Dimerization of the pulmonary surfactant protein C in a membrane environment

• Verfasst von: Korolainen, Hanna [VerfasserIn]
• Verfasst von: Lolicato, Fabio [VerfasserIn]
• Verfasst von: Enkavi, Giray [VerfasserIn]
• Verfasst von: Pérez-Gil, Jesús [VerfasserIn]
• Verfasst von: Kulig, Waldemar [VerfasserIn]
• Verfasst von: Vattulainen, Ilpo [VerfasserIn]
• Titel: Dimerization of the pulmonary surfactant protein C in a membrane environment
• Verf.angabe: Hanna Korolainen, Fabio Lolicato, Giray Enkavi, Jesús Pérez-Gil, Waldemar Kulig, Ilpo Vattulainen
• E-Jahr: 2022
• Jahr: April 27, 2022
• Umfang: 15 S.
• Fussnoten: Gesehen am 22.11.2022
• Titel Quelle: Enthalten in: PLOS ONE
• Ort Quelle: San Francisco, California, US : PLOS, 2006
• Jahr Quelle: 2022
• Band/Heft Quelle: 17(2022), 4, Artikel-ID 0267155, Seite 1-15
• ISSN Quelle: 1932-6203
• DOI: doi:10.1371/journal.pone.0267155
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Biochemical simulations
• Sach-SW: Dimerization
• Sach-SW: Dimers
• Sach-SW: Free energy
• Sach-SW: Lipid structure
• Sach-SW: Monomers
• Sach-SW: Simulation and modeling
• Sach-SW: Surfactants
• K10plus-PPN: 1823191533

Abstract

Surfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role in surfactant recycling and homeostasis, and involvement in modulation of the innate defense system. Despite these important functions, the structures of functional SP-C complexes have remained unclear. SP-C is known to exist as a primarily α-helical structure with an apparently unstructured N-terminal region, yet there is recent evidence that the functions of SP-C could be associated with the formation of SP-C dimers and higher oligomers. In this work, we used molecular dynamics simulations, two-dimensional umbrella sampling, and well-tempered metadynamics to study the details of SP-C dimerization. The results suggest that SP-C dimerizes in pulmonary surfactant membranes, forming dimers of different topologies. The simulations identified a dimerization motif region V21xxxVxxxGxxxM33 that is much larger than the putative A30xxxG34 motif that is commonly assumed to control the dimerization of some α-helical transmembrane domains. The results provide a stronger basis for elucidating how SP-C functions in concert with other surfactant proteins.