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Demonstrates versatile synthesis of lysine homologs in functional biomaterials, indicating potential applications.
The Front Cover shows how a concise Hofmann-rearrangement route from protected asparagine and glutamine provides short-chain C1/C2 lysine homologs as versatile platforms for noncanonical amino acid synthesis. Donor, acceptor, fluorescent, and redox-active residues were introduced into peptide hydrogelators by solid-phase peptide synthesis, thereby enabling the synthesis of functional biomaterials with tunable self-assembly, fluorescence, and redox-responsive behavior. More information can be found in the Research Article by V. A. Azov and co-workers (DOI: 10.1002/ejoc.70413).
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Mashweu et al. (2026) studied this question.
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