Abstract
Amyloids are highly ordered, cross-β-sheet-rich protein/peptide aggregates associated with both human diseases and native functions. Given the well established ability of amyloids in interacting with cell membranes, we hypothesize that amyloids can serve as universal cell-adhesive substrates. Here, we show that, similar to the extracellular matrix protein collagen, amyloids of various proteins/peptides support attachment and spreading of cells via robust stimulation of integrin expression and formation of integrin-based focal adhesions. Additionally, amyloid fibrils are also capable of immobilizing non-adherent red blood cells through charge-based interactions. Together, our results indicate that both active and passive mechanisms contribute to adhesion on amyloid fibrils. The present data may delineate the functional aspect of cell adhesion on amyloids by various organisms and its involvement in human diseases. Our results also raise the exciting possibility that cell adhesivity might be a generic property of amyloids.
Highlights
The extracellular matrix (ECM)5 composed of proteins, minerals, and carbohydrates [1] provides physical support to individual cells and facilitates interactions between cells and links them into functional tissue [2]
Our results showed more cell adhesion and cell spreading on amyloid fibrils of polyamino acid (PAA) than in its respective unstructured state (Fig. 16, A–C)
These findings clearly indicate that integrins play a significant role in amyloid-mediated cellular adhesion and suggest that charge of the peptide/proteins helps in adhesion, the cross-structured state further promotes stronger adhesion
Summary
Amyloid fibrils have been reported to be a part of the biofilms in numerous microorganisms, including harpins of Xanthomonas campestris and Pseudomonas syringae [27], pili from Mycobacterium tuberculosis [28], chaplins from Streptomyces coelicolor [29], and hydrophobins from fungi [30] These amyloidogenic ECM components help these organisms to adhere onto the surface and form colonies. Recent studies suggest that amyloid fibrils alone (without any functionalization) are capable of supporting cell adhesion due to their unique nanotopographic features [33,34,35,36,37] It remains unclear whether this celladhesive property is dependent on the sequence composition or is a consequence of the amyloid nature.
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