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Varilly P, Willard AP, Kirkegaard JB, et al. Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers. J Chem Phys. 2017;146(13):135102doi: 10.1063/1.4977932.
Varilly, P., Willard, A. P., Kirkegaard, J. B., Knowles, T. P., & Chandler, D. (2017). Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers. The Journal of chemical physics, 146(13), 135102. https://doi.org/10.1063/1.4977932
Varilly, Patrick, et al. "Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers." The Journal of chemical physics vol. 146,13 (2017): 135102. doi: https://doi.org/10.1063/1.4977932
Varilly P, Willard AP, Kirkegaard JB, Knowles TP, Chandler D. Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers. J Chem Phys. 2017 Apr 07;146(13):135102. doi: 10.1063/1.4977932. PMID: 28390364.
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J Chem Phys. 2017 Apr 07;146(13):135102. doi: 10.1063/1.4977932.

Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers.

The Journal of chemical physics

Patrick Varilly, Adam P Willard, Julius B Kirkegaard, Tuomas P J Knowles, David Chandler

Affiliations

  1. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
  2. Department of Chemistry, MIT, Cambridge, Massachusetts 02139, USA.
  3. Department Applied Mathematics and Theoretical Physics, Centre for Mathematical Sciences, University of Cambridge, Wilberforce Road, Cambridge CB3 0WA, United Kingdom.
  4. Department of Chemistry, University of California, Berkeley, California 94720, USA.

PMID: 28390364 DOI: 10.1063/1.4977932

Abstract

Aggregation of amphiphiles through the action of hydrophobic interactions is a common feature in soft condensed matter systems and is of particular importance in the context of biophysics as it underlies both the generation of functional biological machinery as well as the formation of pathological misassembled states of proteins. Here we explore the aggregation behaviour of amphiphilic polymers using lattice Monte Carlo calculations and show that the distribution of hydrophobic residues within the polymer sequence determines the facility with which dry/wet interfaces can be created and that such interfaces drive the aggregation process.

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