Table 1.

Properties of the peptides included in this study^a

Peptide	Sequence	No. of aa	Net chargeb	Hydrophobic ratio (%)b	Origin	Reference(s)
Penetratin	RQIKIWFQNRRMKWKK-amide	16	+7	37	Drosophila transcription factor Antennapedia	61
pVEC	LLIILRRRIRKQAHAHSL-amide	18	+7	50	Murine vascular endothelial cadherin	9, 40
R41	FILFILFILGGKHKHKHKHKHK-amide	22	+11	40	Designed peptide	Unpublished
R8	GPPRFPPRFPPRFPPRFPPRFP-amide	22	+5	22	Design based on sequence of PR-39	Unpublished
TP10	AGYLLGKINLKALAALAKKIL-amide	21	+4	61	Deletion analogue of transportan, a chimeric peptide	26, 38, 39
M918	MVTVLFRRLRIRRASGPPRVRV-amide	22	+7	45	Tumor suppressor protein p14ARF	62
YTA-4	Acetyl-IAWVKAFIRKLRKGPLG-amide	17	+5	52	Substrate of matrix metalloprotease 2	63
MAP	KLALKALKALKAALKLA-amide	17	+5	70	Designed model amphipathic peptide	9, 27
LL-37	LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES	37	+6	35	Human cathelicidin	64

^aAbbreviations: TP10, transportan-10; MAP, model amphipathic peptide; aa, amino acids.

^bAs predicted by using the Antimicrobial Peptide Database website (http://aps.unmc.edu/AP/main.html) (65).