Bibliographic Details
| Title: |
Peptide-bridged bis-porphyrin compounds: A photophysical and molecular dynamics study |
| Authors: |
Rita Cimino, Emanuela Gatto, Marta De Zotti, Fernando Formaggio, Claudio Toniolo, Micaela Giannetti, Antonio Palleschi, Carlos Serpa, Mariano Venanzi |
| Source: |
Journal of Photochemistry and Photobiology, Vol 16, Iss , Pp 100191- (2023) |
| Publisher Information: |
Elsevier, 2023. |
| Publication Year: |
2023 |
| Collection: |
LCC:Chemistry |
| Subject Terms: |
Bis-porphyrins, Exciton coupling, Peptide spacers, Singlet oxygen production, Time-resolved spectroscopy, Ultrafast transient absorption, Chemistry, QD1-999 |
| More Details: |
Covalently linked peptide-porphyrin compounds are most suitable systems for fundamental studies aiming to the comprehension of the mechanisms driving photoinduced energy/electron transfer processes. Mimicking photosynthetic units, the porphyrin groups act as antenna moieties while the peptide chain is the active medium through which energy and/or electron funneling occur. In this contribution we studied the transfer of excitation between two identical tetraphenylporphyrin groups connected by short peptide chains of different length formed by non-coded conformationally constrained α-amino acids, i.e., Cα-methylvaline. The photophysical events following porphyrin photoexcitation were characterized from the microsecond to the picosecond time region by time-resolved spectroscopy techniques. Ultrafast transient absorption measurements revealed the presence of a transient species that we assign to a self-trapped exciton migrating through the peptide chain. The exciton species propagates the electronic coupling between the two porphyrin groups giving rise to a characteristic bisignate band measured by circular dichroism experiments. Molecular dynamics simulations strongly suggest that the long lifetime (hundreds of picoseconds) of the exciton species is determined by the rigidity of the Cα-methylvaline residues, that inhibited energy relaxation pathways coupled to torsional motions of the peptide chain. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
2666-4690 |
| Relation: |
http://www.sciencedirect.com/science/article/pii/S2666469023000325; https://doaj.org/toc/2666-4690 |
| DOI: |
10.1016/j.jpap.2023.100191 |
| Access URL: |
https://doaj.org/article/2d5b3f1be43f42db8446e689ad601b69 |
| Accession Number: |
edsdoj.2d5b3f1be43f42db8446e689ad601b69 |
| Database: |
Directory of Open Access Journals |
