Protein/Peptide Aggregation and Amyloidosis on Biointerfaces

Abstract

Recently, studies of protein/peptide aggregation, particularly the amyloidosis, have attracted considerable attention in discussions of the pathological mechanisms of most neurodegenerative diseases. The protein/peptide aggregation processes often occur at the membrane–cytochylema interface in vivo and behave differently from those occurring in bulk solution, which raises great interest to investigate how the interfacial properties of artificial biomaterials impact on protein aggregation. From the perspective of bionics, current progress in this field has been obtained mainly from four aspects: (1) hydrophobic–hydrophilic interfaces; (2) charged surface; (3) chiral surface; and (4) biomolecule-related interfaces. The specific physical and chemical environment provided by these interfaces is reported to strongly affect the adsorption of proteins, transition of protein conformation, and diffusion of proteins on the biointerface, all of which are ultimately related to protein assembly. Meanwhile, these compelling results of in vitro experiments can greatly promote the development of early diagnostics and therapeutics for the relevant neurodegenerative diseases. This paper presents a brief review of these appealing studies, and particular interests are placed on weak interactions (i.e., hydrogen bonding and stereoselective interactions) that are also non-negligible in driving amyloid aggregation at the interfaces. Moreover, this paper also proposes the future perspectives, including the great opportunities and challenges in this field as well.

Adsorption of unfolded Cu/Zn superoxide dismutase onto hydrophobic surfaces catalyzes its formation of amyloid fibrils

“…Polystyrene is a hydrophobic polymer known to interact with hydrophobic patches on solutes, such as those presented by unfolded proteins (Thormann et al, 2008;Faghihnejad and Zeng, 2012;Shen et al, 2012;Lu et al, 2016). By contrast, surfaces coated with polyethylene glycol present a non-ionic hydrophilic environment that mitigates protein adsorption and concomitant unfolding (Alcantar et al, 2000;Shen et al, 2012;Lu et al, 2016).…”

“…Interactions between amyloidogenic proteins and membrane surfaces play a prominent role in fibril formation and toxicity in vivo (Stefani, 2007;Aisenbrey et al, 2008;Lu et al, 2016). Association of proteins onto a surface can increase the effective concentration and reduce the stability of the native state, thereby nucleating aggregation.…”

In Silico Studies of The Human IAPP In Presence of Osmolytes

“…Aggregation process of proteins or peptides can be triggered by hydrophobic-hydrophilic interfaces [68]. Protein-protein interactions in the aggregation process can be electrostatic or hydrophobic.…”

Chiral Effect at Nano-Bio Interface: A Model of Chiral Gold Nanoparticle on Amylin Fibrillation

“…More and more evidences have indicated that the multiscale biological membranes in vivo provide a larger number of reactive sites to interact with dissociative protein/peptides [8,9,10,11], which play a key procedure for their accumulation and fibrillation at very low concentrations [12,13,14]. Various models with different physicochemical properties (e.g., composition [15,16], surface charge [17], hydrophilicity [18], hydrophobicity [19,20], chirality [21,22,23,24] and size [25,26]) of interfaces have been built to simulate the interaction between peptides and membranes [27]. Some of our previous works [21,28] have verified the chiral effect on Aβ peptides fibrillation and assembly on flat solid-liquid interface.…”