Amyloid-β: An Antimicrobial Defense Peptide

Dear Colleagues,

The physiologically produced and circulating Beta-Amyloid protein (Aβ) may have important functions. In contrast, although Aβ is a key player in Alzheimer’s disease (AD), it may initially be beneficial at the onset of infection. Acting as an antimicrobial peptide (AMP), Aβ helps contain pathogens. Host defense peptide such as Aß not only kill pathogens through their antimicrobial activity but also exhibit high affinity for bacterial lipopolysaccharides (LPS) and membrane receptors.

The microbial agglutination effect of Aß is overlooked and rarely discussed. This interaction occurs at the molecular level, driven by their common surfactant properties. Detergents, lipids, and fatty acids may facilitate Aß aggregations by confining the protein to small surfaces (e.g., vesicles), thereby increasing its effective concentration and driving aggregation through mass action. An additional potential contribution to membrane-induced amyloid aggregation may arise from conformational changes induced by membrane interactions, which can favor intermolecular interactions leading to aggregation.

This Special Issue welcomes the submission of original research articles and reviews focusing on protein aggregation and inhibition studies, particularly those identifying physiologically relevant binding partners of Aβ that modulate fibril formation or inhibition. For example, during infection, LL-37—a human AMP released by degranulation of neutrophils or secreted from other cells—is expected to modulate the innate immune response in diverse ways. LL-37 binds more strongly to Aβ oligomers than to mature fibrils, thereby tending to prevent fibril formation. Studies providing such insights are strongly encouraged, as they will help elucidate the molecular basis for the new therapeutic strategies and contribute to understanding the etiology AD.

Dr. Anna Lia Asti
Guest Editor

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