Structural and functional stability of the sulfur-free surfactant protein B peptide mimic B-YL in synthetic surfactant lipids.

ABSTRACT:

Background

Optimal functionality of synthetic lung surfactant for treatment of respiratory distress syndrome in preterm infants largely depends on the quality and quantity of the surfactant protein B (SP-B) peptide mimic and the lipid mixture. B-YL peptide is a 41-residue sulfur-free SP-B mimic with its cysteine and methionine residues replaced by tyrosine and leucine, respectively, to enhance its oxidation resistance.

Aim

Testing the structural and functional stability of the B-YL peptide in synthetic surfactant lipids after long-term storage.

Methods

The structural and functional properties of B-YL peptide in surfactant lipids were studied using three production runs of B-YL peptides in synthetic surfactant lipids. Each run was held at 5 °C ambient temperature for t

SUBMITTER: Walther FJ 

PROVIDER: S-EPMC8540162 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature