For the first time the ability of the first generation dendrimer belonging to the family of polyester-benzylether, (3,5)12G1-PE-BMPA-(OH)(4), to form dendrimersomes is presented together with their capability to reconstitute the integral membrane protein complex called Reaction Centre (RC) purified from the photosynthetic bacterium Rhodobacter sphaeroides. Size, polydispersity and time stability of the empty and protein containing dendrimersomes are presented together with the photochemical activity of the guest protein. The RC presence appears to strongly enhance the self-assembly properties of the Janus dendrimer, leading to the formation of proteo-dendrimersomes showing a photochemical activity similar to that found for RC in solution. The interaction of the embedded RC with reduced cyt-c has also been investigated, indicating that the incorporation of the protein is vectorial (almost 90% of the guest protein faces the dendrimerosomes exterior with its cyt-c docking site) at variance with lecithin liposomes where the reconstitution is essentially statistical. (C) 2012 Elsevier B.V. All rights reserved.

Incorporation of the bacterial reaction centre into dendrimersomes / Giustini, Mauro; Cristina, Bellinazzo; Galantini, Luciano; Antonia, Mallardi; Gerardo, Palazzo; Sennato, Simona; Bordi, Federico; Kari, Rissanen. - In: COLLOIDS AND SURFACES. A, PHYSICOCHEMICAL AND ENGINEERING ASPECTS. - ISSN 0927-7757. - STAMPA. - 413:(2012), pp. 38-43. (Intervento presentato al convegno 25th Meeting of the European-Colloid-and-Interface-Society (ECIS) tenutosi a Berlin, GERMANY nel SEP 04-09, 2011) [10.1016/j.colsurfa.2012.01.040].

Incorporation of the bacterial reaction centre into dendrimersomes

GIUSTINI, Mauro;GALANTINI, Luciano;SENNATO, Simona;BORDI, FEDERICO;
2012

Abstract

For the first time the ability of the first generation dendrimer belonging to the family of polyester-benzylether, (3,5)12G1-PE-BMPA-(OH)(4), to form dendrimersomes is presented together with their capability to reconstitute the integral membrane protein complex called Reaction Centre (RC) purified from the photosynthetic bacterium Rhodobacter sphaeroides. Size, polydispersity and time stability of the empty and protein containing dendrimersomes are presented together with the photochemical activity of the guest protein. The RC presence appears to strongly enhance the self-assembly properties of the Janus dendrimer, leading to the formation of proteo-dendrimersomes showing a photochemical activity similar to that found for RC in solution. The interaction of the embedded RC with reduced cyt-c has also been investigated, indicating that the incorporation of the protein is vectorial (almost 90% of the guest protein faces the dendrimerosomes exterior with its cyt-c docking site) at variance with lecithin liposomes where the reconstitution is essentially statistical. (C) 2012 Elsevier B.V. All rights reserved.
2012
charge recombination; dendrimersomes; dynamic light scattering; integral proteins; self-aggregation
01 Pubblicazione su rivista::01a Articolo in rivista
Incorporation of the bacterial reaction centre into dendrimersomes / Giustini, Mauro; Cristina, Bellinazzo; Galantini, Luciano; Antonia, Mallardi; Gerardo, Palazzo; Sennato, Simona; Bordi, Federico; Kari, Rissanen. - In: COLLOIDS AND SURFACES. A, PHYSICOCHEMICAL AND ENGINEERING ASPECTS. - ISSN 0927-7757. - STAMPA. - 413:(2012), pp. 38-43. (Intervento presentato al convegno 25th Meeting of the European-Colloid-and-Interface-Society (ECIS) tenutosi a Berlin, GERMANY nel SEP 04-09, 2011) [10.1016/j.colsurfa.2012.01.040].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/437980
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