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Researchers' Work from Northwestern University Focuses on Proteomics (Directing the self-assembly of supra-biomolecular nanotubes using entropic...

August 5, 2014



Researchers' Work from Northwestern University Focuses on Proteomics (Directing the self-assembly of supra-biomolecular nanotubes using entropic forces)

By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Proteomics are discussed in a new report. According to news reporting originating from Evanston, Illinois, by NewsRx correspondents, research stated, "Peptide self-assembly, ubiquitous in biology, is one of the most promising 'bottom-up' approaches for the generation of synthetic supramolecular architectures. However, directing the self-assembly of functional peptides into predictable ordered structures most often requires precise tuning of weak intermolecular forces."

Our news editors obtained a quote from the research from Northwestern University, "Existing strategies are generally based on specific interactions between molecular mediators that require complex chemical synthesis pathways and elaborated design rules. Here we establish a theoretical framework that delineates a generic route towards directing the self-assembly of small peptides by simply using entropic forces generated by the polymer chains attached to the peptides. We demonstrate the viability of this concept for polymer-conjugated peptide nanotubes using coarse-grained molecular dynamics (CGMD) simulations combined with theoretical calculations. We show that conjugated polymer chains create an entropic penalty due to chain confinement upon assembly, and illustrate that the self-assembly process can be directed by merely varying the degree of polymer conjugation. Specifically, the entropic penalty, and consequently, the binding energy between peptides can be greatly varied by changing the length and the number of conjugated polymers. Extending this concept for peptides with different degrees of conjugation reveals a path towards controlling the stacking sequence of binary mixtures. Remarkably, we find that a large disparity in the conjugation degree of the two peptides results in a preference towards alternating mixed sequences that minimize the entropic penalty of confinement in the thermodynamic limit."

According to the news editors, the research concluded: "Our study explains recent experiments on polymer-peptide conjugates and sets the stage for utilizing entropic forces to guide the stacking sequence of functional macrocycles in tubular assemblies."

For more information on this research see: Directing the self-assembly of supra-biomolecular nanotubes using entropic forces. Soft Matter, 2014;10(6):851-61. (Royal Society of Chemistry - www.rsc.org/; Soft Matter - pubs.rsc.org/en/journals/journalissues/sm)

The news editors report that additional information may be obtained by contacting L. Ruiz, Dept. of Civil & Environmental Engineering and Mechanical Engineering, Northwestern University, Evanston, Illinois 60208-3111, United States (see also Proteomics).

Keywords for this news article include: Evanston, Illinois, Nanotube, Peptides, Proteins, Proteomics, United States, Nanotechnology, Emerging Technologies, North and Central America.

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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