期刊
ACS NANO
卷 13, 期 2, 页码 1900-1909出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.8b08117
关键词
self-assembly; peptide solvation; 2D structures; fibrils; pathway dependence
类别
资金
- Engineering and Physical Sciences Research Council (EPSRC) i-sense IRC in Early Warning Sensing Systems for Infectious Diseases [EP/K031953/1]
- U.K. Regenerative Medicine Platform Acellular/Smart Materials-3D Architecture [MR/R015651/1]
- China Scholarship Council
- ERC FP7Marie Curie actions through the Intra-European Marie Curie Fellowship Peptide Osteogel [275433]
- Australian Research Council [DP140101888, DP170100511]
- EPSRC [EP/K020641/1]
- Wellcome Trust [098411/Z/12/Z]
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/L015129/1]
- BBSRC [BB/L015129/1] Funding Source: UKRI
- EPSRC [EP/K031953/1, EP/K020641/1] Funding Source: UKRI
- MRC [MR/R015651/1] Funding Source: UKRI
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.
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