Facet-Dependent Interactions of Islet Amyloid Polypeptide with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption.

作者: Shih-Ting Wang , Yiyang Lin , Nevena Todorova , Yingqi Xu , Manuel Mazo

DOI: 10.1021/ACS.CHEMMATER.6B04144

关键词:

摘要: A comprehensive understanding of the mechanisms interaction between proteins or peptides and nanomaterials is crucial for development nanomaterial-based diagnostics therapeutics. In this work, we systematically explored interactions citrate-capped gold nanoparticles (AuNPs) islet amyloid polypeptide (IAPP), a 37-amino acid peptide hormone co-secreted with insulin from pancreatic islet. We utilized diffusion-ordered spectroscopy, isothermal titration calorimetry, localized surface plasmon resonance gel electrophoresis, atomic force microscopy, transmission electron microscopy (TEM), molecular dynamics (MD) simulations to elucidate underlying mechanism IAPP–AuNP interactions. Because presence metal-binding sequence motif in hydrophilic domain, IAPP strongly interacts Au both monomeric fibrillar states. Circular dichroism showed that AuNPs triggered conformational transit...

参考文章(71)
Chenxuan Wang, Aihua Yang, Xia Li, Denghua Li, Min Zhang, Huiwen Du, Chao Li, Yuanyuan Guo, Xiaobo Mao, Mingdong Dong, Flemming Besenbacher, Yanlian Yang, Chen Wang, Observation of molecular inhibition and binding structures of amyloid peptides Nanoscale. ,vol. 4, pp. 1895- 1909 ,(2012) , 10.1039/C2NR11508E
Amanda S. Barnard, Yu Chen, Kinetic modelling of the shape-dependent evolution of faceted gold nanoparticles Journal of Materials Chemistry. ,vol. 21, pp. 12239- 12245 ,(2011) , 10.1039/C1JM11677K
Yanina D. Álvarez, Jonathan A. Fauerbach, Jésica V. Pellegrotti, Thomas M. Jovin, Elizabeth A. Jares-Erijman, Fernando D. Stefani, Influence of gold nanoparticles on the kinetics of α-synuclein aggregation. Nano Letters. ,vol. 13, pp. 6156- 6163 ,(2013) , 10.1021/NL403490E
Yaron Bram, Anat Frydman-Marom, Inbal Yanai, Sharon Gilead, Ronit Shaltiel-Karyo, Nadav Amdursky, Ehud Gazit, Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies Scientific Reports. ,vol. 4, pp. 4267- 4267 ,(2015) , 10.1038/SREP04267
Per Westermark, Zhan-Chun Li, Gunilla T Westermark, Arnold Leckström, Donald F Steiner, None, Effects of beta cell granule components on human islet amyloid polypeptide fibril formation FEBS Letters. ,vol. 379, pp. 203- 206 ,(1996) , 10.1016/0014-5793(95)01512-4
Emma T.A.S Jaikaran, Anne Clark, Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochimica et Biophysica Acta. ,vol. 1537, pp. 179- 203 ,(2001) , 10.1016/S0925-4439(01)00078-3
Sajith A. Jayasinghe, Ralf Langen, Lipid membranes modulate the structure of islet amyloid polypeptide. Biochemistry. ,vol. 44, pp. 12113- 12119 ,(2005) , 10.1021/BI050840W
Wei-Feng Xue, Andrew L. Hellewell, Walraj S. Gosal, Steve W. Homans, Eric W. Hewitt, Sheena E. Radford, Fibril fragmentation enhances amyloid cytotoxicity. Journal of Biological Chemistry. ,vol. 284, pp. 34272- 34282 ,(2009) , 10.1074/JBC.M109.049809
Jessica A. Williamson, J. Patrick Loria, Andrew D. Miranker, Helix Stabilization Precedes Aqueous and Bilayer-Catalyzed Fiber Formation in Islet Amyloid Polypeptide Journal of Molecular Biology. ,vol. 393, pp. 383- 396 ,(2009) , 10.1016/J.JMB.2009.07.077