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Is there a Beta-Peptide Equivalent of the Alpha-Helix?

MPS-Authors
/persons/resource/persons21325

Baldauf,  Carsten
Theory, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons22084

Schubert,  Franziska
Theory, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons32738

Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons22220

Warnke,  Stephan
Molecular Physics, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons21421

Rossi,  Mariana
Theory, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons21614

Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons21379

Blum,  Volker
Theory, Fritz Haber Institute, Max Planck Society;

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Citation

Baldauf, C., Schubert, F., Pagel, K., Warnke, S., Rossi, M., Salwiczek, M., et al. (2014). Is there a Beta-Peptide Equivalent of the Alpha-Helix?. Poster presented at Biophysical Society, 58th Annual Meeting, San Francisco, CA, USA. doi:10.1016/j.bpj.2013.11.3621.


Cite as: https://hdl.handle.net/11858/00-001M-0000-001A-2DDC-B
Abstract
In organic chemistry, the concept of homologation describes the extension of a carbon chain by one methylene unit. The application of this concept to peptides gives rise to the class of β-peptides that feature an additional -CH2- unit in the monomer backbone. The study of such non-natural peptides offers insight into general folding mechanisms. The similarities to α-peptide structure combined with stability against proteases makes such foldamers promising scaffolds with possible applications in drug design.