Nanoparticulate architecture of protein-based artificial viruses is supported by protein-DNA interactions

El pdf del artículo es la versión post-print.-- et al.Aim & Methods: We have produced two chimerical peptides of 10.2 kDa, each contain four biologically active domains, which act as building blocks of protein-based nonviral vehicles for gene therapy. In solution, these peptides tend to aggregate as amorphous clusters of more than 1000 nm, while the presence of DNA promotes their architectonic reorganization as mechanically stable nanometric spherical entities of approximately 80 nm that penetrate mammalian cells through arginine-glycine-aspartic acid cell-binding domains and promote significant transgene expression levels. Results & Conclusion: The structural analysis of the protein in these hybrid nanoparticles indicates a molecular conformation with predominance of α-helix and the absence of cross-molecular, β-sheet-supported protein interactions. The nanoscale organizing forces generated by DNA-protein interactions can then be observed as a potentially tunable, critical factor in the design of protein-only based artificial viruses for gene therapy. © 2011 Future Medicine Ltd.The authors appreciate the financial support received for the design and production of artificial viruses for gene therapy from MICINN (BIO2007-61194 and ACI2009-0919), AGAUR (2009SGR-108) and CIBER de Bioingenieria, Biomateriales y Nanomedicina (CIBER-BBN, Spain), an initiative funded by the VI National R+D+i Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. We also thank ANII, Ministerio de Educacion y Cultura, Uruguay, for financial support.Peer Reviewe