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90 Cell-Penetrating Peptides: Processes and Applications
The fluorescence intensity in each ROI was recorded as the mean of 30 scans with
a scan time of 2 sec with double averaging. The reflection mode was used to
determine the cell geometry and each different ∆Z n in the Z direction from the center
of ROI to the extracellular medium. Thereby the distances ∆Z n were obtained with
the knowledge of the dimension of cell, the Z position at the cell, and the positions
of ROIs at the focal plane by simple mathematical calculation. The values of the
fluorescence intensities of the ROIs and the distances of the ∆Z n values were stored
for later computation.
REFERENCES
1. Lindgren, M. et al., Cell-penetrating peptides, Trends Pharmacol. Sci., 21, 99, 2000.
2. Steiner, V. et al., Retention behaviour of a template-assembled synthetic protein and its
amphiphilic building blocks on reversed-phase columns, J. Chromatogr., 586, 43, 1991.
3. Rothemund, S. et al., Peptide destabilization by two adjacent D-amino acids in singlestranded
amphipathic alpha-helices, Pept. Res., 9, 79, 1996.
4. Rothemund, S. et al., Recognition of alpha-helical peptide structures using highperformance
liquid chromatographic retention data for D-amino acid analogues:
influence of peptide amphipathicity and of stationary phase hydrophobicity, J. Chromatogr.,
689, 219, 1995.
5. Krause, E. et al., Location of an amphipathic alpha-helix in peptides using reversedphase
HPLC retention behavior of D-amino acid analogs, Anal. Chem., 67, 252, 1995.
6. Dathe, M. et al., Hydrophobicity, hydrophobic moment and angle subtended by
charged residues modulate antibacterial and haemolytic activity of amphipathic helical
peptides, FEBS Lett., 403, 208, 1997.
7. Cross, L.J. et al., Influence of alpha-helicity, amphipathicity and D-amino acid incorporation
on the peptide-induced mast cell activation, Eur. J. Pharmacol., 291, 291,
1995.
8. Oehlke, J. et al., Nonendocytic, amphipathicity dependent cellular uptake of helical
model peptides, Protein Pept. Lett., 3, 393, 1996.
9. Derossi, D. et al., The third helix of the Antennapedia homeodomain translocates
through biological membranes, J. Biol. Chem., 269, 10444, 1994.
10. Oehlke, J. et al., Cellular uptake of an alpha-helical amphipathic model peptide with
the potential to deliver polar compounds into the cell interior non-endocytically,
Biochim. Biophys. Acta, 1414, 127, 1998.
11. Oehlke, J., Savoly, B., and Blasig, I.E., Utilization of endothelial cell monolayers of
low tightness for estimation of transcellular transport characteristics of hydrophilic
compounds, Eur. J. Pharm. Sci., 2, 365, 1994.
12. Guillot, F.L., Audus, K.L., and Raub, T.J., Fluid-phase endocytosis by primary cultures
of bovine brain microvessel endothelial cell monolayers, Microvasc. Res., 39,
1, 1990.
13. Prochiantz, A., Getting hydrophilic compounds into cells: lessons from homeopeptides,
Curr. Opin. Neurobiol., 6, 629, 1996.
14. Hawiger, J., Cellular import of functional peptides to block intracellular signaling,
Curr. Opin. Immunol., 9, 189, 1997.
15. Mellman, I., Endocytosis and molecular sorting, Annu. Rev. Cell Dev. Biol., 12, 575,
1996.