexed in Scilit:
- 2D 1H/1H RFDR and NOESY NMR Experiments on a Membrane-Bound Antimicrobial Peptide Under Magic Angle SpinningThe Journal of Physical Chemistry B, 2013
- Membrane Protein Structure and Dynamics from NMR SpectroscopyAnnual Review of Physical Chemistry, 2012
- Vesicular assembly and thermo-responsive vesicle-to-micelle transition from an amphiphilic random copolymerChemical Communications, 2011
- Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMRScience, 2010
- Orientation, Dynamics, and Lipid Interaction of an Antimicrobial Arylamide Investigated by 19F and 31P Solid-State NMR SpectroscopyJournal of the American Chemical Society, 2010
- Lipid Bilayer Structure Determined by the Simultaneous Analysis of Neutron and X-Ray Scattering DataBiophysical Journal, 2008
- Dynamic personalities of proteinsNature, 2007
- NMR methods for studying membrane‐active antimicrobial peptidesConcepts in Magnetic Resonance Part A, 2004
- The Preference of Tryptophan for Membrane InterfacesBiochemistry, 1998
- Elektronenstruktur und physikalisch‐chemische Eigenschaften von Azo‐Verbindungen. Teil VIII: Die konjugaten Säuren des trans‐ und des cis‐ AzobenzolsHelvetica Chimica Acta, 1960