0000000001051315
AUTHOR
Joanna Watly
Zn(II) and Ni(II) complexes with poly-histidyl peptides derived from a snake venom
Abstract The snake venoms are complex mixtures containing many bioactive peptides and proteins; some of them are aimed to protect the snake glands, where the venom is stored, until the latter is inoculated in the victim. In the venom of some vipers of the genus Atheris , a set of peptides containing poly-His and poly-Gly segments was recently found. Poly-His peptides are not rare in Nature. Although their exact biological function is most often unknown, one thing is certain: they have good binding properties towards the transition metal ions. As a matter of fact, the imidazole side chain of histidine is one of the groups most frequently involved in metal complexation in the active sites of …
Poly-Xaa Sequences in Proteins - Biological Role and Interactions with Metal Ions: Chemical and Medical Aspects
Background: The understanding of the bioinorganic and coordination chemistry of metalloproteins containing unusual poly-Xaa sequences, in which a single amino acid is repeated consecutively, is crucial for describing their metal binding-structure-function relationship, and therefore also crucial for understanding their medicinal potential. To the best of our knowledge, this is the first systematic review on metal complexes with polyXaa sequences. Methods: We performed a thorough search of high quality peer reviewed literature on poly-Xaa type of sequences in proteins, focusing on their biological importance and on their interactions with metal ions. Results: 228 papers were included in the…