TY - JOUR
T1 - Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air-Water Interface
AU - Meister, Konrad
AU - Bäumer, Alexander
AU - Szilvay, Geza R.
AU - Paananen, Arja
AU - Bakker, Huib J.
N1 - Publisher Copyright:
© 2016 American Chemical Society.
PY - 2016/10/20
Y1 - 2016/10/20
N2 - We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water-air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.
AB - We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water-air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.
UR - http://www.scopus.com/inward/record.url?scp=84992183709&partnerID=8YFLogxK
U2 - 10.1021/acs.jpclett.6b01917
DO - 10.1021/acs.jpclett.6b01917
M3 - Article
AN - SCOPUS:84992183709
VL - 7
SP - 4067
EP - 4071
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
IS - 20
ER -