Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles
The driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim o...
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| Published in | Molecules (Basel, Switzerland) Vol. 26; no. 12; p. 3607 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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| Abstract | The driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim of elucidating conformational changes promoting interaction with bilayers. From previous studies, it is known that A-Cage-C causes membrane leakages associated with the sporadic formation of amorphous aggregates on solid-supported bilayers. Here we express and purify double-labelled A-Cage-C and prepare partially deuterated bicelles as a membrane mimicking system. We investigate A-Cage-C in the presence and absence of these bicelles at non-binding (pH 7.0) and binding (pH 4.5) conditions. Using in silico analyses, NMR, conformational clustering, and Molecular Dynamics, we provide tentative insights into the conformations of bound and unbound A-Cage-C. The conformation of each state is dynamic and samples a large amount of overlapping conformational space. We identify one of the clusters as likely representing the binding conformation and conclude tentatively that the unfolding around the central W23 segment and its reorientation may be necessary for full intercalation at binding conditions (pH 4.5). We also see evidence for an overall elongation of A-Cage-C in the presence of model bilayers. |
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| AbstractList | The driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim of elucidating conformational changes promoting interaction with bilayers. From previous studies, it is known that A-Cage-C causes membrane leakages associated with the sporadic formation of amorphous aggregates on solid-supported bilayers. Here we express and purify double-labelled A-Cage-C and prepare partially deuterated bicelles as a membrane mimicking system. We investigate A-Cage-C in the presence and absence of these bicelles at non-binding (pH 7.0) and binding (pH 4.5) conditions. Using in silico analyses, NMR, conformational clustering, and Molecular Dynamics, we provide tentative insights into the conformations of bound and unbound A-Cage-C. The conformation of each state is dynamic and samples a large amount of overlapping conformational space. We identify one of the clusters as likely representing the binding conformation and conclude tentatively that the unfolding around the central W23 segment and its reorientation may be necessary for full intercalation at binding conditions (pH 4.5). We also see evidence for an overall elongation of A-Cage-C in the presence of model bilayers. The driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim of elucidating conformational changes promoting interaction with bilayers. From previous studies, it is known that A-Cage-C causes membrane leakages associated with the sporadic formation of amorphous aggregates on solid-supported bilayers. Here we express and purify double-labelled A-Cage-C and prepare partially deuterated bicelles as a membrane mimicking system. We investigate A-Cage-C in the presence and absence of these bicelles at non-binding (pH 7.0) and binding (pH 4.5) conditions. Using in silico analyses, NMR, conformational clustering, and Molecular Dynamics, we provide tentative insights into the conformations of bound and unbound A-Cage-C. The conformation of each state is dynamic and samples a large amount of overlapping conformational space. We identify one of the clusters as likely representing the binding conformation and conclude tentatively that the unfolding around the central W23 segment and its reorientation may be necessary for full intercalation at binding conditions (pH 4.5). We also see evidence for an overall elongation of A-Cage-C in the presence of model bilayers.The driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim of elucidating conformational changes promoting interaction with bilayers. From previous studies, it is known that A-Cage-C causes membrane leakages associated with the sporadic formation of amorphous aggregates on solid-supported bilayers. Here we express and purify double-labelled A-Cage-C and prepare partially deuterated bicelles as a membrane mimicking system. We investigate A-Cage-C in the presence and absence of these bicelles at non-binding (pH 7.0) and binding (pH 4.5) conditions. Using in silico analyses, NMR, conformational clustering, and Molecular Dynamics, we provide tentative insights into the conformations of bound and unbound A-Cage-C. The conformation of each state is dynamic and samples a large amount of overlapping conformational space. We identify one of the clusters as likely representing the binding conformation and conclude tentatively that the unfolding around the central W23 segment and its reorientation may be necessary for full intercalation at binding conditions (pH 4.5). We also see evidence for an overall elongation of A-Cage-C in the presence of model bilayers. |
| Author | Teigen, Knut Strømland, Øyvind Govasli, Morten L. Dobrovolska, Olena Handegård, Ørjan Sele Jakubec, Martin Halskau, Øyvind Skjevik, Åge Aleksander Frøystein, Nils Åge |
| AuthorAffiliation | 1 Department of Biological Sciences, University of Bergen, N-5020 Bergen, Norway; odo021@uib.no (O.D.); oyvind.stromland@uib.no (Ø.S.); orjan.handegard@gmail.com (Ø.S.H.); martin.jakubec@uit.no (M.J.); m.larsen@ucl.ac.uk (M.L.G.) 3 Division of Infection and Immunity, University College London, London WC1E 6BT, UK 4 Department of Chemistry, University of Bergen, N-5020 Bergen, Norway; nils.froystein@uib.no 2 Department of Biomedicine, University of Bergen, N-5020 Bergen, Norway; age.a.skjevik@gmail.com (Å.A.S.); knut.teigen@uib.no (K.T.) |
| AuthorAffiliation_xml | – name: 4 Department of Chemistry, University of Bergen, N-5020 Bergen, Norway; nils.froystein@uib.no – name: 1 Department of Biological Sciences, University of Bergen, N-5020 Bergen, Norway; odo021@uib.no (O.D.); oyvind.stromland@uib.no (Ø.S.); orjan.handegard@gmail.com (Ø.S.H.); martin.jakubec@uit.no (M.J.); m.larsen@ucl.ac.uk (M.L.G.) – name: 3 Division of Infection and Immunity, University College London, London WC1E 6BT, UK – name: 2 Department of Biomedicine, University of Bergen, N-5020 Bergen, Norway; age.a.skjevik@gmail.com (Å.A.S.); knut.teigen@uib.no (K.T.) |
| Author_xml | – sequence: 1 givenname: Olena surname: Dobrovolska fullname: Dobrovolska, Olena – sequence: 2 givenname: Øyvind surname: Strømland fullname: Strømland, Øyvind – sequence: 3 givenname: Ørjan Sele orcidid: 0000-0002-4618-2204 surname: Handegård fullname: Handegård, Ørjan Sele – sequence: 4 givenname: Martin surname: Jakubec fullname: Jakubec, Martin – sequence: 5 givenname: Morten L. surname: Govasli fullname: Govasli, Morten L. – sequence: 6 givenname: Åge Aleksander surname: Skjevik fullname: Skjevik, Åge Aleksander – sequence: 7 givenname: Nils Åge surname: Frøystein fullname: Frøystein, Nils Åge – sequence: 8 givenname: Knut orcidid: 0000-0002-7031-9215 surname: Teigen fullname: Teigen, Knut – sequence: 9 givenname: Øyvind orcidid: 0000-0003-2517-1060 surname: Halskau fullname: Halskau, Øyvind |
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| Title | Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles |
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