Dynamic assembly of class II hydrophobins from T. reesei at the air-water interface

Hendrik Hähl (Corresponding Author), Alessandra Griffo, Neda Safaridehkohneh, Jonas Heppe, Sebastian Backes, Michael Lienemann, Markus B. Linder, Ludger Santen, Päivi Laaksonen (Corresponding Author), Karin Jacobs

Research output: Contribution to journalArticleScientificpeer-review

Abstract

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 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 nondestructive ellipsometry measurements. 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. The formation of multilayers was not observed. Atomic force microscopy revealed formation and growth of non-fusing protein clusters at the interface. 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 to identify the underlying mechanism of the unconventional adsorption kinetics.
Original languageEnglish
Pages (from-to)9202 - 9212
Number of pages11
JournalLangmuir
Volume35
Issue number28
DOIs
Publication statusPublished - 20 Jun 2019
MoE publication typeA1 Journal article-refereed

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assembly
Proteins
Kinetics
Water
Monolayers
air
Air
water
Adsorption
proteins
Ellipsometry
Ionic strength
Fungi
kinetics
Self assembly
Atomic force microscopy
Multilayers
adsorption
fungi
Monitoring

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Hähl, H., Griffo, A., Safaridehkohneh, N., Heppe, J., Backes, S., Lienemann, M., ... Jacobs, K. (2019). Dynamic assembly of class II hydrophobins from T. reesei at the air-water interface. Langmuir, 35(28), 9202 - 9212. https://doi.org/10.1021/acs.langmuir.9b01078
Hähl, Hendrik ; Griffo, Alessandra ; Safaridehkohneh, Neda ; Heppe, Jonas ; Backes, Sebastian ; Lienemann, Michael ; Linder, Markus B. ; Santen, Ludger ; Laaksonen, Päivi ; Jacobs, Karin. / Dynamic assembly of class II hydrophobins from T. reesei at the air-water interface. In: Langmuir. 2019 ; Vol. 35, No. 28. pp. 9202 - 9212.
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abstract = "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 hydrophobinsHFBI and HFBII and some of their engineered variants at the air−water interface were measured by monitoring the accumulated mass at the interface via nondestructive ellipsometry measurements. 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. The formation of multilayers was not observed. Atomic force microscopy revealed formation and growth of non-fusing protein clusters at the interface. 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 to identify the underlying mechanism of the unconventional adsorption kinetics.",
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Hähl, H, Griffo, A, Safaridehkohneh, N, Heppe, J, Backes, S, Lienemann, M, Linder, MB, Santen, L, Laaksonen, P & Jacobs, K 2019, 'Dynamic assembly of class II hydrophobins from T. reesei at the air-water interface', Langmuir, vol. 35, no. 28, pp. 9202 - 9212. https://doi.org/10.1021/acs.langmuir.9b01078

Dynamic assembly of class II hydrophobins from T. reesei at the air-water interface. / Hähl, Hendrik (Corresponding Author); Griffo, Alessandra; Safaridehkohneh, Neda; Heppe, Jonas; Backes, Sebastian; Lienemann, Michael; Linder, Markus B.; Santen, Ludger; Laaksonen, Päivi (Corresponding Author); Jacobs, Karin.

In: Langmuir, Vol. 35, No. 28, 20.06.2019, p. 9202 - 9212.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Backes, Sebastian

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AU - Jacobs, Karin

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N2 - 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 hydrophobinsHFBI and HFBII and some of their engineered variants at the air−water interface were measured by monitoring the accumulated mass at the interface via nondestructive ellipsometry measurements. 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. The formation of multilayers was not observed. Atomic force microscopy revealed formation and growth of non-fusing protein clusters at the interface. 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 to identify the underlying mechanism of the unconventional adsorption kinetics.

AB - 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 hydrophobinsHFBI and HFBII and some of their engineered variants at the air−water interface were measured by monitoring the accumulated mass at the interface via nondestructive ellipsometry measurements. 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. The formation of multilayers was not observed. Atomic force microscopy revealed formation and growth of non-fusing protein clusters at the interface. 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 to identify the underlying mechanism of the unconventional adsorption kinetics.

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Hähl H, Griffo A, Safaridehkohneh N, Heppe J, Backes S, Lienemann M et al. Dynamic assembly of class II hydrophobins from T. reesei at the air-water interface. Langmuir. 2019 Jun 20;35(28):9202 - 9212. https://doi.org/10.1021/acs.langmuir.9b01078