Nature Nanotech. 8, 130–136 (2013)

Amyloid fibrils composed of human-derived peptides are known to enhance retroviral gene delivery. Now, Jan Münch et al. report the improved efficiency of fibril-induced retroviral gene transfer using a 12-amino-acid peptide, termed EF-C. It was identified during a study of the viral infection ability of peptide fragments isolated from the human immunodeficiency virus type 1 glycoprotein gp120. The EF-C peptide spontaneously self-assembles into fibrils in solution and these peptide fibrils interact with virions in seconds. Using low-speed centrifugation, Münch et al. show that the fibrils can bind, precipitate and concentrate virions. Microscopic analysis of fibril–virion complexes in the presence of cells, suggests that a stable interaction is formed between the positively charged fibrils and the negatively charged surfaces of viral and cell membranes. This electrostatic interaction probably improves the fusion of the fibrils and the biological species, resulting in the observed enhancement in virus infection. Compared with RetroNectin, a commonly used retroviral agent, EF-C is found to be as effective, but is simpler and quicker to use.