Protein–Nanoparticle Interaction‐Induced Changes in Protein Structure and Aggregation. Issue 13 (2nd June 2016)

• Record Type: Journal Article
• Authors: Kim, Yuna; Ko, Sung Min; Nam, Jwa‐Min
• Is Part Of: Chemistry, an Asian journal. Volume 11:Issue 13(2016)
• Page Start: 1869
• Page End: 1877
• Publication Date: 2016-06-02
• Subjects: aggregation -- nanoparticles -- noncovalent interactions -- proteins -- self-assembly; Chemistry -- Periodicals; 540.5
• DOI: 10.1002/asia.201600236
• Languages: English
• ISSNs: 1861-4728

Abstract

Abstract: Large surface area, small size, strong optical properties, controllable structural features, variety of bioconjugation chemistries, and biocompatibility make many different types of nanoparticles (NPs), such as gold NPs, useful for many biological applications, such as biosensing, cellular imaging, disease diagnostics, drug delivery, and therapeutics. Recently, interactions between proteins and NPs have been extensively studied to understand, control, and utilize the interactions involved in biomedical applications of NPs and several biological processes, such as protein aggregation, for many diseases, including Alzheimer's disease. These studies also offer fundamental knowledge on changes in protein structure, protein aggregation mechanisms, and ways to unravel the roles and fates of NPs within the human body. This review focuses on recent studies on the roles and uses of NPs in protein structural changes and aggregation processes. Abstract : Probe the surface : Protein–nanoparticle (NP) interactions affect structural changes to proteins on the surface of NPs, protein–NP aggregation, and amyloidogenic protein self‐assembly (see figure). Studies of these interactions help to unravel the roles and fates of NPs within the human body.