Abstract

Event Abstract Back to Event Periodically sequenced peptides: A new tool for nanoscale materials synthesis Matthew Kubilius1 and Raymond S. Tu1 1 City College of New York, Chemical Engineering, United States Synthesizing useful, periodically-sequenced, self-assembling, amphipathic polypeptides is difficult due to increasing polydispersity indices of large molecular weight polymer systems. Accounting for this, we engineered amino acid dimers that polymerize into amphipathic chains with alternating hydrophilic/hydrophobic side groups. This system's periodicity is typical of amino acid sequences that self-assemble into beta-sheets. We limit polydispersity in the growing polypeptide chains through changes to the kinetics of growth by transport-limited chain elongation and partitioning of large molecular weight polypeptides to interfaces. We show that in the absence of a bulk micellular interface, standard condensation polymerization occurs. However, the amphipathic character of our peptide chains increases with increasing molecular weight, resulting in a polypeptide that preferentially partitions into surfactant micelles with increasing molecular weight. Grown that way, with exposure to large, diffuse, bulk-phase interfacial areas, this kinetically-limited growth narrows the polydispersity of our polypeptides. We quantify polydispersity indices using multi-angle light scattering and characterize evolving sheet-like secondary structure using circular dichroism for various amino acid dimer systems. Our results show that the peptides grown in micelle-containing media show significantly enhanced self-assembly and narrowed polydispersity indices. We further characterize these self-assemblies as Langmuir-Blodgett films when the polypeptide partitions strongly to an air-water interface, and image them using Brewster angle microscopy. We conclude that transport-limited polymerization shows great promise in the synthesis of low-cost, surface-active, self-assembling polypeptides. National Science Foundation, Division of Materials Research; National Science Foundation, Chemical, Bioengineering, Environmental, and Transport Systems Keywords: self-assembly, amphiphile, Polymeric material, Polypeptide Conference: 10th World Biomaterials Congress, Montréal, Canada, 17 May - 22 May, 2016. Presentation Type: Poster Topic: Naturally-derived materials and biopolymers Citation: Kubilius M and Tu RS (2016). Periodically sequenced peptides: A new tool for nanoscale materials synthesis. Front. Bioeng. Biotechnol. Conference Abstract: 10th World Biomaterials Congress. doi: 10.3389/conf.FBIOE.2016.01.02762 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 27 Mar 2016; Published Online: 30 Mar 2016. Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Matthew Kubilius Raymond S Tu Google Matthew Kubilius Raymond S Tu Google Scholar Matthew Kubilius Raymond S Tu PubMed Matthew Kubilius Raymond S Tu Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.

Highlights

  • Sequenced peptides can be confined to interfaces and assembled into patterns that present chemical functionalities with exceptional spatial precision

  • The role of dynamics during the assembly of these peptides appears to be very important for inorganic nucleation and growth

  • Our work applies periodically sequenced sheet-forming peptides at interfaces to explore the fundamental dynamics of assembly

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Summary

Introduction

Sequenced peptides can be confined to interfaces and assembled into patterns that present chemical functionalities with exceptional spatial precision. Sequenced Peptides: A New Tool for Nanoscale Materials Synthesis Dr Raymond S Tu Department of Chemical Engineering The City College of New York

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