Relationship between magnesium ions (Mg²⁺), amyloid aggregation, and prion-like mechanisms
Studies show a complex relationship where Mg²⁺ can modulate amyloid-β (Aβ) aggregation in various ways.
Some studies report Mg²⁺ promoting the formation of shorter, fragmented amyloid proteins, while others suggest it decreases β-sheet content, leading to aggregation-resistant states.
High intracellular Mg²⁺ can promote α-secretase-mediated cleavage of the amyloid precursor protein (APP), leading to clearance, while low levels increase Aβ secretion.
Mg²⁺ can induce tau aggregation in vitro, but in AD models, it can also reduce tau hyperphosphorylation by increasing GSK-3β phosphorylation.
Mg²⁺ may mediate interactions between intrinsically disordered nascent protein chains and ribosomes, potentially influencing folding and aggregation in the early stages of protein life.
Mg²⁺ can also stabilize the secondary structure of some proteins and inhibit their aggregation, as shown in studies on bovine serum albumin.
The strong binding affinity of noble metals for the thiol moiety of cysteine has been exploited in materials synthesis from amyloid systems.
Magnesium ions (Mg²⁺) are crucial for RNA stability and folding, primarily by neutralizing the negative charges on the phosphate backbone of RNA, which allows for the formation of tertiary structures.
Mg²⁺ binding stabilizes RNA by reducing electrostatic repulsion between phosphate groups, facilitating the compaction of RNA molecules and stabilizing their folded conformations.
RE: Intercellular Homeostasis