Self-assembly of NrTP6 cell-penetrating lipo-peptide with variable number of lipid chains: Impact of phosphate ions on lipid association.

Hypothesis: Lipopeptides synthesized from the Nucleolar Targeting Peptide (NrTP6) with one, two or four dodecanoic fatty acid (FA) chains, display large head to tail volumes, which together with the number of lipid chains per molecule, impacts their self-assembly behavior. In phosphate buffer (PB), peptide to peptide interactions are triggered by the presence of phosphate ions that act as ionic crosslinkers, affecting the organization of the lipid assemblies.

Experimental: The NrTP6 lipopeptides were synthesized by the solid phase peptide synthesis technique.