Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
Plenarvorträge - DPG-Tagungen
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Arbeitskreis Biologische Physik Freitag<br />
to vesicles, which are homogenously filled membrane shells. The bending<br />
rigidity κ of the membrane and the molecular interaction with external<br />
substances have an important influence on the cell morphology and<br />
the cell’s adhesion behavior. Rather few attention has been paid in the<br />
past to the influence of thermal fluctuations on the adhesion behavior.<br />
With the help of Monte Carlo simulations we study the behavior of a<br />
one-component vesicle adhered to a substrate at finite temperature. The<br />
adhesion behavior of vesicles was studied systematically as a function of<br />
temperature, potential depth and potential width. For high enough adhesion<br />
strength the contact area of the vesicle goes linear with T/κ. This<br />
behavior can be justified by an analytic approach. Further, a master equation<br />
has been derived which describes all our simulation results. Thus, by<br />
measuring the adhesion area one can derive the adhesion strength from<br />
κ or vice versa.<br />
AKB 50.49 Fr 10:30 B<br />
Morphogen transport by planar transcytosis — •Tobias<br />
Bollenbach 1 , Karsten Kruse 1 , Periklis Pantazis 2 , Marcos<br />
González-Gaitán 2 , and Frank Jülicher 1 — 1 MPI for Physics<br />
of Complex Systems, Nöthnitzerstr. 38, 01187 Dresden — 2 MPI for<br />
Molecular Cell Biology and Genetics, Pfotenhauerstr. 108, 01307<br />
Dresden<br />
Morphogens are signaling molecules that play a key role in development.<br />
They spread from a restricted source into an adjacent target tissue<br />
forming a concentration gradient therein. The fate of cells in the target<br />
tissue is determined by the local concentration of such morphogens.<br />
So far, the dominant mechanism by which morphogens are transported<br />
through the tissue has not been clearly identifed. While diffusion through<br />
the extracellular space is a possibility, recent in vivo experiments on the<br />
morphogen Dpp in the fruit fly Drosophila provide evidence for an active<br />
transport mechanism that was termed “planar transcytosis”. Here,<br />
a theoretical description of this transport mechanism is presented. As a<br />
consequence of nonlinearities in the current, this transport phenomenon<br />
exhibits rich behavior. We compare our description to experimental observations<br />
and aim at a quantitative description of morphogen transport.<br />
AKB 50.50 Fr 10:30 B<br />
Kinetics of salivary protein adsorption — •Anthony Quinn, Hubert<br />
Mantz, and Karin Jacobs — Experimental Physics, Saarland<br />
University, POB 151 150, 66041 Saarbrücken<br />
Exposure to saliva in the oral cavity results in the formation of a layer<br />
of proteins and related biopolymers on all solid surfaces, known as an<br />
acquired salivary pellicle. Pellicle formation occurs immediately and is<br />
considered to be complete within 1-2 hours, with a thickness of approximately<br />
1 micron. Bacteria in the saliva then selectively attaches to the<br />
pellicle (dependent on the surface characteristics of the bacteria and the<br />
specific proteins), marking the onset of plaque formation. Observations<br />
of plaque, which is known to play a crucial role in the development of<br />
oral diseases, reveal an enhanced or diminished growth dependent on the<br />
supporting substrate. This research therefore aims to identify the mechanisms<br />
for salivary protein adsorption at solid-liquid interfaces, with the<br />
intention of optimising the biocompatibility of dental replacement materials,<br />
and reduce the incidence of disease inducing plaque formation.<br />
In-situ ellipsometry is utilized to follow the adsorption kinetics of purified<br />
protein solutions, and the competitive adsorption from mixed protein<br />
solutions on a series of tailored substrates. The physicochemical composition<br />
of these tailored surfaces is carefully controlled and fully characterised<br />
via AFM and wettability analysis, enabling the structural and<br />
interfacial tension components to be identified respectively.<br />
AKB 50.51 Fr 10:30 B<br />
Studying cell adhesion with holographic optical tweezers —<br />
•Jennifer E. Curtis and Joachim P. Spatz — Biophysical Chemistry,<br />
Institiute for Physical Chemistry, University of Heidelberg<br />
Most cells must adhere to a surface if they are to survive. Cell adhesion<br />
involves the orchestration of a stunning number of proteins to form focal<br />
complexes, the physical link between the surface, plasma membrane, and<br />
the stabilizing cytoskeleton. Despite this complexity, simple mechanical<br />
force plays a unique role in the initiation of cell adhesion. The activities<br />
of cells depend sensitively on the mechanical nature of their adhesion<br />
substrate. When too soft, a cell cannot adhere and focal contacts fail to<br />
form. When too hard, unphysiological actin stress fibers plague the cell.<br />
