Table 1. Peptides used in this study.

ID	Sequence	MW	P(CPP)	P(eff)	P(membind)
α-factor	WHWLQLKPGQPMY	1.68	0.39	0.5	0.34
NLS	QPKKKRKV	1.49	1	0.06	0.13
NLS-α	PKKKRKVWHWLQLKPGQPMY	2.55	0.89	0.45	0.08
NLS-CE	WRFVWMNPKKKRKV	1.90	0.97	0.75	0.09
α-NLS-C	RLWHWLQLKPGQPMYWRQPKSKRKVRR	3.56	0.91	0.59	0
NLS-α-CE	FRKWRRKPKKKRKVWWRKVKRRWHWLQLKPGQPMY	4.80	0.97	0.77	0.1
chimera	KRRWRFVWMNPKKKRKVPPWPYLLWWHWLQLKPGQPMY	5.01	0.88	0.63	0.16
MPG	GALFLGFLGAAGSTMGAWSQPKKKRKV	2.81	1	0.33	0.03
Iztli-1	KFLNRFWHWLQLKPGQPMY	2.49	0.64	0.41	0.22
TAMRA-α-NLS-C	TAMRA-RLWHWLQLKPGQPMYWRQPKSKRKVRR	3.97	ND	ND	ND
TAMRA-α-NLS-C woRK	TAMRA-ELWHWLQLEPGQPMYWEQPESEEEVEE	3.83	ND	ND	ND
TAMRA-NLS-α-CE	FRKWRRKPKKKRKVWWRKVKRRWHWLQLKPGQPMY	5.21	ND	ND	ND
TAMRA-NLS-α-CE woRK	FEEWEEEPEEEEEVWWEEVEEEWHWLQLEPGQPMY	5.03	ND	ND	ND
TAMRA-chimera	KRRWRFVWMNPKKKRKVPPWPYLLWWHWLQLKPGQPMY	5.01	ND	ND	ND
TAMRA-chimera woRK	EEEWEFVWMNPEEEEEVPPWPYLLWWHWLQLEPGQPMY	5.01	ND	ND	ND

The name of the peptide (column titled ID), the peptide sequence (column Sequence), the molecular weight in kDa (column MW), the calculated probability to match CPP rules (P(CPP)), the calculated probability to match efficient CPP rules (P(eff)) and the probability to match transmembrane protein regions (P(membind)) are indicated for each peptide tested in this study. Only NLS-CE, NLS-α-CE, and chimera were optimized for efficient CPP activity (in bold) and only chimera was also partially optimized for high membrane-binding activity. Peptides modified at the N-terminus with the fluorescent dye TAMRA (5-(6)-Carboxytetramethylrhodamine) are shown in this table as well. The peptides denoted with the “woRK” postfix (without RK) substitute every Arginine and Lysine residues in the corresponding peptide for Glutamic acids. ND stands for Not Determined.