Cyclodextrins (CDs) are cyclic oligomers of α-1,4-linked D-glucopyranose. Due to their unique structure, marked by a chiral and hydrophobic cavity, CDs have been extensively used as chiral selectors and drug delivery systems. The functionalization both improve the CD applications and widen their use in many other fields, such as molecular recognition and enzyme mimicking. Moreover, the functionalization highly increases the metal binding properties of the CDs. This critical review is a report of recent applications concerning the CD derivatives and their metal complexes. The metal ion assists the host–guest interaction often increasing the properties of CDs to act as chiral receptors. Furthermore, it can act as a catalytic center in the mimicking of metalloenzymes based on functionalized CDs (164 references).

Although organic compounds account for more than 99% of currently approved clinical drugs, the established clinical use of cisplatin in cancer or auranofin in rheumatoid arthritis have paved the way to several research initiatives to identify metal-based drugs for a wide range of human diseases. Nitrogen and sulfur donor ligands, characterized by different binding motifs, have been the subject in recent years of one of the main research areas in coordination chemistry. Among the nitrogen/sulfur compounds, very little is known about thiocarbohydrazones (TCH), the higher homologues of the well-known thiosemicarbazones (TSC), and their metal complexes. The extra hydrazine moiety provides the ligands of variable metal binding modes, structural diversity and promising biological implications. The interesting coordination chemistry of TCH has mainly been focused on symmetric derivatives, which are relatively simple to synthesize while few examples of asymmetric ligands have been reported. This informative review on TCHs and their metal complexes will be helpful for improving the design of metal-based pharmaceuticals for applications ranging from anticancer to antinfective therapy.

Angiogenesis plays a key role in the wound healing process, involving the migration, growth, and differentiation of endothelial cells. Angiogenesis is controlled by a strict balance of different factors, and among these, the angiogenin protein plays a relevant role. Angiogenin is a secreted protein member of the ribonuclease superfamily that is taken up by cells and translocated to the nucleus when the process of blood vessel formation has to be promoted. However, the chemical signaling that activates the protein, normally present in the plasma, and the transport pathways through which the protein enters the cell are still largely unclear. Copper is also an angiogenic factor that regulates angiogenin expression and participates in the activation of common signaling pathways. The interaction between angiogenin and copper could be a relevant mechanism in regulating the formation of new blood vessel pathways and paving the way to the development of new drugs for chronic non-healing wounds.

Angiogenesis is a multi-step process by which new blood capillaries are formed starting from preexisting functional vessels