Residue-specific solvation directed thermodynamic and kinetic control over peptide self-assembly with 1D/2D structure selection
File(s)
Published version
Author(s)
Type
Journal Article
Abstract
Understanding the self-organization and structural transformations of molecular ensembles is important to explore the complexity of biological systems. Here, we illustrate the crucial role of cosolvents and solvation effects in thermodynamic and kinetic control over peptide association into ultrathin Janus nanosheets, elongated nanobelts, and amyloid-like fibrils. We gained further insight into the solvation-directed self-assembly (SDSA) by investigating residue-specific peptide solvation using molecular dynamics modeling. We proposed the preferential solvation of the aromatic and alkyl domains on the peptide backbone and protofibril surface, which results in volume exclusion effects and restricts the peptide association between hydrophobic walls. We explored the SDSA phenomenon in a library of cosolvents (protic and aprotic), where less polar cosolvents were found to exert a stronger influence on the energetic balance at play during peptide propagation. By tailoring cosolvent polarity, we were able to achieve precise control of the peptide nanostructures with 1D/2D shape selection. We also illustrated the complexity of the SDSA system with pathway-dependent peptide aggregation, where two self-assembly states (i.e., thermodynamic equilibrium state and kinetically trapped state) from different sample preparation methods were obtained.
Date Issued
2019-02-26
Date Acceptance
2019-01-16
Citation
ACS Nano, 2019, 13 (2), pp.1900-1909
ISSN
1936-0851
Publisher
American Chemical Society
Start Page
1900
End Page
1909
Journal / Book Title
ACS Nano
Volume
13
Issue
2
Copyright Statement
© 2019 American Chemical Society. This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Sponsor
Commission of the European Communities
Engineering & Physical Science Research Council (E
Biotechnology and Biological Sciences Research Council (BBSRC)
Engineering & Physical Science Research Council (EPSRC)
Wellcome Trust
Medical Research Council (MRC)
Grant Number
PIEF_GA-2010-275433
EP/K031953/1
BB/L015129/1
EP/K020641/1
098411/Z/12/Z
MR/R015651/1
Subjects
2D structures
fibrils
pathway dependence
peptide solvation
self-assembly
MD Multidisciplinary
Nanoscience & Nanotechnology
Publication Status
Published
Date Publish Online
2019-01-23