Polypeptide Oligomers Comprised of Corroles – Hydrogen Bonding Provides “Short-Circuit” Coupling Pathways for Electron Transfer

Abstract

Electron flow through proteins is a crucial factor, which decides about their multiple functions in living organisms. Incorporating polypeptides as bridges in donor-bridge-acceptor (DBA) conjugates allows for examining how various structural features in proteins affect the kinetics of the CT processes they mediate. Based on the premise that hydrogen-bonds formation could serve to modify geometry and special orientation of donor and acceptor scaffolds in covalently linked bichromophoric system we designed and synthesized series of dyads comprised of perylene-bisimide and free-base corrole. Specifically, the object of the study was hydrogen-bonded discrete assemblies of corroles possessing core-NH as hydrogen bond donor and amide groups located at position meso-10 as hydrogen bond acceptor. The three dyads differ in type and number of bridging aminoacids’ moieties: L-alanine and L-phenylalanine and one or four respectively. These complex corroles were prepared via synthesis of perylenebisimide-amino acid conjugate possessing free NH2 group followed by amidation of COOH-corrole. Combined steady-state and time-resolved photophysical studies identified that electron-transfer occurs in all four bichromophoric systems. Our focus was on alanine tetramer that is long enough not to mediate too efficiently through-bond CT. A corrole moiety serves as an electron donor, and a perylenediimide as an acceptor. The picosecond rates of electron transfer suggests that the electronic-coupling pathways cannot be through-bond and most likely involve through-hydrogen bond interaction.References Orłowski, R.; Vakuliuk, O.; Gullo, M. P.; Danylyuk, O.; Ventura, B.; Koszarna, B.; Tarnowska, A.; Jaworska, N.; Barbieri, A.; Gryko, D. T. Commun. 2015, 51, 8284-8287.Orłowski, R.; Cichowicz, G.; Staszewska-Krajewska, O.; Schilf, W.; Cyrański, M. K.; Gryko, D. T. Eur. J. 2019, 25, 9658-9664. Figure 1