Prof. Beate Koksch

Free University of Berlin, Germany
Professor

Email: beate.koksch@fu-berlin.de

Qualifications

1995  PhD, Leipzig University, Biochemistry
1991 Chemistry, Leipzig University

1. E. Brandenburg, H.v. Berlepsch, B. Koksch, Specific in situ discrimination of amyloid fibrils versusα-helical fibres by the fluorophore NIAD-4. Mol Biosyst. 2012 Feb; 8(2):557-64.
2. M. Salwiczek, E. K. Nyakatura, U. I. M. Gerling, S. Ye, B. Koksch, Fluorinated amino acids: Compatibility with native protein structures and effects on protein-protein interactions. ChemSocRev 2012, DOI: 10.1039/c1cs15241f.
3. T. Vagt, M. Salwiczek, B. Koksch, Molecular interactions of fluorinated amino acids within the hydrophobic core of a coiled coil peptide: In V. Gouverneur, K. Müller (Eds.) Fluorine in pharmaceutical and medicinal chemistry: From biophysical aspects to clinical applications, Imperial College Press, 2012, in print.
4. R. Rezaei Araghi, C. Baldauf, U.I.M. Gerling, C. D. Cadicamo, B. Koksch, A systematic study of fundamentals in a-helical coiled coil mimicry by alternating sequences of b- und g-amino acids, Amino Acids 2011, 41, 733-742
5. E. Brandenburg, H. v. Berlepsch, U.I.M. Gerling, C. Böttcher, B. Koksch, Inhibition of Amyloid Aggregation by Formation of Helical Assemblies. Chemistry - A European Journal, 2011, 17(38), 10651–10661
6. U.I.M. Gerling, E. Brandenburg, H.v. Berlepsch, K. Pagel, B. Koksch, Structure Analysis of an Amyloid-Forming Model Peptide by a Systematic Glycine and Proline Scan. Biomacromolecules. 2011, 12(8), 2988-96
7. A. Kashiwada, M. Tsuboi, N.Takamura, E. Brandenburg, K. Matsuda, B. Koksch, Design and characterization of endosomal-pH-responsive coiled coil for constructing artificial membrane fusion system. Chemistry - A European Journal, 2011, 17, 6179 – 6186
8. R. Rezaei Araghi, B. Koksch, A helix-forming α-chimeric peptide with catalytic activity: a hybrid peptide ligase. B. Chem. Commun., 2011, 47, 3544-3546
9. J.A. Falenski, M. Broncel, S.C. Wagner, C. Hackenberger, B.Koksch. How Posttranslational modifications influence amyloid formation: A systematic study of phosphorylation and glycosylation in model peptides. Chem. Eur. J. 2010, 16(26), 7881-7888
10. S.C. Wagner, M. Roskamp, M. Pallerla, R.R. Araghi, S. Schlecht, B. Koksch. Nanoparticle-induced peptide folding and aggregation. Small, 2010, 6(12), 1321-1328
11. J.A. Falenski, U. Gerling, B. Koksch. Multiple glycosylation of de novo designed alpha-helical coiled coil peptides. Bioorg. Med. Chem. 2010, 18, 3703-3706
12. H.v. Berlepsch, E. Brandenburg, B. Koksch, C. Böttcher, Peptide adsorption to cyanine dye aggregrates revealed by cryro-transmission electron microscopy, Langmuir, 2010, 26, 11452-11460
13. M. Hoernke, B. Koksch, G. Brezesinski, Influence of the hydrophobic interface and transition metal ions on the conformation of amyloidogenic model peptides, Biophysical Chemistry, 2010, 150, 64-72
14. S. Ye, A. Berger, D. Petzold, O. Reimann, B. Matt, B. Koksch. Chemical aminoacylation of tRNAs with fluorinated amino acids for in vitro protein mutagenesis. Beilstein J Org Chem., 2010, 6, 40
15. M. Broncel, S.C. Wagner, C. Hackenberger, B. Koksch. Towards understanding secondary structure transitions: phosphorylation and metal coordination in model peptides. Org. Biomol. Chem., 2010, 8, 2575-2579
16. M. Broncel, S.C. Wagner, C. Hackenberger, B. Koksch, Ezymatically triggered amyloid formation: an approach for studying aggregation, Chem. Comm., 2010, 46, 3080-3082
17. P. Kupser, K. Pagel, J. Oomens, N. Polfer, B. Koksch, G. Meijer, G. von Helden, Amide-I and -II vibrations of the cyclic β-sheet model peptide gramicidin S in the gas phase, J. Am. Chem. Soc., 2010, 132, 2085-2093
18. T. Vagt, E. Nyakatura, C. Jäckel, B. Koksch, Approaches towards identifying preferred interaction partners of fluorinated amino acids within the hydrophobic environment of a dimeric coiled-coil peptide, Org. Biomol. Chem., 2010, 8, 1382-1386
19. R.R. Araghi, C. Jäckel, M. Salwiczek, S.C. Wagner, S. Wieczorek, C. Baldauf, B. Koksch, A β/γ motif to mimic α-helical turns in proteins ChemBioChem, 2010, 11, 335-339
20. Sergey A. Samsonov, M. Salwiczek, Gerd Anders, B. Koksch, M. T. Pisabarro, Fluorine in Protein Environments: A QM and MD Study, J. Phys. Chem. B, 2009, 113, 16400-16408
21. 60 M. Salwiczek, B. Koksch, Effects of fluorination on the folding kinetics of a heterodimeric coiled coil, ChemBioChem, 2009, 10, 2867-2870
22. J. Becaud, L. Mu, M. Karramkam, P.A. Schubiger, S.M. Ametamey, K. Graham, T. Stellfeld, L. Lehmann, S. Borkowski, D. Berndorff, L. Dinkelborg, A. Srinivasan, R. Smits, B. Koksch. Direct one-step 18F-labeling of peptides via nucleophilic aromatic substitution. Bioconjugate Chem., 2009, 20(12), 2254-2261
23. D. Maisch, P. Wadhwani, S. Afonin, C. Böttcher, B. Koksch, A.S. Ulrich, Chemical labeling strategy with (R)- and (S)-trifluoromethylalanie for solid state 19F-NMR analysis of peptaibols in membranes. J. Am. Chem. Soc., 2009, 131(43), 15596-15597
24. D.P. Weimann, H.D.F. Winkler, J.A. Falenski, B. Koksch, C.A. Schalley. Highly dynamic motion of crown ethers along oligolysine peptide chains. Nat. Chem., 2009, 1(7), 573-577
25. T. Vagt, C. Jaeckel, S. Samsonov, M. T. Pisabarro, B. Koksch, Selection of a buried salt bridge by phage display, Bioorg. Med. Chem. Let. 2009, 19, 3924-3927
26. K. Pagel, P. Kupser, F. Bierau, N. C. Polfer, J. D. Steill, J. Oomens, G. Meijer, B. Koksch, G. von Helden. Gas-phase IR spectra of intact a-helical coiled coil protein complexes, Int. J. Mass Spec. 2009, 283, 161-168

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Last Updated: August, 2012.

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