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AHNAK C-Terminal Peptide Membrane Binding-Interactions between the Residues 5654-5673 of AHNAK and Phospholipid Monolayers and Bilayers.

Author(s): Yan X, Noël F, Marcotte I, DeWolf CE, Warschawski DE, Boisselier E

The dysferlin membrane repair complex contains a small complex, S100A10-annexin A2, which initiates membrane repair by recruiting the protein AHNAK to the membrane, where it interacts via binding sites in the C-terminal region. However, no molecular data ar...

Article GUID: 31825630

Interfacial Self-Assembly of Antimicrobial Peptide GL13K into Non-Fibril Crystalline β-Sheets.

Author(s): Youssef H, DeWolf CE

Langmuir. 2020 Jan 06;: Authors: Youssef H, DeWolf CE

Article GUID: 31880463

Energy Budget of Liquid Drop Impact at Maximum Spreading: Numerical Simulations and Experiments.

Author(s): Lee JB, Derome D, Dolatabadi A, Carmeliet J

Langmuir. 2016 Feb 09;32(5):1279-88 Authors: Lee JB, Derome D, Dolatabadi A, Carmeliet J

Article GUID: 26745364

Model Lung Surfactant Films: Why Composition Matters.

Author(s): Selladurai SL, Miclette Lamarche R, Schmidt R, DeWolf CE

Langmuir. 2016 Oct 18;32(41):10767-10775 Authors: Selladurai SL, Miclette Lamarche R, Schmidt R, DeWolf CE

Article GUID: 27641759

Microfluidic Assembly To Synthesize Dual Enzyme/Oxidation-Responsive Polyester-Based Nanoparticulates with Controlled Sizes for Drug Delivery.

Author(s): Hong SH, Patel T, Ip S, Garg S, Oh JK

Langmuir. 2018 03 13;34(10):3316-3325 Authors: Hong SH, Patel T, Ip S, Garg S, Oh JK

Article GUID: 29485889


Title:Model Lung Surfactant Films: Why Composition Matters.
Authors:Selladurai SLMiclette Lamarche RSchmidt RDeWolf CE
Link:https://www.ncbi.nlm.nih.gov/pubmed/27641759?dopt=Abstract
Category:Langmuir
PMID:27641759
Dept Affiliation: CNSR
1 Department of Chemistry and Biochemistry and Centre for NanoScience Research, Concordia University , 7141 Sherbrooke Street West, Montreal, Canada H4B 1R6.

Description:

Model Lung Surfactant Films: Why Composition Matters.

Langmuir. 2016 Oct 18;32(41):10767-10775

Authors: Selladurai SL, Miclette Lamarche R, Schmidt R, DeWolf CE

Abstract

Lung surfactant replacement therapies, Survanta and Infasurf, and two lipid-only systems both containing saturated and unsaturated phospholipids and one containing additional palmitic acid were used to study the impact of buffered saline on the surface activity, morphology, rheology, and structure of Langmuir monolayer model membranes. Isotherms and Brewster angle microscopy show that buffered saline subphases induce a film expansion, except when the cationic protein, SP-B, is present in sufficient quantities to already screen electrostatic repulsion, thus limiting the effect of changing pH and adding counterions. Grazing incidence X-ray diffraction results indicate an expansion not only of the liquid expanded phase but also an expansion of the lattice of the condensed phase. The film expansion corresponded in all cases with a significant reduction in the viscosity and elasticity of the films. The viscoelastic parameters are dominated by liquid expanded phase properties and do not appear to be dependent on the structure of the condensed phase domains in a phase separated film. The results highlight that the choice of subphase and film composition is important for meaningful interpretations of measurements using model systems.

PMID: 27641759 [PubMed]