Abstract
Recent advances in nanotechnologies have led to wide use of nanomaterials in biomedical field. However, nanoparticles are found to interfere with protein misfolding and aggregation associated with many human diseases. It is still a controversial issue whether nanoparticles inhibit or promote protein aggregation. In this study, we used molecular dynamics simulations to explore the effects of three kinds of carbon nanomaterials including graphene, carbon nanotube and C60 on the aggregation behavior of islet amyloid polypeptide fragment 22–28 (IAPP22–28). The diverse behaviors of IAPP22–28 peptides on the surfaces of carbon nanomaterials were studied. The results suggest these nanomaterials can prevent β-sheet formation in differing degrees and further affect the aggregation of IAPP22–28. The π–π stacking and hydrophobic interactions are different in the interactions between peptides and different nanoparticles. The subtle differences in the interaction are due to the difference in surface curvature and area. The results demonstrate the adsorption interaction has competitive advantages over the interactions between peptides. Therefore, the fibrillation of IAPP22–28 may be inhibited at its early stage by graphene or SWCNT. Our study can not only enhance the understanding about potential effects of nanomaterials to amyloid formation, but also provide valuable information to develop potential β-sheet formation inhibitors against type II diabetes.
Highlights
Nanoparticles are highly promising candidates for various important biological applications, such as gene delivery [1], cellular imaging [2], and tumor therapy [3]
We focus on another fragment of the central region of amylin, hIAPP22–28, the fibril structure of which was reported belonging to the antiparallel hetero zipper class [53], to investigate the effects of different carbon NPs on its aggregation
In this work, we simulated disordered tetramer and octamer of hIAPP22–28 without or with different carbon NPs including graphene/single-wall carbon nanotube (SWCNT)/C60 to investigate the effects of these carbon nanomaterials on the aggregation behaviors of IAPP22–28
Summary
Nanoparticles are highly promising candidates for various important biological applications, such as gene delivery [1], cellular imaging [2], and tumor therapy [3]. When NPs are introduced in a living organism, their surfaces may perturb the native structure of proteins [8] as well as self-assembly pathway of peptides or proteins [9,10]. A lot of researches indicate NPs can interfere with amyloid formation [11,12,13,14,15,16,17]. Experimental studies indicate that the diverse effects of fullerene [11,12,13,14], carbon nanotube [15,16], graphite [17,18] and mica [17] on amyloid formation depend on the intrinsic property of the peptide and the surface, and the way they interact with each other
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