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Pulmonary Surfactant Lipid Reorganization Induced by the Adsorption of the Oligomeric Surfactant Protein B Complex
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SYSNO ASEP 0523856 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Pulmonary Surfactant Lipid Reorganization Induced by the Adsorption of the Oligomeric Surfactant Protein B Complex Author(s) Liekkinen, J. (FI)
Enkavi, G. (FI)
Javanainen, Matti (UOCHB-X) RID, ORCID
Olmeda, B. (ES)
Pérez-Gil, J. (ES)
Vattulainen, I. (FI)Source Title Journal of Molecular Biology. - : Elsevier - ISSN 0022-2836
Roč. 432, č. 10 (2020), s. 3251-3268Number of pages 18 s. Language eng - English Country GB - United Kingdom Keywords pulmonary surfactant ; protein–lipid interactions ; SP-B ; molecular dynamics simulation Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry Method of publishing Open access Institutional support UOCHB-X - RVO:61388963 UT WOS 000532829100011 EID SCOPUS 85082856561 DOI 10.1016/j.jmb.2020.02.028 Annotation Surfactant protein B (SP-B) is essential in transferring surface-active phospholipids from membrane-based surfactant complexes into the alveolar air–liquid interface. This allows maintaining the mechanical stability of the surfactant film under high pressure at the end of expiration, therefore, SP-B is crucial in lung function. Despite its necessity, the structure and the mechanism of lipid transfer by SP-B have remained poorly characterized. Earlier, we proposed higher-order oligomerization of SP-B into ring-like supramolecular assemblies. In the present work, we used coarse-grained molecular dynamics simulations to elucidate how the ring-like oligomeric structure of SP-B determines its membrane binding and lipid transfer. In particular, we explored how SP-B interacts with specific surfactant lipids, and how consequently SP-B reorganizes its lipid environment to modulate the pulmonary surfactant structure and function. Based on these studies, there are specific lipid–protein interactions leading to perturbation and reorganization of pulmonary surfactant layers. Especially, we found compelling evidence that anionic phospholipids and cholesterol are needed or even crucial in the membrane binding and lipid transfer function of SP-B. Also, on the basis of the simulations, larger oligomers of SP-B catalyze lipid transfer between adjacent surfactant layers. Better understanding of the molecular mechanism of SP-B will help in the design of therapeutic SP-B-based preparations and novel treatments for fatal respiratory complications, such as the acute respiratory distress syndrome. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2021 Electronic address https://www.sciencedirect.com/science/article/pii/S0022283620302059
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