Using holographic optical tweezers, we present dozens of microspheres<br />
directly above the surface of a fibroblast to study the dynamics of focal<br />
adhesion formation. We also study how the initial position and the force<br />
exerted by the optical traps influences the final binding strength, the total<br />
time for full binding, and the subsequent motion of the bead. Lastly,<br />
we hope to elucidate the role of the hylauronic acid layer in focal adhesion<br />
by studying binding dynamics with and without this sticky sugar<br />
matrix.<br />
AKB 50.52 Fr 10:30 B<br />
Electronic Transport in DNA — •Daphne Klotsa, Rudolf A.<br />
Römer, and Matthew S. Turner — Department of Physics, University<br />
of Warwick, CV4 7AL, Coventry, United Kingdom<br />
Based on a theoretical model proposed by Cuniberti et al. [1] we are focusing<br />
on electron localisation along the Deoxyribose Nucleic Acid (DNA)<br />
double helix, using a tight-binding Hamiltonian. The possibility that this<br />
organic super molecule might facilitate electron transfer, along the overlapping<br />
π-orbitals [2], as a means of signalling other biomolecules, has<br />
led us to perform calculations varying the DNA sequences. We have performed<br />
simulations on random sequence, λ- and telomeric DNA. For the<br />
first two the resulting localisation lengths as functions of energy and<br />
disorder show similar behaviour whereas the latter — specific sequence<br />
DNA — gives significantly larger localisation lengths. In all cases an energy<br />
bandgap, indicating semiconducting behaviour, has been observed.<br />
Counter intuitively, for random absorption of Sodium (Na) atoms onto<br />
the backbone, preliminary results have shown localisation lengths to increase<br />
with increasing disorder. A “moving window”technique will be<br />
used in order to assess whether particular shorter fragments of a sequence<br />
behave differently, whose contribution would inevitably be smoothed out<br />
when the whole sequence is considered. Finally, we are looking at another<br />
theoretical way of modelling DNA’s complex structure and properties,<br />
the “ladder model”— an extension of the aforementioned model.<br />
[1] G. Cuniberti, et al., Phys. Rev. B 65, 241314 (2002)<br />
[2] P. J. de Pablo, et al. Phys. Rev. Letters 85, 4992 (2000)<br />
AKB 50.53 Fr 10:30 B<br />
Interlamellar variation of the 3D bone nanostructure<br />
— •Wolfgang Wagermaier 1 , Himadri S. Gupta 1 , Paul<br />
Roschger 2 , Manfred Burghammer 3 , Klaus Klaushofer 2 , and<br />
Peter Fratzl 1 — 1 MPI-KGF, Biomaterials, Potsdam, Germany —<br />
2 LBIO, 4th Med. Dept., Hanusch Hospital and UKH Meidling, Vienna,<br />
Austria — 3 ESRF, Grenoble, France<br />
Bone is a biomineralised tissue structurally optimised for its biological<br />
function. Diverse fibrillar array types - at the 0.1 - 10 micrometer range,<br />
adapted to their local load bearing requirements - bring about this optimisation.<br />
We used a novel combination of synchrotron scanning small<br />
angle X-ray scattering combined with sample rotation to see how the 3D<br />
mineralised nanostructure varied in bone with inter-lamellar resolution.<br />
Several osteons around blood vessels in compact bone were scanned over<br />
a total area of typically (100 x 100 micrometer) and a simple physical<br />
model was developed to reconstruct the 3D orientation. Our results show<br />
mineral crystallite orientation has a fiber texture within single lamellae,<br />
but shows a smooth spatial variation around the cylindrical core of the<br />
osteon. Biomechanically the variation may be explained in terms of the<br />
in-vivo stresses developed around osteonal channels, requiring a composite<br />
structure able to resist large deformation and bending stresses. Our<br />
results provide insights into how bone is designed at the lamellar level<br />
for its biophysical function.<br />
AKB 50.54 Fr 10:30 B<br />
Fusion of giant vesicles observed with time resolution below<br />
a millisecond — •Rumiana Dimova 1 , Christopher Haluska 1 ,<br />
Karin A. Riske 1 , Valerie Marchi-Arztner 1 , and Reinhard<br />
Lipowsky 2 — 1 Max Planck Institute of Colloids and Interfaces, Am<br />
Muehlenberg 1, 14476 Golm, Germany — 2 Universite de Rennes, Rennes<br />
France<br />
Using optical microscopy and a high speed camera, we are able to<br />
record the fusion process with a high temporal resolution of 100us. We<br />
consider two model membrane systems: functionalized giant unilamellar<br />
vesicles (GUVs) in the presence of multivalent ions, and lipid or polymer<br />
GUVs subjected to electrical pulses.<br />
In the first case, we functionalize lecithin membranes with synthetic<br />
molecules bearing a ligand, which form complexes with Eu3+ (2:1). Micropipettes<br />
are used to manipulate GUV’s and inject Eu3+ solution in<br />
the contact zone between two vesicles. The injections induce adhesion<br />
and formation of intermembrane complexes, followed by fusion. This system<br />
has the potential to mimic the action of fusogenic SNARE proteins