Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles
To establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface, we used X-ray diffuse scattering (XDS) to determine an order parameter of the lipid chains ( S xray ) and the bending modulus of the lipid bilayers ( K C ). Samples contained...
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| creator | Loney, Ryan W Brandner, Bret Dagan, Maayan P Smith, Paige N Roche, Megan Fritz, Jonathan R Hall, Stephen B Tristram-Nagle, Stephanie A |
| description | To establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface, we used X-ray diffuse scattering (XDS) to determine an order parameter of the lipid chains (
S
xray
) and the bending modulus of the lipid bilayers (
K
C
). Samples contained different amounts of the proteins with two sets of lipids. Dioleoylphosphatidylcholine (DOPC) provided a simple, well characterized model system. The nonpolar and phospholipids (N&PL) from extracted calf surfactant provided the biological mix of lipids. For both systems, the proteins produced changes in
S
xray
that correlated well with
K
C
. The dose-response to the proteins, however, differed. Small amounts of protein generated large decreases in
S
xray
and
K
C
for DOPC that progressed monotonically. The changes for the surfactant lipids were erratic. Our studies then tested whether the proteins produced correlated effects on adsorption. Experiments measured the initial fall in surface tension during adsorption to a constant surface area, and then expansion of the interface during adsorption at a constant surface tension of 40 mN m
−1
. The proteins produced a sigmoidal increase in the rate of adsorption at 40 mN m
−1
for both lipids. The results correlated poorly with the changes in
S
xray
and
K
C
in both cases. Disordering of the lipid chains produced by the proteins, and the softening of the bilayers, fail to explain how the proteins promote adsorption of lipid vesicles.
We used X-ray diffuse scattering to determine the bending modulus of lipid bilayers and an order parameter of the acyl chains to establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface. |
| doi_str_mv | 10.1039/d0sm02223c |
| format | Article |
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S
xray
) and the bending modulus of the lipid bilayers (
K
C
). Samples contained different amounts of the proteins with two sets of lipids. Dioleoylphosphatidylcholine (DOPC) provided a simple, well characterized model system. The nonpolar and phospholipids (N&PL) from extracted calf surfactant provided the biological mix of lipids. For both systems, the proteins produced changes in
S
xray
that correlated well with
K
C
. The dose-response to the proteins, however, differed. Small amounts of protein generated large decreases in
S
xray
and
K
C
for DOPC that progressed monotonically. The changes for the surfactant lipids were erratic. Our studies then tested whether the proteins produced correlated effects on adsorption. Experiments measured the initial fall in surface tension during adsorption to a constant surface area, and then expansion of the interface during adsorption at a constant surface tension of 40 mN m
−1
. The proteins produced a sigmoidal increase in the rate of adsorption at 40 mN m
−1
for both lipids. The results correlated poorly with the changes in
S
xray
and
K
C
in both cases. Disordering of the lipid chains produced by the proteins, and the softening of the bilayers, fail to explain how the proteins promote adsorption of lipid vesicles.
