Surfactant protein SP-B: one ring to rule the molecular and biophysical mechanisms of the pulmonary surfactant system
- PMID: 40376411
- PMCID: PMC12075752
- DOI: 10.1007/s12551-025-01285-y
Surfactant protein SP-B: one ring to rule the molecular and biophysical mechanisms of the pulmonary surfactant system
Abstract
Pulmonary surfactant is a lipid/protein complex crucial to maintain mammalian lungs open, as it facilitates breathing mechanics through a dramatic reduction of surface tension at the air-liquid interface. Intensive research during a few decades has identified many of the molecular actors defining the molecular and biophysical mechanisms of surfactant at the airspaces. Pulmonary surfactant protein SP-B has been undoubtedly identified as the most important and essential molecule to allow for air breathing in the mammalian lungs, as its absence is incompatible with life. We now know that SP-B directs the assembly of surfactant complexes into the lamellar bodies of type II pneumocytes, their secretion, adsorption, and reorganization at the interface as well as the homeostasis of the surfactant layer during different pathophysiological contexts. This review summarizes current models on SP-B structure and biophysical function, supporting how the activity of SP-B may be crucial for the design and production of a new generation of therapeutic products in respiratory medicine.
Keywords: Molecular and biophysical mechanisms; Pulmonary surfactant system; SP-B structure.
© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2025. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
Conflict of interest statement
Competing InterestsThe authors declare no competing interests.
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