TY  - JOUR
A1  - Reinicke, Stefan
A1  - Rees, Huw C.
A1  - Espeel, Pieter
A1  - Vanparijs, Nane
A1  - Bisterfeld, Carolin
A1  - Dick, Markus
A1  - Rosencrantz, Ruben R.
A1  - Brezesinski, Gerald
A1  - de Geest, Bruno G.
A1  - Du Prez, Filip E.
A1  - Pietruszka, Jörg
A1  - Böker, Alexander
T1  - Immobilization of 2-Deoxy-D-ribose-5-phosphate Aldolase in Polymeric Thin Films via the Langmuir-Schaefer Technique
JF  - ACS applied materials & interfaces
N2  - A synthetic protocol for the fabrication of ultrathin polymeric films containing the enzyme 2-deoxy-D-ribose-5-phosphate aldolase from Escherichia coli (DERA(EC)) is presented. Ultrathin enzymatically active films are useful for applications in which only small quantities of active material are needed and at the same time quick response and contact times without diffusion limitation are wanted. We show how DERA as an exemplary enzyme can be immobilized in a thin polymer layer at the air-water interface and transferred to a suitable support by the Langmuir-Schaefer technique under full conservation of enzymatic activity. The polymer in use is a poly(N-isopropylacrylamide-co-N-2-thiolactone acrylamide) (P(NIPAAm-co-TlaAm)) statistical copolymer in which the thiolactone units serve a multitude of purposes including hydrophobization of the polymer, covalent binding of the enzyme and the support and finally cross-linking of the polymer matrix. The application of this type of polymer keeps the whole approach simple as additional cocomponents such as cross-linkers are avoided.
KW  - Langmuir-Schaefer
KW  - enzyme immobilization
KW  - 2-deoxy-D-ribose-5-phosphate aldolase
KW  - polymeric thin film
KW  - poly(N-isopropylacrylamide)
KW  - thiolactone
Y1  - 2017
U6  - https://doi.org/10.1021/acsami.6b13632
SN  - 1944-8244
VL  - 9
SP  - 8317
EP  - 8326
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Rosencrantz, Ruben R.
A1  - Vu Hoa Nguyen, 
A1  - Park, Hyunji
A1  - Schulte, Christine
A1  - Böker, Alexander
A1  - Schnakenberg, Uwe
A1  - Elling, Lothar
T1  - Lectin binding studies on a glycopolymer brush flow-through biosensor by localized surface plasmon resonance
JF  - Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry and Analusis
N2  - A localized surface plasmon resonance biosensor in a flow-through configuration was applied for investigating kinetics of lectin binding to surface-grafted glycopolymer brushes. Polycarbonate filter membranes with pore sizes of 400 nm were coated with a 114-nm thick gold layer and used as substrate for surface-initiated atom-transfer radical polymerization of a glycomonomer. These grafted from glycopolymer brushes were further modified with two subsequent enzymatic reactions on the surface to yield an immobilized trisaccharide presenting brush. Specific binding of lectins including Clostridium difficile toxin A receptor domain to the glycopolymer brush surface could be investigated in a microfluidic setup with flow-through of the analytes and transmission surface plasmon resonance spectroscopy.
KW  - Localized surface plasmon resonance
KW  - Glycopolymer brush
KW  - Microfluidics
KW  - Bacterial toxin
KW  - Glycosyltransferase
KW  - Biosensors
Y1  - 2016
U6  - https://doi.org/10.1007/s00216-016-9667-9
SN  - 1618-2642
SN  - 1618-2650
VL  - 408
SP  - 5633
EP  - 5640
PB  - Springer
CY  - Heidelberg
ER  -