Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/65306

Title1-aminoanthracene transduction into liposomes driven by odorant-binding protein proximity
Author(s)Gonçalves, Filipa Daniela Gomes
Silva, C.
Ribeiro, Artur
Cavaco-Paulo, Artur
Keywords(GQ)20 spacer
1-AMA transduction
1-aminoanthracene (1-AMA)
functionalized liposomes
odorant-binding protein
SP-DS3 anchor peptide
(GQ) spacer 20
Issue date24-Jul-2018
PublisherAmerican Chemical Society
JournalACS Applied Materials & Interfaces
CitationGonçalves, Filipa; Silva, Carla; Ribeiro, Artur; Cavaco-Paulo, Artur, 1-aminoanthracene transduction into liposomes driven by odorant-binding protein proximity. ACS Applied Materials & Interfaces, 10(32), 27531-27539, 2018
Abstract(s)In this work, the anchorage of pig odorant binding protein (OBP-I) into liposomal membrane was promoted by the fusion of OBP-I with the anchor SP-DS3 peptide and with the (GQ)20 spacer. The presence of the (GQ)20 spacer in the construct confers flexibility to the protein and increases the distance between the OBP binding site and the liposomal surface. The engineered proteins, OBP::SP-DS3 and OBP::(GQ)20::SP-DS3, were produced in Escherichia coli BL21(DE3) and characterized by circular dichroism spectroscopy and MALDI-TOF. The functionalization of liposomes with the OBP proteins was performed through ethanol injection, and similar liposomal anchorage (9297%) was found for both OBP constructs. The effect of OBPs proximity to the liposomes membrane on 1-aminoanthracene (1-AMA, model ligand) transduction was evaluated by measuring the amount of 1-AMA transduced into liposomes by fluorescence spectroscopy. While protein flexibility, given by the presence of the (GQ)20 spacer, seems to influence the binding efficiency, 45% for OBP::(GQ)20::SP-DS3 and 29% for OBP::SP-DS3, the distance between the proteins binding site and the liposomal membrane determines their ability to transduce the 1-AMA into the liposomes (23% for OBP::SP-DS3 and 19% for OBP::(GQ)20::SP-DS3). The anchorage capacity and proximity effect were confirmed by an experimental control where the wild-type (wt) OBP was added to the liposomes, resulting in low 1-AMA transduction (3.5%) and low binding to OBPwt (9%). These findings evidence the effect of anchorage, carrier proteins flexibility, and proximity as key features for the entrapment of molecules into the liposomal membrane. The developed OBP-based devices are thus promising anchorage systems for the capture and storage of odors with potential applications in textile and cosmetic industries.
TypeArticle
URIhttp://hdl.handle.net/1822/65306
DOI10.1021/acsami.8b10158
ISSN1944-8244
e-ISSN1944-8252
Publisher versionhttp://pubs.acs.org/journal/aamick
Peer-Reviewedyes
AccessRestricted access (UMinho)
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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