TY  - JOUR
A1  - Ghobadi, Ehsan
A1  - Heuchel, Matthias
A1  - Kratz, Karl
A1  - Lendlein, Andreas
T1  - Atomistic simulation of the shape-memory effect in dry and water swollen Poly[(rac-lactide)-co-glycolide] and copolyester urethanes thereof
JF  - Macromolecular chemistry and physics
N2  - An atomistic molecular dynamics simulation approach is applied to model the influence of urethane linker units as well as the addition of water molecules on the simulated shape-memory properties of poly[(rac-lactide)-co-glycolide] (PLGA) and PLGA-based copolyester urethanes comprising different urethane linkers. The shape-memory performance of these amorphous packing models is explored in a simulated heating-deformation-cooling-heating procedure. Depending on the type of incorporated urethane linker, the mechanical properties of the dry copolyester urethanes are found to be significantly improved compared with PLGA, which can be attributed to the number of intermolecular hydrogen bonds between the urethane units. Good shape-memory properties are observed for all the modeled systems. In the dry state, the shape fixation is found to be improved by implementation of urethane units. After swelling of the copolymer models with water, which results in a reduction of their glass transition temperatures, the relaxation kinetics during unloading and shape recovery are found to be substantially accelerated.
KW  - molecular dynamics simulations
KW  - polyesterurethane
KW  - shape-memory effect
Y1  - 2014
U6  - https://doi.org/10.1002/macp.201300507
SN  - 1022-1352
SN  - 1521-3935
VL  - 215
IS  - 1
SP  - 65
EP  - 75
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - GEN
A1  - Kunstmann, Ruth Sonja
A1  - Engström, Olof
A1  - Wehle, Marko
A1  - Widmalm, Göran
A1  - Santer, Mark
A1  - Barbirz, Stefanie
T1  - Increasing the affinity of an O-Antigen polysaccharide binding site in Shigella flexneri bacteriophage Sf6 tailspike protein
T2  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - Broad and unspecific use of antibiotics accelerates spread of resistances. Sensitive and robust pathogen detection is thus important for a more targeted application. Bacteriophages contain a large repertoire of pathogen-binding proteins. These tailspike proteins (TSP) often bind surface glycans and represent a promising design platform for specific pathogen sensors. We analysed bacteriophage Sf6 TSP that recognizes the O-polysaccharide of dysentery-causing Shigella flexneri to develop variants with increased sensitivity for sensor applications. Ligand polyrhamnose backbone conformations were obtained from 2D H-1,H-1-trNOESY NMR utilizing methine-methine and methine-methyl correlations. They agreed well with conformations obtained from molecular dynamics (MD), validating the method for further predictions. In a set of mutants, MD predicted ligand flexibilities that were in good correlation with binding strength as confirmed on immobilized S. flexneri O-polysaccharide (PS) with surface plasmon resonance. In silico approaches combined with rapid screening on PS surfaces hence provide valuable strategies for TSP-based pathogen sensor design.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1417 
KW  - carbohydrates
KW  - molecular dynamics simulations
KW  - NMR spectroscopy
KW  - protein-carbohydrate interactions
KW  - surface plasmon resonance
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-519418
SN  - 1866-8372
IS  - 32
ER  - 
TY  - JOUR
A1  - Kunstmann, Ruth Sonja
A1  - Engström, Olof
A1  - Wehle, Marko
A1  - Widmalm, Göran
A1  - Santer, Mark
A1  - Barbirz, Stefanie
T1  - Increasing the affinity of an O-Antigen polysaccharide binding site in Shigella flexneri bacteriophage Sf6 tailspike protein
JF  - Chemistry – A European Journal
N2  - Broad and unspecific use of antibiotics accelerates spread of resistances. Sensitive and robust pathogen detection is thus important for a more targeted application. Bacteriophages contain a large repertoire of pathogen-binding proteins. These tailspike proteins (TSP) often bind surface glycans and represent a promising design platform for specific pathogen sensors. We analysed bacteriophage Sf6 TSP that recognizes the O-polysaccharide of dysentery-causing Shigella flexneri to develop variants with increased sensitivity for sensor applications. Ligand polyrhamnose backbone conformations were obtained from 2D H-1,H-1-trNOESY NMR utilizing methine-methine and methine-methyl correlations. They agreed well with conformations obtained from molecular dynamics (MD), validating the method for further predictions. In a set of mutants, MD predicted ligand flexibilities that were in good correlation with binding strength as confirmed on immobilized S. flexneri O-polysaccharide (PS) with surface plasmon resonance. In silico approaches combined with rapid screening on PS surfaces hence provide valuable strategies for TSP-based pathogen sensor design.
KW  - carbohydrates
KW  - molecular dynamics simulations
KW  - NMR spectroscopy
KW  - protein-carbohydrate interactions
KW  - surface plasmon resonance
Y1  - 2020
U6  - https://doi.org/10.1002/chem.202000495
SN  - 0947-6539
SN  - 1521-3765
VL  - 26
IS  - 32
SP  - 7263
EP  - 7273
PB  - Wiley-VCH
CY  - Weinheim
ER  -