Molecular tweezers

[1] These molecular tweezers consist of a pair of anthracene arms held at a distance that allows aromatic guests to gain π–π interactions from both (see Figure).

[10] Water-soluble phosphate-substituted molecular tweezers made of alternating phenyl and norbornenyl substituents bind to positively charged aliphatic side chains of basic amino acids, such as lysine and arginine (Figure 3).

[13] These mutually exclusive binding modes make these compounds valuable tools for probing critical biological interactions of basic amino acid side chains in peptides and proteins as well as of NAD(P)+ and similar cofactors.

The molecular tweezers, but not the clips, efficiently inhibit the formation of toxic oligomers and aggregates by amyloidogenic proteins associated with different diseases.

They were also shown to destroy the membranes of enveloped viruses, such as HIV, herpes, and hepatitis C,[27] which makes them good candidates for development of microbicides.

Figure 1. Trinitrofluorene bound in molecular tweezers reported by Lehn and coworkers. [ 1 ]
Figure 2. A fullerene bound in a buckycatcher through aromatic stacking interactions . [ 2 ]
Figure 3. The aliphatic sidechain of lysine bound inside the cavity of the phosphate-substituted molecular benzene tweezer by electrostatic, CH-p and hydrophobic interactions reported by Klärner, Schrader, and coworkers. [9,10]
Figure 4. The double-sandwich host–guest complex of the phosphate-substituted molecular clip and nicotinamide adenine dinucleotide (NAD + , the cofactor of many redox enzymes). The nicotinamide ring (the active site of NAD + ) is bound between the clip naphthalene sidewalls, as reported by Klärner, Schrader, Ochsenfeld, and coworkers. [11]