Opposing enantiomers of tartaric acid anchored on a surface generate different insulin assemblies and hence contrasting cellular responses

Wei, Weili; Xu, Can; Gao, Nan; Ren, Jinsong; Qu, Xiaogang

doi:10.1039/c4sc01386g

Cited by 31 publications

(24 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More interestingly, a similar chiral effect was not only obtained for A β aggregation but also for the insulin assemblies by Qu et al [102]. In their study, classical biogenic chiral molecules, d - and l -tartaric acid, were assembled into monolayers on mica substrates, constructed as a model chiral surface.…”

Section: Protein Aggregation Modulated By Chiral Interfacesupporting

confidence: 62%

Protein/Peptide Aggregation and Amyloidosis on Biointerfaces

et al. 2016

View full text Add to dashboard Cite

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.

show abstract

Section: Protein Aggregation Modulated By Chiral Interfacesupporting

confidence: 62%

Protein/Peptide Aggregation and Amyloidosis on Biointerfaces

et al. 2016

View full text Add to dashboard Cite

show abstract

“…In addition to the aforementioned strategies, chiral molecules [292][293][294] or nanostructures, 295 carbon nanotubes coated by sonicated fragments of whey protein b-lactoglobulin, 23 gold nanoparticles coated with milk protein b-casein, 296 and polyoxometalate-Dawson derivatives (POMDs) functionalized with histidine-chelating metals (Cu, Fe, Ni, Co and Mn), 297 have been utilized as inhibitors against amyloidosis in cell cultures and with zebrafish models (embryos, larvae and adults), exploiting the chirality of amyloid fibrils, protein-metal coordination, chaperone-like inhibition of protein aggregation, as well as functional-pathological double protein coronae mediated by hydrogen bonding and b-sheet stacking. Zebrafish, in particular, have been validated as a high-fecundity alternative to AD, PD and T2D (transgenic) mouse models, [298][299][300] and are especially suited for testing a library of nanoparticle inhibitors to render significant statistics at low cost and high throughput.…”

Section: Amyloidosis Mitigation In Vitro and In Vivomentioning

confidence: 99%

Half a century of amyloids: past, present and future

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Within this topic, chiral discrimination on chiral surfaces has significant effects in protein adsorption and cellular adhesion and proliferation. 1 It would be expected that similar chiral discrimination was relevant in 3D-enviroments, such as in protein crystallogenesis. Remarkably, the expected influence of the chirality in protein crystallogenesis remains unexplored probably owing to the difficulty in obtaining a pair of enantiomeric environments suitable for crystallization.…”

mentioning

confidence: 99%