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June 2021
Science Advances
Stable but not rigid: Chronic in vivo STED nanoscopy reveals extensive remodeling of spines, indicating multiple drivers of plasticity
Steffens H, Mott AC, Li S, Wegner W, Švehla P, Kan VWY, Wolf F, Liebscher S, Willig KI
June 2021
Nature Protocols
Graphene- and metal-induced energy transfer for single-molecule imaging and live-cell nanoscopy with (sub)-nanometer axial resolution
Ghosh A, Chizhik AI, Karedla N, Enderlein J
June 2021
Journal of Peptide Science
Transmembrane β-peptide helices as molecular rulers at the membrane surface
Kloos M, Sharma A, Enderlein J, Diederichsen U

Authors

Kloos M, Sharma A, Enderlein J, Diederichsen U

Journal

Journal of Peptide Science

Citation

J Pept Sci. 2021 Jun 2:e3355.

Abstract

β-Peptides are known to form 14-helices with high conformational rigidity, helical persistence length, and well-defined spacing and orientation regularity of amino acid side chains. Therefore, β-peptides are well suited to serve as backbone structures for molecular rulers. On the one hand, they can be functionalized in a site-specific manner with molecular probes or fluorophores, and on the other hand, the β-peptide helices can be recognized and anchored in a biological environment of interest. In this study, the β-peptide helices were anchored in lipid bilayer membranes, and the helices were elongated in the outer membrane environment. The distances of the covalently bound probes to the membrane surface were determined using graphene-induced energy transfer (GIET) spectroscopy, a method based on the distance-dependent quenching of a fluorescent molecule by a nearby single graphene sheet. As a proof of principle, the predicted distances were determined for two fluorophores bound to the membrane-anchored β-peptide molecular ruler.

DOI

10.1002/psc.3355

 
Pubmed Link

 

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