The Library
Profiling the serum protein corona of fibrillar human islet amyloid polypeptide
Tools
Tools
Tools
Pilkington, Emily H., Gustafsson, Ove Johan Ragnar, Xing, Yanting, Hernandez Fernaud, Juan Ramon, Zampronio, Cleidiane, Kakinen, Aleksandr, Faridi, Ava, Ding, Feng, Wilson, Paul, Ke, Pu Chun and Davis, Thomas P. (2018) Profiling the serum protein corona of fibrillar human islet amyloid polypeptide. ACS Nano . doi:10.1021/acsnano.8b02346 (In Press)
![[img]](http://wrap.warwick.ac.uk/style/images/fileicons/application_pdf.png) |
PDF
WRAP-profiling-serum-protein-corona-fibrillar-Davis-2018.pdf - Accepted Version Embargoed item. Restricted access to Repository staff only until 10 May 2019. Contact author directly, specifying your specific needs. - Requires a PDF viewer. Download (2428Kb) |
|
PDF
WRAP-amyloid-protein-corona-Supporting-information-2018.pdf - Supplemental Material Embargoed item. Restricted access to Repository staff only until 10 May 2019. Contact author directly, specifying your specific needs. - Requires a PDF viewer. Download (4Mb) |
Official URL: http://dx.doi.org/10.1021/acsnano.8b02346
Abstract
Amyloids may be regarded as native nanomaterials that form in the presence of complex protein mixtures. By drawing an analogy with the physicochemical properties of nanoparticles in biological fluids, we hypothesized that amyloids should form a protein corona in vivo that would imbue the underlying amyloid with a modified biological identity. To explore this hypothesis we characterized the protein corona of human islet amyloid polypeptide (IAPP) fibrils in FBS using two complementary methodologies developed herein; quartz crystal microbalance and ‘centrifugal capture’, coupled with nano-liquid chromatography tandem mass spectroscopy. Clear evidence for a significant protein corona was obtained. No trends were identified for amyloid corona proteins based on their physicochemical properties, while strong binding with IAPP fibrils occurred for linear proteins or multi-domain proteins with structural plasticity. Proteomic analysis identified amyloid-enriched proteins that are known to play significant roles in mediating cellular machinery and processing, potentially leading to pathological outcomes and therapeutic targets.
| Item Type: | Journal Article | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QP Physiology R Medicine > RS Pharmacy and materia medica |
||||||||||||||||||
| Divisions: | Faculty of Science > Chemistry | ||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Amyloid, Polypeptides, Nanoparticles | ||||||||||||||||||
| Journal or Publication Title: | ACS Nano | ||||||||||||||||||
| Publisher: | American Chemical Society | ||||||||||||||||||
| ISSN: | 1936-0851 | ||||||||||||||||||
| Official Date: | 10 May 2018 | ||||||||||||||||||
| Dates: |
|
||||||||||||||||||
| Date of first compliant deposit: | 11 May 2018 | ||||||||||||||||||
| DOI: | 10.1021/acsnano.8b02346 | ||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||
| Publication Status: | In Press | ||||||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | ||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
