Publicação
Self-Assembly and Crystal Structure of Boc-Protected Dipeptides Containing L-Phenylalanine and L-Tyrosine
| Resumo: | The self-assembly of a novel synthesized chiral dipeptide, Boc-p-nitro-L-phenylalanyl-tyrosine, into supramolecular structures is investigated by optical absorption and photoluminescence spectroscopy as well as single crystal X-ray diffraction. The compound is a diphenylalanine derivative belonging to a family of aromatic dipeptides that spontaneously self-organize into nanostructures through molecular recognition. The dipeptide exhibits several step-like peaks in its absorption band, indicative of self-assembly into quantum-confined nanostructures. In contrast, the parent Boc-p-nitro-L-phenylalanine amino acid lacks these features, indicating that the tyrosine residue favors quantum-confined self-assembly. Crystal structure determination reveals distinct packing styles: Boc-p-nitro-L-phenylalanine forms two-dimensional hydrogen-bonded layers, while the related p-nitro-free Boc-L-phenylalanyl-tyrosine dipeptide organizes into a 3D helical columnar architecture, driven by the additional hydrogen-bonding capacity of the peptide bond and tyrosine hydroxyl group, which favors the formation of a channel-type tetragonal architecture network over the planar sheets of the monomer. Furthermore, the introduction of a tyrosine residue into the Boc-p-nitro-L-phenylalanine molecule alters its supramolecular assembly, as the dipeptide Boc-p-nitro-L-phenylalanyl-tyrosine crystallizes as a monohydrate. The water molecule present in the structure acts as a bridge, participating in a hydrogen-bonding network between the tyrosine hydroxyl groups of neighboring columns through intermolecular interactions. |
|---|---|
| Autores principais: | Baptista, Rosa M. F. |
| Outros Autores: | Ayala, Alejandro P.; Gomes, Clara S. B.; Santos, Daniela; Belsley, Michael S.; Gomes, Etelvina de Matos |
| Assunto: | Dipeptides Optical properties Self-assembly Supramolecular structures X-ray single crystal structures General Materials Science Condensed Matter Physics |
| Ano: | 2026 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade Nova de Lisboa |
| Idioma: | inglês |
| Origem: | Repositório Institucional da UNL |
| Resumo: | The self-assembly of a novel synthesized chiral dipeptide, Boc-p-nitro-L-phenylalanyl-tyrosine, into supramolecular structures is investigated by optical absorption and photoluminescence spectroscopy as well as single crystal X-ray diffraction. The compound is a diphenylalanine derivative belonging to a family of aromatic dipeptides that spontaneously self-organize into nanostructures through molecular recognition. The dipeptide exhibits several step-like peaks in its absorption band, indicative of self-assembly into quantum-confined nanostructures. In contrast, the parent Boc-p-nitro-L-phenylalanine amino acid lacks these features, indicating that the tyrosine residue favors quantum-confined self-assembly. Crystal structure determination reveals distinct packing styles: Boc-p-nitro-L-phenylalanine forms two-dimensional hydrogen-bonded layers, while the related p-nitro-free Boc-L-phenylalanyl-tyrosine dipeptide organizes into a 3D helical columnar architecture, driven by the additional hydrogen-bonding capacity of the peptide bond and tyrosine hydroxyl group, which favors the formation of a channel-type tetragonal architecture network over the planar sheets of the monomer. Furthermore, the introduction of a tyrosine residue into the Boc-p-nitro-L-phenylalanine molecule alters its supramolecular assembly, as the dipeptide Boc-p-nitro-L-phenylalanyl-tyrosine crystallizes as a monohydrate. The water molecule present in the structure acts as a bridge, participating in a hydrogen-bonding network between the tyrosine hydroxyl groups of neighboring columns through intermolecular interactions. |
|---|