Zinc is required for virtually all biological processes. In plasma, Zn is predominantly transported by human serum albumin (HSA), which possesses two Zn-binding sites of differing affinities (sites A and B). Fatty acids (FAs) are also transported by HSA, with seven structurally characterized FA-binding sites (named FA1-FA7) known.
View Article and Find Full Text PDFInteractions between proteins and metal ions and their complexes are important in many areas of the life sciences, including physiology, medicine, and toxicology. Despite the involvement of essential elements in all major processes necessary for sustaining life, metalloproteomes remain ill-defined. This is not only owing to the complexity of metalloproteomes, but also to the non-covalent character of the complexes that most essential metals form, which complicates analysis.
View Article and Find Full Text PDFBiomimetic mineralization of enzymes for enhanced stability and activity is an important area of research due to its potential applications. Inorganic materials with enzymes coated and or embedded in them, viz., protein-inorganic hybrid nanomaterials with distinctive morphology and surface characteristics are promising candidates for exploring their elevated enzymatic activity.
View Article and Find Full Text PDFA triazole-derivatized, spiro-indoline-linked, 1,3-di-derivative of calix[4]arene () has been synthesized to take advantage of its ion-binding capability in the ring-open form. Indeed, the spiro-indoline moiety is well known for its photochromic, acidochromic, and metallochromic properties. Therefore, the has been explored for Cu binding, cell imaging, and anticancer activity of the corresponding complex since Cu complexes are known for such activity.
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