Cover Picture: Omniligase‐1: A Powerful Tool for Peptide Head‐to‐Tail Cyclization (Adv. Synth. Catal. 12/2017)

The inside cover picture, provided by Nuijens and co‐workers, illustrates the power and versatility of the peptide ligase omniligase‐1. This ligase provides a promising green and clean alternative to chemical approaches used for peptide cyclization, peptide fragment condensation and protein labellin...

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Bibliographic Details
Published in:Advanced synthesis & catalysis 2017-06, Vol.359 (12), p.2010-2010
Main Authors: Schmidt, Marcel, Toplak, Ana, Quaedflieg, Peter J. L. M., Ippel, Hans, Richelle, Gaston J. J., Hackeng, Tilman M., van Maarseveen, Jan H., Nuijens, Timo
Format: Article
Language:English
Subjects:
Catalysis
chemo-enzymatic peptide synthesis (CEPS)
Condensates
cyclic peptides
cyclization
cyclotide synthesis
cyclotides
enzyme catalysis
Fragmentation
head-to-tail cyclization
ligases
macrocycles
omniligase-1
Peptides
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Summary:The inside cover picture, provided by Nuijens and co‐workers, illustrates the power and versatility of the peptide ligase omniligase‐1. This ligase provides a promising green and clean alternative to chemical approaches used for peptide cyclization, peptide fragment condensation and protein labelling. The ligations are traceless, proceed with very high catalytic efficiency and result in high product yields. Details on omniligase‐mediated peptide cyclization can be found in the communication on pages 2050–2055 (M. Schmidt, A. Toplak, P. J. L. M. Quaedflieg, H. Ippel, G. J. J. Richelle, T. M. Hackeng, J. H. van Maarseveen, T. Nuijens, Adv. Synth. Catal. 2017, 359, 2050–2055; DOI: 10.1002/adsc.201700314).
ISSN:1615-4150
1615-4169
DOI:10.1002/adsc.201700590