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Materials 2016, 9(9), 740; doi:10.3390/ma9090740

Protein/Peptide Aggregation and Amyloidosis on Biointerfaces

1
State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, 122 Luoshi Road, Wuhan 430070, China
2
School of Chemistry, Chemical Engineering and Life Science, Wuhan University of Technology, 122 Luoshi Road, Wuhan 430070, China
*
Authors to whom correspondence should be addressed.
Academic Editor: Qun Ren
Received: 10 July 2016 / Revised: 12 August 2016 / Accepted: 25 August 2016 / Published: 30 August 2016
(This article belongs to the Special Issue Advances in Biointerfaces)
View Full-Text   |   Download PDF [16359 KB, uploaded 30 August 2016]   |  

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. View Full-Text
Keywords: protein aggregation; neurodegenerative disease; biomaterials; biointerface; surface chemistry protein aggregation; neurodegenerative disease; biomaterials; biointerface; surface chemistry
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Lu, Q.; Tang, Q.; Xiong, Y.; Qing, G.; Sun, T. Protein/Peptide Aggregation and Amyloidosis on Biointerfaces. Materials 2016, 9, 740.

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