Imperial College London

Professor Molly Stevens FREng

Faculty of EngineeringDepartment of Materials

Prof of Biomedical Materials&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{Lin:2019:10.1021/acsnano.8b08117,
author = {Lin, Y and Penna, M and Thomas, MR and Wojciechowski, J and Leonardo, V and Wang, Y and Pashuck, ET and Yarovsky, I and Stevens, M},
doi = {10.1021/acsnano.8b08117},
journal = {ACS Nano},
pages = {1900--1909},
title = {Residue-specific solvation directed thermodynamic and kinetic control over peptide self-assembly with 1D/2D structure selection},
url = {http://dx.doi.org/10.1021/acsnano.8b08117},
volume = {13},
year = {2019}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - 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.
AU - Lin,Y
AU - Penna,M
AU - Thomas,MR
AU - Wojciechowski,J
AU - Leonardo,V
AU - Wang,Y
AU - Pashuck,ET
AU - Yarovsky,I
AU - Stevens,M
DO - 10.1021/acsnano.8b08117
EP - 1909
PY - 2019///
SN - 1936-0851
SP - 1900
TI - Residue-specific solvation directed thermodynamic and kinetic control over peptide self-assembly with 1D/2D structure selection
T2 - ACS Nano
UR - http://dx.doi.org/10.1021/acsnano.8b08117
UR - http://hdl.handle.net/10044/1/67149
VL - 13
ER -