Cucurbituril‐Based Biomacromolecular Assemblies

Abstract

The construction of controlled biomacromolecular assemblies has become a thriving area of supramolecular chemistry. In this context, cucurbiturils (CBs), a class of macrocyclic receptors having robust skeletons, hydrophobic cavities, and carbonyl‐laced portals, have been drawn into the limelight because of their advantageous molecular recognition characteristics with a variety of biomacromolecules, including peptides, nucleic acids, and proteins. In this minireview, we focus on the impressive advances in CB‐based biomacromolecular assemblies, such as in biosensors and assays, the regulation of biochemical reactions, and the treatment of serious diseases. CB‐promoted subcellular bioimaging has also been demonstrated in different organelles. The case studies presented herein demonstrate the numerous applications, from fundamental research to translational applications, of diverse CB‐based supra/biomacromolecular architectures.

Quantitative Heterodimerization of Aromatic Peptides through Host-Enhanced Polar–π Interactions for On-Resin Recognition

“…[4,6] On account of high binding affinity and the wide scope of guests, cucurbit[n]uril (CB[n])-mediated host-guest complexes are ideal systems to bind peptides. [15][16][17][18][19][20] Urbach et al found that two FGG tripeptides can be complexed with CB [8] to form a peptide homodimer, exhibiting high binding strength (K ≈ 10 11 M -2 ). [15] This type of homodimer has been adopted as a versatile building block in the design and fabrication of supramolecular oligomers [21] and † These authors contributed equally to this work.…”

Quantitative Heterodimerization of Aromatic Peptides through Host-Enhanced Polar–π Interactions for On-Resin Recognition

“…[4,6] On account of high binding affinity and the wide scope of guests, cucurbit[n]uril (CB[n])-mediated host-guest complexes are ideal systems to bind peptides. [15][16][17][18][19][20] Urbach et al found that two FGG tripeptides can be complexed with CB [8] to form a peptide homodimer, exhibiting high binding strength (K ≈ 10 11 M -2 ). [15] This type of homodimer has been adopted as a versatile building block in the design and fabrication of supramolecular oligomers [21] and polymers, [22,23] supramolecular hydrogels, [24,25] and protein/peptide assemblies.…”

Selective Recognition of Amino Acids and Peptides by Small Supramolecular Receptors

“…Most thermodynamic studies show that the complexation process is enthalpy driven in great part due to the displacement of high energy water molecules from the cavity of the host [ 102 , 105 , 106 , 107 , 108 ]. This hydrophobic effect can be complemented by attractive ion-dipole interactions between the protonated amino group of the biomolecules and the carbonyl group of the cucurbituril ( Figure 7 ) [ 35 , 44 , 109 ]. In the case of the binding of aromatic amino acids by CB7, the process is also enthalpy driven with unfavorable negative entropy contributions.…”

“…These types of tripeptides show sub micromolar affinities towards CB8 and are also a plausible target for the detection of proteins by their N -terminal, seeing as, despite methionine being a common site of excision, large amino acids in the position next to Met can block the binding of the enzymes that catalyze this process, which distinguishes these N -terminal sequences from the excised ones [ 139 ]. Additionally, this functionality of the macrocycle can be used as a protection against excision of the N -terminal, for proteins presenting these sequences [ 109 ].…”