scholarly journals Polymer Lung Surfactants

2018 ◽  
Vol 1 (3) ◽  
pp. 581-592
Author(s):  
Hyun Chang Kim ◽  
Madathilparambil V. Suresh ◽  
Vikas V. Singh ◽  
Davis Q. Arick ◽  
David A. Machado-Aranda ◽  
...  
Keyword(s):  
2009 ◽  
Vol 44 (12) ◽  
pp. 1157-1158 ◽  
Author(s):  
Wolfgang Bernhard ◽  
Christopher J. Pynn
Keyword(s):  

MedChemComm ◽  
2011 ◽  
Vol 2 (12) ◽  
pp. 1167 ◽  
Author(s):  
Adrian L. Schwan ◽  
Suneel P. Singh ◽  
Jason A. Davy ◽  
Alan J. Waring ◽  
Larry M. Gordon ◽  
...  
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2006 ◽  
Vol 63 (16) ◽  
pp. 1504-1521 ◽  
Author(s):  
Mandana Ghodrat
Keyword(s):  

2016 ◽  
Vol 1 (3) ◽  
pp. 1-21 ◽  
Author(s):  
Frans J. Walther ◽  
Larry M. Gordon ◽  
Alan J. Waring

Surfactant protein (SP)-B is a 79-residue polypeptide crucial for the biophysical and physiological function of endogenous lung surfactant. SP-B is a member of the saposin or saposin-like proteins (SAPLIP) family of proteins that share an overall three-dimensional folding pattern based on secondary structures and disulfide connectivity and exhibit a wide diversity of biological functions. Here, we review the synthesis, molecular biophysics and activity of synthetic analogs of saposin proteins designed to mimic those interactions of the parent proteins with lipids that enhance interfacial activity. Saposin proteins generally interact with target lipids as either monomers or multimers via well-defined amphipathic helices, flexible hinge domains, and insertion sequences. Based on the known 3D-structural motif for the saposin family, we show how bioengineering techniques may be used to develop minimal peptide constructs that maintain desirable structural properties and activities in biomedical applications. One important application is the molecular design, synthesis and activity of Saposin mimics based on the SP-B structure. Synthetic lung surfactants containing active SP-B analogs may be potentially useful in treating diseases of surfactant deficiency or dysfunction including the neonatal respiratory distress syndrome and acute lung injury/acute respiratory distress syndrome.


2013 ◽  
Vol 39 (4-5) ◽  
pp. 191-200 ◽  
Author(s):  
Karen W. Lu ◽  
H. William Taeusch ◽  
John A. Clements
Keyword(s):  

Author(s):  
M. L. Longo

Respiratory distress syndrome (RDS), a life threatening disorder, occurs if a lipid-protein complex which lines the airspaces of the lungs is compromised. Successful treatment of RDS has been reported with a vesicular dispersion containing dipalmitoylphosphatidylcholine (DPPC), egg phosphatidylglycerol (egg PG), palmitic acid and lung surfactant protein, SP-B. It has been hypothesized that amphipathic regions of SP-B are important in these synthetic lung surfactants as they serve as a point of insertion for the protein into the lipid bilayer. Therefore two amphipathic peptides, SP-B(l-25) and SP-B(49-66), were synthesized to use in reconstitution studies. The incorporation of SP-B(l-25) into lipid bilayer has been visualized using immunofluorescent tagging in a specially designed flow-chamber.


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