研究领域

Peptidic Materials and Therapeutics with Unnatural Building Blocks

Our research group specializes in the design, synthesis, characterization, and application of peptide model systems to a diverse range of current problems in biomedicine, biotechnology, and materials science. Peptides and proteins have numerous responsibilities in nature. They may be enzymes that perform chemical reactions in cells, structural components of, for example, spider silk, transport molecules, molecular motors, warehouses for the storage of important goods in organisms, not to mention their roles in defense and regulatory processes. Their overwhelming structural and functional diversity depends upon the physical and chemical properties of the amino acid building blocks that they are composed of. We attempt to systematically evaluate how mutations in the primary structure influence the stability of the diverse quarternary structures formed by α-helices and β-strands. In the former case, the α-helical coiled coil folding motif is studied, and, in the latter case,β-sheet containing amyloid structures are studied. Based on phenomenological rules that govern the behavior of these biologically relevant assemblies, a variety of peptide model systems have been rationally designed. By means of these, we have gained insight into aggregation processes, the complex interactions of nonnatural amino acids in the context of a protein environment, and development strategies for novel chimeric structures using building blocks with alternative backbone connectivities, to give just three examples.

近期论文

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Fluorine meets peptides Beate Koksch, Ulla Gerling-Driessen Fluorinated amino acids: Compatibility with native protein structures and effects on protein-protein interactions M. Salwiczek*, E.K. Nyakatura, U.I.M. Gerling, S. Ye, B. Koksch* Chem.Soc.Rev. 2012, 41 (6), 2135 - 2171 Inhibition of Amyloid Aggregation by Formation of Helical Assemblies Enrico Brandenburg Hans v. Berlepsch Ulla I.M. Gerling C. Böttcher, B. Koksch Chem. Eur. J., 2011, 17, 10650-10660 Following polypeptide folding and assembly with conformational switches K. Pagel, B. Koksch Curr. Opin. Chem. Biol., 2008, 12, 730-739 Synthetic Strategies to α-Trifluoro-methyl and α-difluoromethyl substituted α-Amino Acids R. Smits, C. D. Cadicamo, K. Burger, B. Koksch Chem. Soc. Rev., 2008, 37, 1455-1464 Estersubstitutionen in α-helicalen Coiled-Coil-Peptiden: Effekt der Eliminierung von Wasserstoffbrücken auf die Struktur von Proteinen J. Scheike, C. Baldauf, J. Spengler, R. Albericio, M. T. Pisabarro, B. Koksch Angew. Chem., 2007, 119, 7912-7916 Amide to ester substitution in coiled coils - The effect of H-bond elimination on protein structure formation J. Scheike, C. Baldauf, J. Spengler, R. Albericio, M. T. Pisabarro, B. Koksch Angew. Chem. Int. Ed., 2007, 46, 7766-7769 Fluorine in peptide design and protein engineering C. Jäckel and B. Koksch Eur. J. Org. Chem., 2005, 21, 4482-4503 From α-helix to β-sheet – a reversible metal ion induced peptide secondary structure switch K. Pagel, T. Kohajda, B. Koksch Org. Biomol. Chem., 2005, 3, 2500-2502