Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide

Understanding the interplay between lipid assemblies and solid supports is crucial for advancing model membrane systems and biomedical applications. This study investigates the interfacial behaviors of unilamellar and multilamellar cationic liposomes on silicon dioxide and their interactions with a...

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Main Authors: Tae, Hyunhyuk, Park, Soohyun, Choe, Younghwan, Yang, Chungmo, Cho, Nam-Joon
Other Authors: School of Materials Science and Engineering
Format: Article
Language:English
Published: 2024
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Online Access:https://hdl.handle.net/10356/181047
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1810472024-11-12T05:58:19Z Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide Tae, Hyunhyuk Park, Soohyun Choe, Younghwan Yang, Chungmo Cho, Nam-Joon School of Materials Science and Engineering Engineering Membrane-active peptide Cationic liposomes Understanding the interplay between lipid assemblies and solid supports is crucial for advancing model membrane systems and biomedical applications. This study investigates the interfacial behaviors of unilamellar and multilamellar cationic liposomes on silicon dioxide and their interactions with a membrane-active AH peptide. Using QCM-D monitoring, unilamellar liposomes were found to rapidly form SLBs through one-step adsorption kinetics, whereas multilamellar liposomes exhibited slower adsorption. Further addition of liposomes caused fusogenic interactions with SLBs, where multilamellar liposomes formed more rigid lipid membranes. Upon AH peptide exposure, unilamellar-based lipid membranes showed higher susceptibility to structural transformations, achieving complete SLB formation, while multilamellar-based lipid membranes displayed reduced sensitivity and retained residual viscoelastic components, indicative of incomplete SLB formation. These findings underscore the significant influence of liposome lamellarity on their interfacial dynamics and peptide interactions, crucial for designing effective lipid-based delivery and sensing systems. Agency for Science, Technology and Research (A*STAR) Ministry of Education (MOE) National Research Foundation (NRF) This research was supported by the Ministry of Education (MOE) in Singapore under Grants RG111/20 and RG34/22. In addition, this work was supported by the National Research Foundation in Singapore (NRF) under Grant REQ414940. H.T. is supported by a SINGA graduate scholarship from the A*STAR Graduate Academy, Singapore. 2024-11-12T05:58:19Z 2024-11-12T05:58:19Z 2024 Journal Article Tae, H., Park, S., Choe, Y., Yang, C. & Cho, N. (2024). Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide. Langmuir. https://dx.doi.org/10.1021/acs.langmuir.4c02273 0743-7463 https://hdl.handle.net/10356/181047 10.1021/acs.langmuir.4c02273 39267337 2-s2.0-85203825913 en RG111/20 RG34/22 REQ414940 Langmuir © 2024 American Chemical Society. All rights reserved.
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering
Membrane-active peptide
Cationic liposomes
spellingShingle Engineering
Membrane-active peptide
Cationic liposomes
Tae, Hyunhyuk
Park, Soohyun
Choe, Younghwan
Yang, Chungmo
Cho, Nam-Joon
Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide
description Understanding the interplay between lipid assemblies and solid supports is crucial for advancing model membrane systems and biomedical applications. This study investigates the interfacial behaviors of unilamellar and multilamellar cationic liposomes on silicon dioxide and their interactions with a membrane-active AH peptide. Using QCM-D monitoring, unilamellar liposomes were found to rapidly form SLBs through one-step adsorption kinetics, whereas multilamellar liposomes exhibited slower adsorption. Further addition of liposomes caused fusogenic interactions with SLBs, where multilamellar liposomes formed more rigid lipid membranes. Upon AH peptide exposure, unilamellar-based lipid membranes showed higher susceptibility to structural transformations, achieving complete SLB formation, while multilamellar-based lipid membranes displayed reduced sensitivity and retained residual viscoelastic components, indicative of incomplete SLB formation. These findings underscore the significant influence of liposome lamellarity on their interfacial dynamics and peptide interactions, crucial for designing effective lipid-based delivery and sensing systems.
author2 School of Materials Science and Engineering
author_facet School of Materials Science and Engineering
Tae, Hyunhyuk
Park, Soohyun
Choe, Younghwan
Yang, Chungmo
Cho, Nam-Joon
format Article
author Tae, Hyunhyuk
Park, Soohyun
Choe, Younghwan
Yang, Chungmo
Cho, Nam-Joon
author_sort Tae, Hyunhyuk
title Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide
title_short Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide
title_full Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide
title_fullStr Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide
title_full_unstemmed Exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on SiO2 and their interactions with membrane-active peptide
title_sort exploring the interfacial dynamics of unilamellar and multilamellar cationic liposomes on sio2 and their interactions with membrane-active peptide
publishDate 2024
url https://hdl.handle.net/10356/181047
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