Synthesis of peptoids containing multiple Nhtrp and Ntrp residues: A comparative study of resin, cleavage cocktails and sub-monomer protection

Abdullah Lone, Håvard Jenssen, Paul Robert Hansen, Biljana Mojsoska*

*Corresponding author

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Peptoids hold status as peptide-mimetics with versatile biological applications due to their proteolytic stability and structural diversity. Among those that have been studied in different biological systems, are peptoids with dominant balanced hydrophobic and charge distribution along the backbone. Tryptophan is an important amino acid found in many biologically active peptides. Tryptophan-like side chains in peptoids allow H-bonding, which is absent from the parent backbone, due to the unique indole ring. Furthermore, the rigid hydrophobic core and flat aromatic system influence the positioning in the hydrocarbon core and allows accommodating tryptophan-like side chains into the interfacial regions of bacterial membranes and causing bacterial membrane damage. Incorporating multiple tryptophan-like side chains in peptoids can be tricky and there is a lack of suitable, synthetic routes established. In this paper, we investigate the synthesis of peptoids rich in Nhtrp and Ntrp residues using different resins, cleavage conditions, and unprotected as well as tert-butyloxycarbonyl-protected amines suitable for automated solid-phase submonomer peptoid synthesis protocols.
Original languageEnglish
Article number370
JournalFrontiers in Chemistry
Volume2020
Issue number8
ISSN2296-2646
DOIs
Publication statusPublished - 29 Apr 2020

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