On-Resin Recognition of Aromatic Oligopeptides and Proteins through Host-Enhanced Heterodimerization


Type
Article
Change log
Authors
McCune, Jade 
Chen, xiaoyi 
Huang, Zehuan 
Sokolowski, kamil 
Abstract

Peptide dimerization is ubiquitous in natural protein conjugates and artificial self-assemblies. A major challenge in artificial systems remains achieving quantitative heterodimerization of peptides, critical for next-generation biomolecular purification and formulation of therapeutics. Here, we employ a synthetic host to simultaneously encapsulate an aromatic peptide and a non-canonical L-perfluorophenylalanine-containing peptide through embedded polar-π interactions, thus constructing an unprecedented series of heteropeptide dimers. To demonstrate the utility, this heteropeptide dimerization strategy was applied to achieve on-resin recognition of N-terminal aromatic residues in peptides as well as insulin, both exhibiting high recycling efficiency (> 95%). This research unveils a generic approach to exploit quantitative heteropeptide dimers for the design of supramolecular (bio)systems.

Description
Keywords
Dimerization, Oligopeptides, Peptides, Proteins
Journal Title
Journal of the American Chemical Society
Conference Name
Journal ISSN
0002-7863
1520-5126
Volume Title
144
Publisher
American Chemical Society
Sponsorship
European Commission Horizon 2020 (H2020) Marie Sk?odowska-Curie actions (845640)
EPSRC (2342310)
Engineering and Physical Sciences Research Council (EP/L027151/1)
European Research Council (726470)
Engineering and Physical Sciences Research Council (EP/R512461/1)