Imperial College London
Alternate

Professor Molly Stevens

Faculty of Engineering, Department of Materials

Professor of Biomedical Materials and Regenerative Medicine
 
 
 
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Contact

 

+44 (0)20 7594 6804m.stevens

 
 
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Location

 

208Royal School of MinesSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wang:2017:10.1021/acs.chemmater.6b04144,
author = {Wang, S and Lin, Y and Todorova, N and Xu, Y and Mazo, M and Rana, S and Leonardo, V and Amdursky, N and Spicer, CD and Alexander, BD and Edwards, AA and Matthews, SJ and Yarovsky, I and Stevens, MM},
doi = {10.1021/acs.chemmater.6b04144},
journal = {Chemistry of Materials},
title = {Facet-dependent interactions of islet amyloid polypeptide with gold nanoparti-cles: implications for fibril formation and peptide-induced lipid membrane dis-ruption},
url = {http://dx.doi.org/10.1021/acs.chemmater.6b04144},
volume = {29},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - A comprehensive understanding of the mechanisms of interaction between proteins or peptides and nanomaterials is crucial for the development of nanomaterial-based diagnos-tics and therapeutics. In this work, we systematically explored the interactions between citrate-capped gold nanoparticles (AuNPs) and islet amyloid polypeptide (IAPP), a 37-amino acid peptide hormone co-secreted with insulin from the pancreatic islet. We uti-lized diffusion-ordered spectroscopy, isothermal titration calorimetry, localized surface plasmon resonance spectroscopy, gel electrophoresis, atomic force microscopy, transmis-sion electron microscopy (TEM), and molecular dynamics (MD) simulations to systemati-cally elucidate the underlying mechanism of the IAPP−AuNP interactions. Because of the presence of a metal-binding sequence motif in the hydrophilic peptide domain, IAPP strongly interacts with the Au surface in both the monomeric and fibrillar states. Circular dichroism showed that AuNPs triggered the IAPP conformational transition from random coil to ordered structures (α-helix and β-sheet), and TEM imaging suggested the accelera-tion of IAPP fibrillation in the presence of AuNPs. MD simulations revealed that the IAPP−AuNP interactions were initiated by the N-terminal domain (IAPP residues 1−19), which subsequently induced a facet-dependent conformational change in IAPP. On a Au(111) surface, IAPP was unfolded and adsorbed directly onto the Au surface, while for the Au(100) surface, it interacted predominantly with the citrate adlayer and retained some helical conformation. The observed affinity of AuNPs for IAPP was further applied to reduce the level of peptide-induced lipid membrane disruption.
AU  - Wang,S
AU  - Lin,Y
AU  - Todorova,N
AU  - Xu,Y
AU  - Mazo,M
AU  - Rana,S
AU  - Leonardo,V
AU  - Amdursky,N
AU  - Spicer,CD
AU  - Alexander,BD
AU  - Edwards,AA
AU  - Matthews,SJ
AU  - Yarovsky,I
AU  - Stevens,MM
DO  - 10.1021/acs.chemmater.6b04144
PY  - 2017///
SN  - 1520-5002
TI  - Facet-dependent interactions of islet amyloid polypeptide with gold nanoparti-cles: implications for fibril formation and peptide-induced lipid membrane dis-ruption
T2  - Chemistry of Materials
UR  - http://dx.doi.org/10.1021/acs.chemmater.6b04144
UR  - http://hdl.handle.net/10044/1/44346
VL  - 29
ER  -
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