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Surfactant Proteins SP-B and SP-C in Pulmonary Surfactant Monolayers: Physical Properties Controlled by Specific Protein–Lipid Interactions
[Image: see text] The lining of the alveoli is covered by pulmonary surfactant, a complex mixture of surface-active lipids and proteins that enables efficient gas exchange between inhaled air and the circulation. Despite decades of advancements in the study of the pulmonary surfactant, the molecular...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10061932/ https://www.ncbi.nlm.nih.gov/pubmed/36917773 http://dx.doi.org/10.1021/acs.langmuir.2c03349 |
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author | Liekkinen, Juho Olżyńska, Agnieszka Cwiklik, Lukasz Bernardino de la Serna, Jorge Vattulainen, Ilpo Javanainen, Matti |
author_facet | Liekkinen, Juho Olżyńska, Agnieszka Cwiklik, Lukasz Bernardino de la Serna, Jorge Vattulainen, Ilpo Javanainen, Matti |
author_sort | Liekkinen, Juho |
collection | PubMed |
description | [Image: see text] The lining of the alveoli is covered by pulmonary surfactant, a complex mixture of surface-active lipids and proteins that enables efficient gas exchange between inhaled air and the circulation. Despite decades of advancements in the study of the pulmonary surfactant, the molecular scale behavior of the surfactant and the inherent role of the number of different lipids and proteins in surfactant behavior are not fully understood. The most important proteins in this complex system are the surfactant proteins SP-B and SP-C. Given this, in this work we performed nonequilibrium all-atom molecular dynamics simulations to study the interplay of SP-B and SP-C with multicomponent lipid monolayers mimicking the pulmonary surfactant in composition. The simulations were complemented by z-scan fluorescence correlation spectroscopy and atomic force microscopy measurements. Our state-of-the-art simulation model reproduces experimental pressure–area isotherms and lateral diffusion coefficients. In agreement with previous research, the inclusion of either SP-B and SP-C increases surface pressure, and our simulations provide a molecular scale explanation for this effect: The proteins display preferential lipid interactions with phosphatidylglycerol, they reside predominantly in the lipid acyl chain region, and they partition into the liquid expanded phase or even induce it in an otherwise packed monolayer. The latter effect is also visible in our atomic force microscopy images. The research done contributes to a better understanding of the roles of specific lipids and proteins in surfactant function, thus helping to develop better synthetic products for surfactant replacement therapy used in the treatment of many fatal lung-related injuries and diseases. |
format | Online Article Text |
id | pubmed-10061932 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-100619322023-03-31 Surfactant Proteins SP-B and SP-C in Pulmonary Surfactant Monolayers: Physical Properties Controlled by Specific Protein–Lipid Interactions Liekkinen, Juho Olżyńska, Agnieszka Cwiklik, Lukasz Bernardino de la Serna, Jorge Vattulainen, Ilpo Javanainen, Matti Langmuir [Image: see text] The lining of the alveoli is covered by pulmonary surfactant, a complex mixture of surface-active lipids and proteins that enables efficient gas exchange between inhaled air and the circulation. Despite decades of advancements in the study of the pulmonary surfactant, the molecular scale behavior of the surfactant and the inherent role of the number of different lipids and proteins in surfactant behavior are not fully understood. The most important proteins in this complex system are the surfactant proteins SP-B and SP-C. Given this, in this work we performed nonequilibrium all-atom molecular dynamics simulations to study the interplay of SP-B and SP-C with multicomponent lipid monolayers mimicking the pulmonary surfactant in composition. The simulations were complemented by z-scan fluorescence correlation spectroscopy and atomic force microscopy measurements. Our state-of-the-art simulation model reproduces experimental pressure–area isotherms and lateral diffusion coefficients. In agreement with previous research, the inclusion of either SP-B and SP-C increases surface pressure, and our simulations provide a molecular scale explanation for this effect: The proteins display preferential lipid interactions with phosphatidylglycerol, they reside predominantly in the lipid acyl chain region, and they partition into the liquid expanded phase or even induce it in an otherwise packed monolayer. The latter effect is also visible in our atomic force microscopy images. The research done contributes to a better understanding of the roles of specific lipids and proteins in surfactant function, thus helping to develop better synthetic products for surfactant replacement therapy used in the treatment of many fatal lung-related injuries and diseases. American Chemical Society 2023-03-14 /pmc/articles/PMC10061932/ /pubmed/36917773 http://dx.doi.org/10.1021/acs.langmuir.2c03349 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Liekkinen, Juho Olżyńska, Agnieszka Cwiklik, Lukasz Bernardino de la Serna, Jorge Vattulainen, Ilpo Javanainen, Matti Surfactant Proteins SP-B and SP-C in Pulmonary Surfactant Monolayers: Physical Properties Controlled by Specific Protein–Lipid Interactions |
title | Surfactant
Proteins SP-B and SP-C in
Pulmonary Surfactant Monolayers: Physical Properties Controlled by
Specific Protein–Lipid Interactions |
title_full | Surfactant
Proteins SP-B and SP-C in
Pulmonary Surfactant Monolayers: Physical Properties Controlled by
Specific Protein–Lipid Interactions |
title_fullStr | Surfactant
Proteins SP-B and SP-C in
Pulmonary Surfactant Monolayers: Physical Properties Controlled by
Specific Protein–Lipid Interactions |
title_full_unstemmed | Surfactant
Proteins SP-B and SP-C in
Pulmonary Surfactant Monolayers: Physical Properties Controlled by
Specific Protein–Lipid Interactions |
title_short | Surfactant
Proteins SP-B and SP-C in
Pulmonary Surfactant Monolayers: Physical Properties Controlled by
Specific Protein–Lipid Interactions |
title_sort | surfactant
proteins sp-b and sp-c in
pulmonary surfactant monolayers: physical properties controlled by
specific protein–lipid interactions |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10061932/ https://www.ncbi.nlm.nih.gov/pubmed/36917773 http://dx.doi.org/10.1021/acs.langmuir.2c03349 |
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