We used X-ray diffuse scattering to determine the bending modulus of lipid bilayers and an order parameter of the acyl chains to establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface.</description><identifier>ISSN: 1744-683X</identifier><identifier>EISSN: 1744-6848</identifier><identifier>DOI: 10.1039/d0sm02223c</identifier><identifier>PMID: 33630985</identifier><language>eng</language><publisher>CAMBRIDGE: Royal Soc Chemistry</publisher><subject>Adsorption ; Bending modulus ; Chains ; Chemistry ; Chemistry, Physical ; Correlation analysis ; Dosage ; Elasticity ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Lipid bilayers ; Lipids ; Materials Science ; Materials Science, Multidisciplinary ; Membrane elasticity ; Order parameters ; Phospholipids ; Physical Sciences ; Physics ; Physics, Multidisciplinary ; Polymer Science ; Proteins ; Pulmonary Surfactants ; Science & Technology ; Surface chemistry ; Surface tension ; Surface-Active Agents ; Surfactants ; Technology ; Vesicles</subject><ispartof>Soft matter, 2021-03, Vol.17 (12), p.3358-3366</ispartof><rights>Copyright Royal Society of Chemistry 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>2</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000635764600007</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c465t-2a5a42edf2d6ebc2da47fcbcd1320126ff0dbe50215b1cbc602e0c55c131cc863</citedby><cites>FETCH-LOGICAL-c465t-2a5a42edf2d6ebc2da47fcbcd1320126ff0dbe50215b1cbc602e0c55c131cc863</cites><orcidid>0000-0002-7278-0304 ; 0000-0003-4608-8928 ; 0000-0002-6009-100X ; 0000-0001-8870-2143 ; 0000-0003-2271-7056</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,782,786,887,27931,27932,39265</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33630985$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Loney, Ryan W</creatorcontrib><creatorcontrib>Brandner, Bret</creatorcontrib><creatorcontrib>Dagan, Maayan P</creatorcontrib><creatorcontrib>Smith, Paige N</creatorcontrib><creatorcontrib>Roche, Megan</creatorcontrib><creatorcontrib>Fritz, Jonathan R</creatorcontrib><creatorcontrib>Hall, Stephen B</creatorcontrib><creatorcontrib>Tristram-Nagle, Stephanie A</creatorcontrib><title>Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles</title><title>Soft matter</title><addtitle>SOFT MATTER</addtitle><addtitle>Soft Matter</addtitle><description>To establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface, we used X-ray diffuse scattering (XDS) to determine an order parameter of the lipid chains (
S
xray
) and the bending modulus of the lipid bilayers (
K
C
). Samples contained different amounts of the proteins with two sets of lipids. Dioleoylphosphatidylcholine (DOPC) provided a simple, well characterized model system. The nonpolar and phospholipids (N&PL) from extracted calf surfactant provided the biological mix of lipids. For both systems, the proteins produced changes in
S
xray
that correlated well with
K
C
. The dose-response to the proteins, however, differed. Small amounts of protein generated large decreases in
S
xray
and
K
C
for DOPC that progressed monotonically. The changes for the surfactant lipids were erratic. Our studies then tested whether the proteins produced correlated effects on adsorption. Experiments measured the initial fall in surface tension during adsorption to a constant surface area, and then expansion of the interface during adsorption at a constant surface tension of 40 mN m
−1
. The proteins produced a sigmoidal increase in the rate of adsorption at 40 mN m
−1
for both lipids. The results correlated poorly with the changes in
S
xray
and
K
C
in both cases. Disordering of the lipid chains produced by the proteins, and the softening of the bilayers, fail to explain how the proteins promote adsorption of lipid vesicles.
We used X-ray diffuse scattering to determine the bending modulus of lipid bilayers and an order parameter of the acyl chains to establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface.