We designed five new odorant binding proteins (OBP-I) to improve the internalization of odors into liposomes. OBP-I was fused with three cell-penetrating peptides (CPPs), namely Tat (OBP::Tat), pVEC (OBP::pVEC) and Pep-1 (OBP::Pep-1); and with SP-DS3 peptide (OBP::SP-DS3 and OBP::(GQ)20::SP-DS3). The proteins were expressed in Escherichia coli BL21(DE3) and characterized regarding their molecular weight, binding ability and secondary structure content. A new methodology using liposomes as reservoirs, OBPs as carriers and 1-aminoanthracene (1-AMA) as a model molecule was developed. The internalization efficiency revealed to be dependent on the initial capacity of OBPs to bind 1-AMA, on the penetration of liposomes promoted by the CPPs and on the anchoring promoted by SP-DS peptide. An encapsulation efficiency of 42% was obtained with OBP::Tat fusion protein while the binding of 1-AMA to functionalized liposomes revealed a maximal binding of 69% for liposomes containing OBP::(GQ)20::SP-DS3. Our approaches offer new liposomes-OBP conjugates with potentialities to mediate molecules capture for the surroundings for textile and cosmetic applications.

OBP fused with cell-penetrating and anchor peptides promotes liposomal transduction of 1-aminoanthracene

256th National Meeting (2018)

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