Dynamic Assembly of Class II Hydrophobins from T. reesei at the Air–Water Interface
Hähl, Hendrik; Griffo, Alessandra; Safaridehkohneh, Neda; Heppe, Jonas; Backes, Sebastian; Lienemann, Michael; Linder, Markus B.; Santen, Ludger; Laaksonen, Päivi; Jacobs, Karin (2019)
avautuu julkiseksi: 07.08.2020
Linder, Markus B.
American Chemical Society
Julkaisun pysyvä osoite on
Hähl H., Griffo A., Safaridehkohneh N., Heppe J., Backes S., Lienemann M., Linder M., Santen L., Laaksonen P., Jacobs K., (2019). Dynamic Assembly of Class II Hydrophobins from T. reesei at the Air–Water Interface. , American Chemical Society.
Class II hydrophobins are amphiphilic proteins produced by filamentous fungi. One of their typical features is the tendency to accumulate at the interface between an aqueous phase and a hydrophobic phase, such as the air-water interface. The kinetics of the interfacial self-assembly of wild-type (WT) hydrophobins HFBI and HFBII and some of their engineered variants at the air-water interface were measured by monitoring the accumulated mass at the interface via non-destructive ellipsometry measurements based on the reflecting light. The resulting mass vs. time curves revealed unusual kinetics for a monolayer formation that did not follow a typical Langmuir-type of behavior but had a rather coverage independent rate instead. Typically, the full surface coverage was obtained at masses corresponding to a monolayer. Formation of multilayers was not observed. The mechanism of the adsorption was studied by varying the structure or charges of the protein or the ionic strength of the subphase revealing that the lateral interactions between the hydrophobins play a role in their interfacial assembly. Additionally, a theoretical model was introduced in order to identify the underlying mechanism of the unconventional adsorption kinetics.