On the scope of the double Ugi multicomponent stapling to produce helical peptides.

Autor: Ricardo MG; Laboratory of Synthetic and Biomolecular Chemistry, Faculty of Chemistry, University of Havana, Zapata y G, Havana 10400, Cuba; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120 Halle (Saale), Germany., Vázquéz-Mena Y; Laboratory of Synthetic and Biomolecular Chemistry, Faculty of Chemistry, University of Havana, Zapata y G, Havana 10400, Cuba., Iglesias-Morales Y; Laboratory of Synthetic and Biomolecular Chemistry, Faculty of Chemistry, University of Havana, Zapata y G, Havana 10400, Cuba., Wessjohann LA; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120 Halle (Saale), Germany. Electronic address: wessjohann@ipb-halle.de., Rivera DG; Laboratory of Synthetic and Biomolecular Chemistry, Faculty of Chemistry, University of Havana, Zapata y G, Havana 10400, Cuba; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120 Halle (Saale), Germany. Electronic address: dgr@fq.uh.cu.
Jazyk: angličtina
Zdroj: Bioorganic chemistry [Bioorg Chem] 2021 Aug; Vol. 113, pp. 104987. Date of Electronic Publication: 2021 May 12.
DOI: 10.1016/j.bioorg.2021.104987
Abstrakt: The stabilization of helical structures by peptide stapling approaches is now a mature technology capable to provide a variety of biomedical applications. Recently, it was shown that multicomponent macrocyclization is not only an effective way to introduce conformational constraints but it also allows to incorporate additional functionalities to the staple moiety in a one-pot process. This work investigates the scope of the double Ugi multicomponent stapling approach in its capacity to produce helical peptides from unstructured sequences. For this, three different stapling combinations were implemented and the CD spectra of the cyclic peptides were measured to determine the effect of the multicomponent macrocyclization on the resulting secondary structure. A new insight into some structural factors influencing the helicity type and content is provided, along with new prospects on the utilization of this methodology to diversify the molecular tethers linking the amino acid side chains.
(Copyright © 2021 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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