NAGARAJ, Vignesh Udyavara, Tunde JUHASZ, Mayra QUEME-PENA, Imola Cs SZIGYARTO, Dora BOGDAN, Andras WACHA, Judith MIHALY, Lorand ROMANSZKI, Zoltan VARGA, Joakim ANDREASSON, Istvan MANDITY and Tamas BEKE-SOMFAI. Stimuli-Responsive Membrane Anchor Peptide Nanofoils for Tunable Membrane Association and Lipid Bilayer Fusion. ACS APPLIED MATERIALS & INTERFACES. WASHINGTON: AMER CHEMICAL SOC, 2022, vol. 14, No 50, p. 55320-55331. ISSN 1944-8244. Available from: https://dx.doi.org/10.1021/acsami.2c11946.
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Basic information
Original name Stimuli-Responsive Membrane Anchor Peptide Nanofoils for Tunable Membrane Association and Lipid Bilayer Fusion
Authors NAGARAJ, Vignesh Udyavara, Tunde JUHASZ, Mayra QUEME-PENA, Imola Cs SZIGYARTO, Dora BOGDAN, Andras WACHA, Judith MIHALY, Lorand ROMANSZKI, Zoltan VARGA, Joakim ANDREASSON, Istvan MANDITY and Tamas BEKE-SOMFAI (guarantor).
Edition ACS APPLIED MATERIALS & INTERFACES, WASHINGTON, AMER CHEMICAL SOC, 2022, 1944-8244.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 21000 2.10 Nano-technology
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 9.500
RIV identification code RIV/00216224:90127/22:00133747
Doi http://dx.doi.org/10.1021/acsami.2c11946
UT WoS 000894035600001
Keywords in English self-assembly; liposomes; membrane activity; spiropyran; peptide bilayer; lipid bilaye r fusion
Tags CF CRYO, ne MU, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Michal Petr, učo 65024. Changed: 12/4/2024 13:03.
Abstract
Self-assembled peptide nanostructures with stimuli-responsive features are promising as functional materials. Despite extensive research efforts, water-soluble supramolecular constructs that can interact with lipid membranes in a controllable way are still challenging to achieve. Here, we have employed a short membrane anchor protein motif (GLFD) and coupled it to a spiropyran photoswitch. Under physiological conditions, these conjugates assemble into similar to 3.5 nm thick, foil-like peptide bilayer morphologies. Photo-isomerization from the closed spiro (SP) form to the open merocyanine (MC) form of the photoswitch triggers rearrangements within the foils. This results in substantial changes in their membrane-binding properties, which also varies sensitively to lipid composition, ranging from reversible nanofoil reformation to stepwise membrane adsorption. The formed peptide layers in the assembly are also able to attach to various liposomes with different surface charges, enabling the fusion of their lipid bilayers. Here, SP-to-MC conversion can be used both to trigger and to modulate the liposome fusion efficiency.
Links
90127, large research infrastructuresName: CIISB II
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