Zn(II) coordination influences the secondary structure, but not antimicrobial activity of the N-terminal histatin 3 hydrolysis product.

The relationship between the coordination chemistry and antimicrobial activity of Zn(II) and Cu(II)-bound histatins, salivary antimicrobial peptides, remains enigmatic. We focus on metal complexes of histatin 3 and its two products of hydrolysis: histatin 4 and its N-terminal fragment (histatin 3-4). The thermodynamic stability of these complexes is quite expected - the binding of Cu(II) the ATCUN motif results in the formation of very stable complexes.

An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.

The formation of a heterogeneous set of advanced glycation end products (AGEs) is the final outcome of a non-enzymatic process that occurs in vivo on long-life biomolecules. This process, known as glycation, starts with the reaction between reducing sugars, or their autoxidation products, with the amino groups of proteins, DNA, or lipids, thus gaining relevance under hyperglycemic conditions. Once AGEs are formed, they might affect the biological function of the biomacromolecule and, therefore, induce the development of pathophysiological events.

Insight into the Effect of Methylglyoxal on the Conformation, Function, and Aggregation Propensity of α-Synuclein.

It is well-known that people suffering from hyperglycemia have a higher propensity to develop Parkinson's disease (PD). One of the most plausible mechanisms linking these two pathologies is the glycation of neuronal proteins and the pathological consequences of it. α-Synuclein, a key component in PD, can be glycated at its fifteen lysine.

Understanding the effect of the membrane-mimetic micelles on the interplay between α-synuclein and Cu(II)/Cu(I) cations.

α-Synuclein (αS) is a presynaptic protein whose aggregates are considered as a hallmark of Parkinson's disease (PD). Although its physiological function is still under debate, it is widely accepted that its functions are always mediated by its interaction with membranes. The association of αS with phospholipid membranes occurs concomitant to its folding from its monomeric, unfolded state towards an antiparallel amphipathic α-helix.