Characterization of protein-only nanoparticles containing antimicrobial peptides and analysis of their protection with liposomes and micelles

JAN ATIENZA GARRIGA; JOSE VICENTE CARRATALA; GENIS PÉREZ-COLLELL; RICARDO BALTÀ-FOIX; ADRIA LÓPEZCANO; JULIETA M. SANCHEZ; JOAQUÍN SERAS FRANZOSO; ANNA ARIS; ELENA GARCIA-FRUITÓS; NEUS FERRER MIRALLES

Santander

Conferencia; 3rd International Conference on Nanomaterials Applied to Life Sciences 2022; 2022

Universidad de Cantabria

Antimicrobial peptides (AMPs) are secreted key factors involved in the innate’s immuneresponse with potent efficacy against bacteria, fungi and viruses. The mechanism of action is relatedto the cationic and amphiphilic characteristics of the peptides which gain access to the negativelycharged surface of the infectious agents and desestabilising biological structures. Therefore, AMPsand formulations including AMPs have been investigated as a potential treatment against antibioticresistant bacteria [1].AMPs are small peptides that are difficult to produce recombinantly at large scale. One of thealternatives to overcome this limitation is the fusion of the peptides to a scaffold protein. Therefore,the resulting recombinant protein can be efficiently produced and purified. Besides, recombinantgene engineering allows the design of novel genes whose expression gives rise to proteins with theability to assemble into protein nanoparticles (NPs). It has been previously demonstrated that AMPsembedded in NP are stable and retain their biological activity [2]. However, protein stability can befurher improved. Thus, in this work, we have analysed the solubility pattern of AMPs fused to a Histagged eGFP at different pHs and we have studied the loading capacity of liposomes and micelleswith the aim to obtain novel formulations of AMP forming NPs with increase stability against proteaseactivity for further intranasal administration [3,4].