A small series of boron‐dipyrromethene (BODIPY) dyes, characterized by the presence of multibranched fluorinated residues, were designed and synthesized. The dyes differ in both the position (para‐perfluoroalkoxy‐substituted phenyl ring or boron functionalization) and number of magnetically equivalent fluorine atoms (27 or 54 fluorine atoms per molecule). Photophysical and crystallographic characterization of the synthesized BODIPYs was carried out to evaluate the effect of the presence of highly fluorinated moieties on the optical and morphological properties of such compounds.

Bromination is herein exploited to promote the emergence of elastic behavior in a short peptide—SDSYGAP—derived from resilin, a rubber‐like protein exerting its role in the jumping and flight systems of insects. Elastic and resilient hydrogels are obtained, which also show self‐healing behavior, thanks to the promoted non‐covalent interactions that limit deformations and contribute to the structural recovery of the peptide‐based hydrogel. In particular, halogen bonds may stabilize the β‐sheet organization working as non‐covalent cross‐links between nearby peptide strands. Importantly, the unmodified peptide (i.e., wild type) does not show such properties. Thus, SDSY(3,5‐Br)GAP is a novel minimalist peptide elastomer.

Halogenation, generally introduced on aromatic aminoacids, is becoming a key supramolecular tool in peptides. Herein, we report the crystal structures and DFT study of two bis-halogenated tyrosines showing the subtle...

Self-assembling peptides are of huge interest for biological, medical and nanotechnological applications. The enormous chemical variety that is available from the 20 amino acids offers potentially unlimited peptide sequences, but...

Supramolecular Chemistry In article number 2200807, Pierangelo Metrangolo and co‐workers report the emergence of elasticity in a short peptide sequence—SDSYGAP—derived from resilin, upon bromination of the tyrosine residue. Bromine‐mediated halogen bonds act as non‐covalent crosslinks between nearby peptide strands, favoring the formation of elastic hydrogels in which such crosslinking points limit deformations and contribute to structural recovery of the peptide‐network. Cover design by Prof. Umberto Tolino and Mr. Davide Formenti from the Department of Design of Politecnico di Milano, Italy.