TY  - JOUR
A1  - Richter, Marina Juliane
A1  - Schulz, Alexander
A1  - Subkowski, Thomas
A1  - Böker, Alexander
T1  - Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces
JF  - Journal of colloid and interface science
N2  - Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H*Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior. (C) 2016 Elsevier Inc. All rights reserved.
KW  - Hydrophobin
KW  - Self-assembly
KW  - Pendant drop tensiometry
KW  - IFT
KW  - Rheology
Y1  - 2016
U6  - https://doi.org/10.1016/j.jcis.2016.06.062
SN  - 0021-9797
SN  - 1095-7103
VL  - 479
SP  - 199
EP  - 206
PB  - Elsevier
CY  - San Diego
ER  - 
TY  - JOUR
A1  - Bogomolova, Anna
A1  - Secker, Christian
A1  - Koetz, Joachim
A1  - Schlaad, Helmut
T1  - Thermo-induced multistep assembly of double-hydrophilic block copolypeptoids in water
JF  - Colloid and polymer science : official journal of the Kolloid-Gesellschaft
N2  - The aqueous solution behavior of thermoresponsive-hydrophilic block copolypeptoids, i.e., poly(N-(n-propyl)glycine) (x) -block-poly(N-methylglycine) (y) (x = 70; y = 23, 42, 76), in the temperature range of 20-45 A degrees C is studied. Turbidimetric analyses of the 0.1 wt% aqueous solutions reveal two cloud points at T (cp)similar to 30 and 45 A degrees C and a clearing point in between at T (cl)similar to 42 A degrees C. Temperature-dependent dynamic light scattering (DLS) suggest that right above the first collapse temperature, single polymer molecules assemble into large structures which upon further heating, i.e., at the clearing point temperature, disassemble into micelle-like structures. Upon further heating, the aggregates start to grow again in size, as recognized by the second cloud point, through a crystallization process.
KW  - Polypeptoids
KW  - Block copolymers
KW  - Thermoresponsive
KW  - Self-assembly
Y1  - 2017
U6  - https://doi.org/10.1007/s00396-017-4044-6
SN  - 0303-402X
SN  - 1435-1536
VL  - 295
SP  - 1305
EP  - 1312
PB  - Springer
CY  - New York
ER  -