Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable
Apolipoprotein B (apoB) is a nonexchangeable apolipoprotein. During lipoprotein assembly, it recruits phospholipids and triacylglycerols (TAG) into TAG-rich lipoprotein particles. It remains bound to secreted lipoproteins during lipid metabolism in plasma. The β1 region (residues 827–1880) of apoB h...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2009-07-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520307823 |
| _version_ | 1818381585646354432 |
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| author | Libo Wang Dale D.O. Martin Erin Genter Jianjun Wang Roger S. McLeod Donald M. Small |
| author_facet | Libo Wang Dale D.O. Martin Erin Genter Jianjun Wang Roger S. McLeod Donald M. Small |
| author_sort | Libo Wang |
| collection | DOAJ |
| description | Apolipoprotein B (apoB) is a nonexchangeable apolipoprotein. During lipoprotein assembly, it recruits phospholipids and triacylglycerols (TAG) into TAG-rich lipoprotein particles. It remains bound to secreted lipoproteins during lipid metabolism in plasma. The β1 region (residues 827–1880) of apoB has a high amphipathic β strand (AβS) content and is proposed to be one region anchoring apoB to lipoproteins. The AβS-rich region between apoB37 and apoB41 (residues 1694–1880) was cloned, expressed, and purified. The interfacial properties were studied at the triolein/water (TO/W) and air/water (A/W) interfaces. ApoB[37–41] is surface-active and adsorbs to the TO/W interface. After adsorption the unbound apoB[37–41] was removed from the aqueous phase. Adsorbed apoB[37–41] did not desorb and could not be forced off by increasing the surface pressure up to 23 mN/m. ApoB[37–41] adsorbed on the TO/W interface was completely elastic when compressed and expanded by ±13% of its area. On an A/W interface, the apoB[37–41] monolayer became solid when compressed to 4 mN/m pressure indicating extended β-sheet formation. It could be reversibly compressed and expanded between low pressure and its collapse pressure (35 mN/m). Our studies confirm that the AβS structure of apoB[37–41] is a lipid-binding motif that can irreversibly anchor apoB to lipoproteins. |
| first_indexed | 2024-12-14T02:36:55Z |
| format | Article |
| id | doaj.art-0b4faf0ffb52493288094db49aaefa35 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-14T02:36:55Z |
| publishDate | 2009-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-0b4faf0ffb52493288094db49aaefa352022-12-21T23:20:06ZengElsevierJournal of Lipid Research0022-22752009-07-0150713401352Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeableLibo Wang0Dale D.O. Martin1Erin Genter2Jianjun Wang3Roger S. McLeod4Donald M. Small5Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5; Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5; Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5; Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5; Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5; Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5; Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201Apolipoprotein B (apoB) is a nonexchangeable apolipoprotein. During lipoprotein assembly, it recruits phospholipids and triacylglycerols (TAG) into TAG-rich lipoprotein particles. It remains bound to secreted lipoproteins during lipid metabolism in plasma. The β1 region (residues 827–1880) of apoB has a high amphipathic β strand (AβS) content and is proposed to be one region anchoring apoB to lipoproteins. The AβS-rich region between apoB37 and apoB41 (residues 1694–1880) was cloned, expressed, and purified. The interfacial properties were studied at the triolein/water (TO/W) and air/water (A/W) interfaces. ApoB[37–41] is surface-active and adsorbs to the TO/W interface. After adsorption the unbound apoB[37–41] was removed from the aqueous phase. Adsorbed apoB[37–41] did not desorb and could not be forced off by increasing the surface pressure up to 23 mN/m. ApoB[37–41] adsorbed on the TO/W interface was completely elastic when compressed and expanded by ±13% of its area. On an A/W interface, the apoB[37–41] monolayer became solid when compressed to 4 mN/m pressure indicating extended β-sheet formation. It could be reversibly compressed and expanded between low pressure and its collapse pressure (35 mN/m). Our studies confirm that the AβS structure of apoB[37–41] is a lipid-binding motif that can irreversibly anchor apoB to lipoproteins.http://www.sciencedirect.com/science/article/pii/S0022227520307823adsorptionair/water interfaceamphipathic β sheet structureapoBcompressibilitydesorption |
| spellingShingle | Libo Wang Dale D.O. Martin Erin Genter Jianjun Wang Roger S. McLeod Donald M. Small Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable Journal of Lipid Research adsorption air/water interface amphipathic β sheet structure apoB compressibility desorption |
| title | Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable |
| title_full | Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable |
| title_fullStr | Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable |
| title_full_unstemmed | Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable |
| title_short | Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable |
| title_sort | surface study of apob1694 1880 a sequence that can anchor apob to lipoproteins and make it nonexchangeable |
| topic | adsorption air/water interface amphipathic β sheet structure apoB compressibility desorption |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520307823 |
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