Location of the Hydrophobic Surfactant Proteins, SP-B and SP-C, in Fluid-Phase Bilayers.


Journal

The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530

Informations de publication

Date de publication:
06 08 2020
Historique:
pubmed: 1 7 2020
medline: 15 5 2021
entrez: 1 7 2020
Statut: ppublish

Résumé

The hydrophobic surfactant proteins, SP-B and SP-C, promote rapid adsorption by the surfactant lipids to the surface of the liquid that lines the alveolar air sacks of the lungs. To gain insights into the mechanisms of their function, we used X-ray diffuse scattering (XDS) and molecular dynamics (MD) simulations to determine the location of SP-B and SP-C within phospholipid bilayers. Initial samples contained the surfactant lipids from extracted calf surfactant with increasing doses of the proteins. XDS located protein density near the phospholipid headgroup and in the hydrocarbon core, presumed to be SP-B and SP-C, respectively. Measurements on dioleoylphosphatidylcholine (DOPC) with the proteins produced similar results. MD simulations of the proteins with DOPC provided molecular detail and allowed direct comparison of the experimental and simulated results. Simulations used conformations of SP-B based on other members of the saposin-like family, which form either open or closed V-shaped structures. For SP-C, the amino acid sequence suggests a partial α-helix. Simulations fit best with measurements of XDS for closed SP-B, which occurred at the membrane surface, and SP-C oriented along the hydrophobic interior. Our results provide the most definitive evidence yet concerning the location and orientation of the hydrophobic surfactant proteins.

Identifiants

pubmed: 32600036
doi: 10.1021/acs.jpcb.0c03665
pmc: PMC8243356
mid: NIHMS1704312
doi:

Substances chimiques

Lipid Bilayers 0
Phospholipids 0
Pulmonary Surfactants 0
Surface-Active Agents 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

6763-6774

Subventions

Organisme : NHLBI NIH HHS
ID : R01 HL060914
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL136734
Pays : United States
Organisme : NHLBI NIH HHS
ID : R56 HL130130
Pays : United States

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Auteurs

Ryan W Loney (RW)

Pulmonary and Critical Care Medicine, Oregon Health & Science University, Portland, Oregon 97239, United States.

Sergio Panzuela (S)

Centre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB T2N 1N4, Canada.
Department of Theoretical Physics and Condensed Matter, Universidad Autónoma de Madrid, E-28049 Madrid, Spain.

Jespar Chen (J)

Biological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.

Zimo Yang (Z)

Biological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.

Jonathan R Fritz (JR)

Biological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.

Zachary Dell (Z)

Biological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.

Valentina Corradi (V)

Centre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB T2N 1N4, Canada.

Kamlesh Kumar (K)

Pulmonary and Critical Care Medicine, Oregon Health & Science University, Portland, Oregon 97239, United States.

D Peter Tieleman (DP)

Centre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB T2N 1N4, Canada.

Stephen B Hall (SB)

Pulmonary and Critical Care Medicine, Oregon Health & Science University, Portland, Oregon 97239, United States.

Stephanie A Tristram-Nagle (SA)

Biological Physics Group, Department of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.

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Classifications MeSH