Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers
The size distribution of domains in phase-separated lung surfactant monolayers influences monolayer viscoelasticity and compressibility which, in turn, influence monolayer collapse and set the compression at which the minimum surface tension is reached. The surfactant-specific protein SP-B decreases...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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Elsevier
2014
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| Online Access: | http://hdl.handle.net/1721.1/91631 |
| _version_ | 1811080675705487360 |
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| author | Dhar, Prajnaparamita Eck, Elizabeth Israelachvili, Jacob N. Lee, Dong Woog Min, Younjin Ramachandran, Arun Waring, Alan J. Zasadzinski, Joseph A. |
| author2 | Massachusetts Institute of Technology. Department of Chemical Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Chemical Engineering Dhar, Prajnaparamita Eck, Elizabeth Israelachvili, Jacob N. Lee, Dong Woog Min, Younjin Ramachandran, Arun Waring, Alan J. Zasadzinski, Joseph A. |
| author_sort | Dhar, Prajnaparamita |
| collection | MIT |
| description | The size distribution of domains in phase-separated lung surfactant monolayers influences monolayer viscoelasticity and compressibility which, in turn, influence monolayer collapse and set the compression at which the minimum surface tension is reached. The surfactant-specific protein SP-B decreases the mean domain size and polydispersity as shown by fluorescence microscopy. From the images, the line tension and dipole density difference are determined by comparing the measured size distributions with a theory derived by minimizing the free energy associated with the domain energy and mixing entropy. We find that SP-B increases the line tension, dipole density difference, and the compressibility modulus at surface pressures up to the squeeze-out pressure. The increase in line tension due to SP-B indicates the protein avoids domain boundaries due to its solubility in the more fluid regions of the film. |
| first_indexed | 2024-09-23T11:34:59Z |
| format | Article |
| id | mit-1721.1/91631 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:34:59Z |
| publishDate | 2014 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/916312022-09-27T20:28:34Z Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers Dhar, Prajnaparamita Eck, Elizabeth Israelachvili, Jacob N. Lee, Dong Woog Min, Younjin Ramachandran, Arun Waring, Alan J. Zasadzinski, Joseph A. Massachusetts Institute of Technology. Department of Chemical Engineering Min, Younjin The size distribution of domains in phase-separated lung surfactant monolayers influences monolayer viscoelasticity and compressibility which, in turn, influence monolayer collapse and set the compression at which the minimum surface tension is reached. The surfactant-specific protein SP-B decreases the mean domain size and polydispersity as shown by fluorescence microscopy. From the images, the line tension and dipole density difference are determined by comparing the measured size distributions with a theory derived by minimizing the free energy associated with the domain energy and mixing entropy. We find that SP-B increases the line tension, dipole density difference, and the compressibility modulus at surface pressures up to the squeeze-out pressure. The increase in line tension due to SP-B indicates the protein avoids domain boundaries due to its solubility in the more fluid regions of the film. National Institutes of Health (U.S.) (Grant GM-076709) 2014-11-20T13:37:37Z 2014-11-20T13:37:37Z 2012-01 2011-08 Article http://purl.org/eprint/type/JournalArticle 00063495 1542-0086 http://hdl.handle.net/1721.1/91631 Dhar, Prajnaparamita, Elizabeth Eck, Jacob N. Israelachvili, Dong Woog Lee, Younjin Min, Arun Ramachandran, Alan J. Waring, and Joseph A. Zasadzinski. “Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers.” Biophysical Journal 102, no. 1 (January 2012): 56–65. © 2012 Biophysical Society en_US http://dx.doi.org/10.1016/j.bpj.2011.11.4007 Biophysical Journal Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf Elsevier Elsevier |
| spellingShingle | Dhar, Prajnaparamita Eck, Elizabeth Israelachvili, Jacob N. Lee, Dong Woog Min, Younjin Ramachandran, Arun Waring, Alan J. Zasadzinski, Joseph A. Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers |
| title | Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers |
| title_full | Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers |
| title_fullStr | Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers |
| title_full_unstemmed | Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers |
| title_short | Lipid-Protein Interactions Alter Line Tensions and Domain Size Distributions in Lung Surfactant Monolayers |
| title_sort | lipid protein interactions alter line tensions and domain size distributions in lung surfactant monolayers |
| url | http://hdl.handle.net/1721.1/91631 |
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