The diphenylalanine peptide FF (H2N-Phe-Phe-COOH) is a simple building-block that has been extensively studied for multiple purposes. Among the many possible mutations finalized to tailor specific functions and properties of FF-based materials, halogenation was marginally considered despite the huge changes it confers to molecular self-assembly. Here, we report a detailed study on the role of halogenation, specifically iodination, in the aggregation behavior of iodine-modified FF dipeptides. Single-crystal X-ray structures of mono-iodinated—F(I)F—and bis-iodinated—F(I)F(I)—diphenylalanine reveal that halogen atoms exert a key role in the packing features of these compounds. Specifically, halogen bonding provides additional stability to the dry interfaces formed by the aromatic rings, providing a contribution in the solid-state packing of these dipeptides. The structural evidence of halogen bonding as crucial noncovalent interaction confirms the great potential of halogenation as supramolecular tool for peptide-based systems.

Halogen bonding as a key interaction in the self-assembly of iodinated diphenylalanine peptides

Pizzi A.;Catalano L.;Dichiarante V.;Terraneo G.;Metrangolo P.
2020

Abstract

The diphenylalanine peptide FF (H2N-Phe-Phe-COOH) is a simple building-block that has been extensively studied for multiple purposes. Among the many possible mutations finalized to tailor specific functions and properties of FF-based materials, halogenation was marginally considered despite the huge changes it confers to molecular self-assembly. Here, we report a detailed study on the role of halogenation, specifically iodination, in the aggregation behavior of iodine-modified FF dipeptides. Single-crystal X-ray structures of mono-iodinated—F(I)F—and bis-iodinated—F(I)F(I)—diphenylalanine reveal that halogen atoms exert a key role in the packing features of these compounds. Specifically, halogen bonding provides additional stability to the dry interfaces formed by the aromatic rings, providing a contribution in the solid-state packing of these dipeptides. The structural evidence of halogen bonding as crucial noncovalent interaction confirms the great potential of halogenation as supramolecular tool for peptide-based systems.
diphenylalanine peptide
halogen bond
halogenated peptides
halogenation
iodination
single-crystal X-ray structure
structural studies
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11311/1156177
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