Page - (000244) - in Biomedical Chemistry: Current Trends and Developments

peptides. Almost every CPP sequence involves positively charged amino acids. In fact, a chain of arginines form one of the most widely used CPPs (Myrberg, 2008). The membranolytic properties of a given CPP can also be governed by its secondary structure, specifically its helicity. It has been shown that peptides with an α-helical region can enter cells more efficiently. Table 3.1.2: Sequences of common CPPs. Name Sequence / (Refs) Origin TAT (48-60) GRKKRRQRRRPPQ (Frankel and Pabo, 1988; Green and Loewentein, 1988) Human immunodeficiency virus type 1 (HIV-1) TAT Penetratin RQIKIWFQNRRMKWKK (Derossi, 1994) Drosophila Antennapedia homeodomain MAP KLALKLALKALKAALKLAa (Oehlke, 1998) Amphipathic model peptide Transportan/ GWTLNS/ Galanin-Lys-mastoparan TP10 AGYLLGKINLKALAALAKKILa (Pooga, 1998; Soomets, 2000) VP22 NAKTRRHERRRKLAIER (Eliott & O’Hare, 1997) Herpes simplex virus Polyarginine Rn,a n = 8,9 (Futaki, 2001) Positively charged sequence MPG GALFLGFLGAAGSTMGAb (Morris, 1997) Hydrophobic domain from the fusion sequence of HIV gp41 and NLS of SV40 T-antigen Pep1 KETWWETWWTEWSQPKKKRKVb (Chaloin, 1998) NLS from Simian Virus 40 large T antigen and reverse transcriptase of HIV-1 pVEC LLIILRRRIRKQAHAHSKa (Säälik, 2004) VE-cadherin YTA2 YTAIAWVKAFIRKLRKa MMP cleavage site as seeding sequence