</description><subject>Adsorption</subject><subject>Bending modulus</subject><subject>Chains</subject><subject>Chemistry</subject><subject>Chemistry, Physical</subject><subject>Correlation analysis</subject><subject>Dosage</subject><subject>Elasticity</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Lipid bilayers</subject><subject>Lipids</subject><subject>Materials Science</subject><subject>Materials Science, Multidisciplinary</subject><subject>Membrane elasticity</subject><subject>Order parameters</subject><subject>Phospholipids</subject><subject>Physical Sciences</subject><subject>Physics</subject><subject>Physics, Multidisciplinary</subject><subject>Polymer Science</subject><subject>Proteins</subject><subject>Pulmonary Surfactants</subject><subject>Science & Technology</subject><subject>Surface chemistry</subject><subject>Surface tension</subject><subject>Surface-Active Agents</subject><subject>Surfactants</subject><subject>Technology</subject><subject>Vesicles</subject><issn>1744-683X</issn><issn>1744-6848</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>EIF</sourceid><recordid>eNqNkktv1TAQhSMEoqWwYQ-yxAaBLvgVJ3eDhNLykIpYABK7yBlPGleJHWynVVb8dXy55fJYsfLI_s7ozBwXxUNGXzAqti8NjRPlnAu4VRyzSsqNqmV9-1CLr0fFvRgvKRW1ZOpucSSEEnRbl8fF92bQ7gIjsY5MOHVBOyQ46pgs2LQS0EtEQ7qVpAHJsJrg58F3FkhcQq8haZfIHHxC6yIBH0IWJySz92FcybVNA9Em-jAn6x3xPRntbA25wmhhxHi_uNPrMeKDm_Ok-PLm7HPzbnP-8e375vX5BqQq04brUkuOpudGYQfcaFn10IFhglPGVd9T02FJOSs7lu8V5UihLIEJBlArcVK82vedl25CA-hS0GM7BzvpsLZe2_bvF2eH9sJftTVlquK7Bk9vGgT_bcGY2slGwHHMC_NLbLncSr7Ny2YZffIPeumX4PJ4LS9pJbNjVmfq2Z6C4GMM2B_MMNrucm1P6acPP3NtMvz4T_sH9FeQGaj3wDV2vo9g0QEeMEqpEmWlpMoVrRqb9C6Oxi8uZenz_5dm-tGeDhEO0O8fKH4AOkXM7A</recordid><startdate>20210328</startdate><enddate>20210328</enddate><creator>Loney, Ryan W</creator><creator>Brandner, Bret</creator><creator>Dagan, Maayan P</creator><creator>Smith, Paige N</creator><creator>Roche, Megan</creator><creator>Fritz, Jonathan R</creator><creator>Hall, Stephen B</creator><creator>Tristram-Nagle, Stephanie A</creator><general>Royal Soc Chemistry</general><general>Royal Society of Chemistry</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7278-0304</orcidid><orcidid>https://orcid.org/0000-0003-4608-8928</orcidid><orcidid>https://orcid.org/0000-0002-6009-100X</orcidid><orcidid>https://orcid.org/0000-0001-8870-2143</orcidid><orcidid>https://orcid.org/0000-0003-2271-7056</orcidid></search><sort><creationdate>20210328</creationdate><title>Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles</title><author>Loney, Ryan W ; 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S
xray
) and the bending modulus of the lipid bilayers (
K
C
). Samples contained different amounts of the proteins with two sets of lipids. Dioleoylphosphatidylcholine (DOPC) provided a simple, well characterized model system. The nonpolar and phospholipids (N&PL) from extracted calf surfactant provided the biological mix of lipids. For both systems, the proteins produced changes in
S
xray
that correlated well with
K
C
. The dose-response to the proteins, however, differed. Small amounts of protein generated large decreases in
S
xray
and
K
C
for DOPC that progressed monotonically. The changes for the surfactant lipids were erratic. Our studies then tested whether the proteins produced correlated effects on adsorption. Experiments measured the initial fall in surface tension during adsorption to a constant surface area, and then expansion of the interface during adsorption at a constant surface tension of 40 mN m
−1
. The proteins produced a sigmoidal increase in the rate of adsorption at 40 mN m
−1
for both lipids. The results correlated poorly with the changes in
S
xray
and
K
C
in both cases. Disordering of the lipid chains produced by the proteins, and the softening of the bilayers, fail to explain how the proteins promote adsorption of lipid vesicles.
We used X-ray diffuse scattering to determine the bending modulus of lipid bilayers and an order parameter of the acyl chains to establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface.</abstract><cop>CAMBRIDGE</cop><pub>Royal Soc Chemistry</pub><pmid>33630985</pmid><doi>10.1039/d0sm02223c</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-7278-0304</orcidid><orcidid>https://orcid.org/0000-0003-4608-8928</orcidid><orcidid>https://orcid.org/0000-0002-6009-100X</orcidid><orcidid>https://orcid.org/0000-0001-8870-2143</orcidid><orcidid>https://orcid.org/0000-0003-2271-7056</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Web of Science - Science Citation Index Expanded - 2021<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; Alma/SFX Local Collection |
| subjects | Adsorption Bending modulus Chains Chemistry Chemistry, Physical Correlation analysis Dosage Elasticity Hydrophobic and Hydrophilic Interactions Hydrophobicity Lipid bilayers Lipids Materials Science Materials Science, Multidisciplinary Membrane elasticity Order parameters Phospholipids Physical Sciences Physics Physics, Multidisciplinary Polymer Science Proteins Pulmonary Surfactants Science & Technology Surface chemistry Surface tension Surface-Active Agents Surfactants Technology Vesicles |
| title | Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles |
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