Heterochirality restricts the self-assembly of phenylalanine dipeptides capped with highly aromatic groups
The influence of stereochemistry on the self-assembly of phenylalanine (Phe) dipeptides bearing aromatic fluorenyl groups at both the N- and C-termini (Fmoc, OFm) has been investigated. For this purpose, Fmoc–d-Phe–l-Phe–OFm and Fmoc–l-Phe–l-Phe–OFm have been examined considering a wide variety of s...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2020 |
| País: | España |
| Institución: | Universitat Politècnica de Catalunya (UPC) |
| Repositorio: | UPCommons. Portal del coneixement obert de la UPC |
| Idioma: | inglés |
| OAI Identifier: | oai:upcommons.upc.edu:2117/335756 |
| Acceso en línea: | https://hdl.handle.net/2117/335756 https://dx.doi.org/10.1021/acs.jpcb.0c04513 |
| Access Level: | acceso abierto |
| Palabra clave: | Chemistry, Physical and theoretical Fisicoquímica Àrees temàtiques de la UPC::Enginyeria química |
| Sumario: | The influence of stereochemistry on the self-assembly of phenylalanine (Phe) dipeptides bearing aromatic fluorenyl groups at both the N- and C-termini (Fmoc, OFm) has been investigated. For this purpose, Fmoc–d-Phe–l-Phe–OFm and Fmoc–l-Phe–l-Phe–OFm have been examined considering a wide variety of solvents, which differ in dielectric constant and volatility. Results reveal that replacement of l-Phe by d-Phe has a major impact on the self-assembly propensities, restricting drastically the structural diversity and polymorphism shown by the homochiral dipeptide. Thus, the analogous heterochiral dipeptide shows a great propensity to form micro/nanofibers, independently of the environmental conditions. Theoretical calculations revealed that the stability of antiparallel disposition is much higher (a factor of ca. 15) for Fmoc–d-Phe–l-Phe–OFm than that for Fmoc–l-Phe–l-Phe–OFm, which has been attributed to the hydrophobic core formed in the former. Overall, results suggest that control of the backbone chirality is a potent and versatile strategy to drive and finely tune the self-assembly propensities of highly aromatic peptides. |
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