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- Title
pH‐Controlled Reversible Folding of Copolymers via Formation of β‐sheet Secondary Structures.
- Authors
Sbordone, Federica; Micallef, Aaron; Frisch, Hendrik
- Abstract
Protein functions are enabled by their perfectly arranged 3D structure, which is the result of a hierarchical intramolecular folding process. Sequence‐defined polypeptide chains form locally ordered secondary structures (i.e., α‐helix and β‐sheet) through hydrogen bonding between the backbone amides, shaping the overall tertiary structure. To generate similarly complex macromolecular architectures based on synthetic materials, a plethora of strategies have been developed to induce and control the folding of synthetic polymers. However, the degree of complexity of the structure‐driving ensemble of interactions demonstrated by natural polymers is unreached, as synthesizing long sequence‐defined polymers with functional backbones remains a challenge. Herein, we report the synthesis of hybrid peptide‐N,N‐Dimethylacrylamide copolymers via radical Ring‐Opening Polymerization (rROP) of peptide containing macrocycles. The resulting synthetic polymers contain sequence‐defined regions of β‐sheet encoding amino acid sequences. Exploiting the pH responsiveness of the embedded sequences, protonation or deprotonation in water induces self‐assembly of the peptide strands at an intramacromolecular level, driving polymer chain folding via formation of β‐sheet secondary structures. We demonstrate that the folding behavior is sequence dependent and reversible.
- Subjects
BIOPOLYMERS; COPOLYMERS; AMINO acid sequence; RING-opening polymerization; TERTIARY structure; PEPTIDES; POLYMERS; BLOCK copolymers
- Publication
Angewandte Chemie, 2024, Vol 136, Issue 10, p1
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.202319839