Synthesis and Charge-Transfer Dynamics in a Ferrocene-Containing Organoboryl aza-BODIPY Donor–Acceptor Triad with Boron as the Hub

A <i>N</i>,<i>N</i>′-bis­(ferroceneacetylene)­boryl complex of 3,3′-diphenylazadiisoindolylmethene was synthesized by the reaction of an <i>N</i>,<i>N</i>′-difluoroboryl complex of 3,3′-diphenylazadiisoindolylmethene and ferroceneacetylene magnesium bromide. The novel diiron complex was characterized by a variety of spectroscopic techniques, electrochemistry, and ultrafast time-resolved methods. Spectroscopy and redox behavior was correlated with the density functional theory (DFT) and time-dependent DFT calculations. An unexpected degree of coupling between the two Fc ligands was observed. Despite a lack of conjugation between the donor and acceptor, the complex undergoes very rapid (τ = 1.7 ± 0.1 ps) photoinduced intramolecular charge separation followed by subpicosecond charge recombination to form a triplet state with a lifetime of 4.8 ± 0.1 μs

Nitrodibenzofuran: A One- and Two-Photon Sensitive Protecting Group That Is Superior to Brominated Hydroxycoumarin for Thiol Caging in Peptides

Photoremovable protecting groups are important for a wide range of applications in peptide chemistry. Using Fmoc-Cys­(Bhc-MOM)-OH, peptides containing a Bhc-protected cysteine residue can be easily prepared. However, such protected thiols can undergo isomerization to a dead-end product (a 4-methylcoumarin-3-yl thioether) upon photolysis. To circumvent that photoisomerization problem, we explored the use of nitrodibenzofuran (NDBF) for thiol protection by preparing cysteine-containing peptides where the thiol is masked with an NDBF group. This was accomplished by synthesizing Fmoc-Cys­(NDBF)-OH and incorporating that residue into peptides by standard solid-phase peptide synthesis procedures. Irradiation with 365 nm light or two-photon excitation with 800 nm light resulted in efficient deprotection. To probe biological utility, thiol group uncaging was carried out using a peptide derived from the protein K-Ras4B to yield a sequence that is a known substrate for protein farnesyltransferase; irradiation of the NDBF-caged peptide in the presence of the enzyme resulted in the formation of the farnesylated product. Additionally, incubation of human ovarian carcinoma (SKOV3) cells with an NDBF-caged version of a farnesylated peptide followed by UV irradiation resulted in migration of the peptide from the cytosol/Golgi to the plasma membrane due to enzymatic palmitoylation. Overall, the high cleavage efficiency devoid of side reactions and significant two-photon cross-section of NDBF render it superior to Bhc for thiol group caging. This protecting group should be useful for a plethora of applications ranging from the development of light-activatable cysteine-containing peptides to the development of light-sensitive biomaterials