Dimerization of the pulmonary surfactant protein C in a membrane environment

Author:

Korolainen Hanna,Lolicato FabioORCID,Enkavi GirayORCID,Pérez-Gil Jesús,Kulig WaldemarORCID,Vattulainen IlpoORCID

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.

Funder

Academy of Finland

University of Helsinki

Spanish Ministry of Science and Innovation

Regional Government of Madrid

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

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