Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Synthesis of Coumarin/Pyrrole-Fused Heterocycles and Their Photochemical and Redox-Switching Properties

Two coumarin/pyrrole-fused heterocycles were synthesized to investigate their photochemical and redox-switching properties. Photooxidation of the colorless diphenyl-substituted pyrrolocoumarin resulted in a distinct change to red and a sharp decrease in fluorescence intensity. The photooxidized product can be swiftly reverted to the original form by NaCNBH₃ reduction or hydrogenation

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex-2

N between the two molecules. Different combinations are depicted by various curves as indicated and the dashed curve is derived from random distribution of = 60 Å donor-acceptor pair [36]. Higher FRET efficiency from experimental data for the labeled NBD-Rho pair than that from the theoretical computation at any given Rhodamine concentration suggests association between TMD and FP in the membrane bilayer.<p><b>Copyright information:</b></p><p>Taken from "Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex"</p><p>http://www.biomedcentral.com/1741-7007/6/2</p><p>BMC Biology 2008;6():2-2.</p><p>Published online 15 Jan 2008</p><p>PMCID:PMC2267159.</p><p></p

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex-6

Nd is assigned to hydrated hydrogen bonded lipid. It is seen that the percentage of dehydrated bands increases as the two peptides form a complex and FP has a higher dehydration level than TMD.<p><b>Copyright information:</b></p><p>Taken from "Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex"</p><p>http://www.biomedcentral.com/1741-7007/6/2</p><p>BMC Biology 2008;6():2-2.</p><p>Published online 15 Jan 2008</p><p>PMCID:PMC2267159.</p><p></p

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex-4

Nteracting with TMD can be rationalized by a better alignment of FP on complexing to TMD. The results also support the notion of FP-TMD interaction in the membrane.<p><b>Copyright information:</b></p><p>Taken from "Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex"</p><p>http://www.biomedcentral.com/1741-7007/6/2</p><p>BMC Biology 2008;6():2-2.</p><p>Published online 15 Jan 2008</p><p>PMCID:PMC2267159.</p><p></p