1078162-71-6Relevant articles and documents
A novel cell-penetrating peptide sequence derived by structural minimization of a snake toxin exhibits preferential nucleolar localization
Rádis-Baptista, Gandhi,De La Torre, Beatriz G.,Andreu, David
, p. 7041 - 7044 (2008)
Structural simplification of a 42-residue venom peptide by N-to-C-terminal splicing led to two sequences [YKQCHKKG-GXKKGSG, where X = nil (1) or 6-aminohexanoyl (2)], both efficiently uptaken by HeLa cells and, most interestingly, specifically localized at the nucleolus. Retro-2 was uptaken less efficiently, but a single (His → Ile) replacement recovered the translocation ability. None of the peptides were cytotoxic up to 100 μM. Enantio-1 did not translocate, suggesting that peptide uptake was receptor-mediated.