The bacterial hydrophobin BslA is a switchable ellipsoidal Janus nanocolloid

Giovanni B. Brandani, Marieke Schor, Ryan Morris, Nicola Stanley-Wall, Cait E. MacPhee, Davide Marenduzzo (Lead / Corresponding author), Ulrich Zachariae (Lead / Corresponding author)

Research output: Contribution to journalArticle

16 Citations (Scopus)
186 Downloads (Pure)

Abstract

BslA is an amphiphilic protein that forms a highly hydrophobic coat around Bacillus subtilis biofilms, shielding the bacterial community from external aqueous solution. It has a unique structure featuring a distinct partition between hydrophilic and hydrophobic surfaces. This surface property is reminiscent of synthesized Janus colloids. By investigating the behavior of BslA variants at water-cyclohexane interfaces through a set of multi-scale simulations informed by experimental data, we show that BslA indeed represents a biological example of an ellipsoidal Janus nanoparticle, whose surface interactions are, moreover, readily switchable. BslA contains a local conformational toggle, which controls its global affinity for, and orientation at, water-oil interfaces. This adaptability, together with single-point mutations, enables the fine-tuning of its solvent and interfacial interactions, and suggests that BslA could be a basis for biotechnological applications.

Original languageEnglish
Pages (from-to)11558-11563
Number of pages6
JournalLangmuir
Volume31
Issue number42
Early online date17 Sep 2015
DOIs
Publication statusPublished - 27 Oct 2015

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