A minimal length rigid helical peptide motif allows rational design of modular surfactants

Sudipta Mondal, Maxim Varenik, Daniel Nir Bloch, Yoav Atsmon-Raz, Guy Jacoby, Lihi Adler-Abramovich, Linda J.W. Shimon, Roy Beck, Yifat Miller (), Oren Regev and Ehud Gazit ()
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Sudipta Mondal: George S. Wise Faculty of Life Sciences, Tel Aviv University
Maxim Varenik: Ben-Gurion University of the Negev
Daniel Nir Bloch: Ben-Gurion University of the Negev
Yoav Atsmon-Raz: Ben-Gurion University of the Negev
Guy Jacoby: The Raymond and Beverly Sackler School of Physics and Astronomy, Tel Aviv University
Lihi Adler-Abramovich: The Goldschleger School of Dental Medicine, Tel Aviv University
Linda J.W. Shimon: Weizmann Institute of Science
Roy Beck: The Raymond and Beverly Sackler School of Physics and Astronomy, Tel Aviv University
Yifat Miller: Ben-Gurion University of the Negev
Oren Regev: Ben-Gurion University of the Negev
Ehud Gazit: George S. Wise Faculty of Life Sciences, Tel Aviv University

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract Extensive work has been invested in the design of bio-inspired peptide emulsifiers. Yet, none of the formulated surfactants were based on the utilization of the robust conformation and self-assembly tendencies presented by the hydrophobins, which exhibited highest surface activity among all known proteins. Here we show that a minimalist design scheme could be employed to fabricate rigid helical peptides to mimic the rigid conformation and the helical amphipathic organization. These designer building blocks, containing natural non-coded α-aminoisobutyric acid (Aib), form superhelical assemblies as confirmed by crystallography and microscopy. The peptide sequence is amenable to structural modularity and provides the highest stable emulsions reported so far for peptide and protein emulsifiers. Moreover, we establish the ability of short peptides to perform the dual functions of emulsifiers and thickeners, a feature that typically requires synergistic effects of surfactants and polysaccharides. This work provides a different paradigm for the molecular engineering of bioemulsifiers.

Date: 2017
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DOI: 10.1038/ncomms14018

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