Synthetic Voltage-dependent Ion Channels and Naturally Occurring Transmembrane Transporters

Synthetic, alpha-helical peptides can be modelled in their structure, in such a manner that ion channels with the characteristics of the acetyl-choline receptor channel can be induced experimentally in lipid bilayers. The biophysical determination of the properties of these ion channel forming peptides provides insight into the function of helix/helix interactions in transmembrane proteins as well as into the mechanisms of signal transduction. The mobility of the backbone and the sidechains of these helices is studied by time-resolved fluorescence spectroscopy and by molecular dynamic simulations.

Publications:

1. H. Schmitt and G. Jung (1985).
Total Synthesis of the a-Helical Eicosapeptide Antibiotic Alamethicin, Liebigs Ann. Chem. 1985, 321-344.

2. R. Bosch, H. Schmitt, G. Jung, and W. Winter (1985).
Crystal Structure of the alpha-Helical Undecapeptide Boc-L-Ala-Aib-Ala-Aib-Ala-Glu(OBzl)-Ala-Aib-Ala-Aib-Ala-OMe, Biopolymers 24, 961-979.

3. G. Menestrina, K.-P. Voges, G. Jung, and G. Boheim (1986).
Voltage-Dependent Channel Formation by Rods of Helical Polypeptides, J. Membrane Biol. 93, 111-132.

4. K.-P. Voges, G. Jung, and W. H. Sawyer (1987).
Depth-Dependent Fluorescence Quenching of a Tryptophan Residue Located at Defined Positions on a Rigid 21-Peptide Helix in Liposomes, Biochim. Biophys. Acta 896, 64-76.

5. H. Vogel, L. Nilsson, R. Rigler, K.-P. Voges, and G. Jung (1988).
Structural Fluctuations of a Helical Polypeptide Traversing a Lipid Bilayer, Proc. Natl. Acad. Sci. USA 85, 5067-5071.

6. H. Vogel, L. Nilsson, R. Rigler, S. Meder, G. Boheim, W. Beck, H.-H. Kurth, and G. Jung (1993).
Structural Fluctuations Between Two Conformational States of a Transmembrane Helical Peptide Are Related to its Channel-Forming Properties in Planar Lipid Membranes, Eur. J. Biochem. 212, 305-313.

7. W. Beck, I. Benz, W. Bessler, G. Jung, and M. Kohlhardt (1993).
Responsiveness of Cardiac Na⁺ Channels to a Site-Directed Antiserum Against the Cytotoxic Linker Between Domains III and IV and Their Sensitivity to Other Modifying Agents, J. Membrane Biol. 134, 231-239.

8. W. Beck, G. Jung, W. G. Bessler, I. Benz, and M. Kohlhardt (1994).
Conformational Mapping of the Cytosolic Linker Between Domains III and IV of the Cardiac Na⁺ Channel Protein and Binding Studies with a Site-Directed Channel Modifying Antibody, Biochim. Biophys. Acta 1206, 263-271.

9. H. Killmann, G. Videnov, G. Jung, H. Schwarz, and V. Braun (1995).
Identification of Receptor Binding Sites by Competing Peptide Mapping: Phages T1, T5, and O/ 80 and Colicin M Bind to the Gating Loop of FhuA, J. Bacteriol. 177, 694-698.

10. S. Uebel, T.H. Meyer, W. Kraas, S. Kienle, G. Jung, K.-H. Wiesmüller and R. Tampe (1995).
Requirements for Peptide Binding to the Human Transporter Associated with Antigen Processing Revealed by Peptide Scans and Complex Peptide Libraries, J. Biol. Chem. 31, 19512-18516.

11. I. Benz, W. Beck, W. Kraas, D. Stoll, G. Jung, and M. Kohlhardt (1997)
Two Types of Modified Cardiac Na⁺ Channels after Cytosolic Interventions at the alpha-Submit Capable of Removing Na⁺ Inactivation, Eur. Biophys. J. 25, 189-220.

cojinfo@uni-tuebingen.de(cojinfo@uni-tuebingen.de) - July 23, 1997