Supramolecular binding of cationic porphyrins on a filamentous bacteriophage template: toward a noncovalent antenna system.
Engineered viruses act as scaffolds to bind porphyrins on their surfaces, exploiting mainly electrostatic interactions. The close proximity between porphyrins and tryptophan residues, exposed on the solvent-accessible surface, leads to an efficient resonant energy transfer, which makes these systems suitable for developing noncovalent antenna systems.
Scolaro
Luigi Monsù
LM
Dipartimento di Chimica Inorganica, Chimica Analitica e Chimica Fisica, Università di Messina and C.I.R.C.M.S.B., Unità di Messina, Salita Sperone 31, 98166 Messina, Italy. lmonsu@unime.it
Castriciano
Maria Angela
MA
Romeo
Andrea
A
Micali
Norberto
N
Angelini
Nicola
N
Lo Passo
Carla
C
Felici
Franco
F
D000595:Amino Acid Sequence; D017104:Bacteriophage M13 / Q000737:chemistry; D001665:Binding Sites; D002412:Cations; D004268:DNA-Binding Proteins / Q000737:chemistry*; D017912:Inovirus / Q000737:chemistry*; D008969:Molecular Sequence Data; D011166:Porphyrins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013698:Templates, Genetic
D002412:Cations; D004268:DNA-Binding Proteins; D011166:Porphyrins