Polskie Towarzystwo Biofizyczne

The seminar will be held in a hybrid version.
We invite you to come in person and meet the Speaker 
at the Auditory of the Institute of Physics (left from the main hall).

             SEMINARIUM Z FIZYKI BIOLOGICZNEJ I BIOINFORMATYKI
         Instytutu Biochemii i Biofizyki PAN, Instytutu Fizyki PAN,
			 i Zakładu Biofizyki UW

                Wednesday, 21.05.2025, 15:15 (3.15 p.m. CET)

                               Auditory
              Intitute of Physics, Polish Academy of Sciences
                      Al. Lotników 32/46, Warszawa

                                  and

    https://zoom.us/j/91976153012?pwd=azNiMWE4UnhPN3lRQlY2UHZHOXVkQT09


   "Lipid Membrane Texture Induced by Specific Protein Binding and Receptor Clustering:
          Active Roles for Lipids in Cellular Function"

                       Jarosław Majewski, Ph. D.

    Department of Chemical & Biological Engineering at the University of New Mexico, Albuquerque, US.
    Visiting Scientist at Los Alamos National Laboratory, Los Alamos, NM, US.
    Affiliated Professor at the University of Warsaw, Poland.

                                       Bogdan Lesyng (UW)
                                       Anna Niedźwiecka (IF PAN)
                                       Piotr Zielenkiewicz (IBB)


ABSTRACT
Biological membranes are complex,
self-organized structures that define boundaries and compartmentalize space in
living matter. Composed of various lipid and protein molecules, these
responsive surfaces mediate transmembrane signaling and material transport
within the cell and with its environment. It is well known that lipid membrane
properties change as a function of composition and phase state and that
protein-lipid interactions can induce changes in the membrane’s properties and
biochemical response. Here, molecular level changes in lipid organization
induced by multivalent toxin binding were investigated using grazing incidence
X-ray diffraction. Structural changes to lipid monolayers at the air-water
interface and bilayers at the solid-water interface were studied before and
after the specific binding of cholera toxin to membrane-embedded receptors. At
biologically relevant surface pressures, protein binding perturbed lipid
packing within monolayers and bilayers resulting in topological defects and the
emergence of a new orientationally textured lipid phase. In bilayers this
altered lipid order was transmitted from the receptor-laden exterior membrane leaflet
to the inner leaflet, representing a potential mechanism for lipid-mediated
outside-in signaling by multivalent protein binding. It is further hypothesized
that cell surface micro-domains exhibiting this type of lipid order may serve
as nucleation sites for vesicle formation in clathrin-independent endocytosis
of cholera toxin.

             SEMINARIUM Z FIZYKI BIOLOGICZNEJ I BIOINFORMATYKI
         Instytutu Biochemii i Biofizyki PAN, Instytutu Fizyki PAN,
			 i Zakładu Biofizyki UW

                Wednesday, 07.05.2025, 15:15 (3.15 p.m. CET)
       

    https://zoom.us/j/91976153012?pwd=azNiMWE4UnhPN3lRQlY2UHZHOXVkQT09


                
           "Protein aggregation in biomolecular condensates: 
             the case of α-synuclein in host-guest systems"

                         Dr Wojciech Lipiński

               Department of Physical Organic Chemistry 
                Institute for Molecules and Materials 
                         Radboud University 
                     Nijmegen, The Netherlands

                                       Bogdan Lesyng (UW)
                                       Anna Niedźwiecka (IF PAN)
                                       Piotr Zielenkiewicz (IBB)


ABSTRACT
Protein aggregation, associated with multiple neurodegenerative disorders, has been
a topic of significant scientific interest for decades. However, it is only recently
that the aggregation process has been recognized as being influenced by another
biologically important phenomenon – liquid-liquid phase separation, which underlies
the formation of membraneless organelles. Investigating the role of biomolecular
condensates in protein aggregation is essential for understanding the mechanisms of
amyloid formation and for identifying new strategies for treatment and prevention.
In the talk, I will discuss the key factors through which the physical and chemical
environment of a condensate can influence protein aggregation. I will also focus on
the specific case of α-synuclein (one of the archetypal amyloid-forming proteins),
its aggregation in the presence of model liquid condensates, and the role of
condensate interfaces in this process.

References:
B.S. Visser, W.P. Lipiński, E. Spruijt “The role of biomolecular condensates in
protein aggregation” Nature Reviews Chemistry, 2024,
https://doi.org/10.1038/s41570-024-00635-w
W.P. Lipiński, B.S. Visser, I. Robu, M.A.A. Fakhree, S. Lindhoud, M.M.A.E.
Claessens, E. Spruijt “Biomolecular condensates can both accelerate and suppress
aggregation of α-synuclein” Science Advances, 2022,
https://doi.org/10.1126/sciadv.abq6495
B.S. Visser, M.H.I. van Haren, W.P. Lipiński, K.A. van Leijenhorst-Groener, M.M.A.E.
Claessens, M.V.A. Queirós, C.H.I. Ramos, J. Eeftens, E. Spruijt, “Controlling
interfacial protein adsorption, desorption and aggregation in biomolecular
condensates” bioRxiv preprint, 2024, https://doi.org/10.1101/2024.10.20.619145

Dear Participants,

The seminar will be held in a hybrid version. We invite you to come in person and meet the Speaker at the Auditory of the Institute of Physics (left from the main hall).

SEMINARIUM Z FIZYKI BIOLOGICZNEJ I BIOINFORMATYKI
Instytutu Biochemii i Biofizyki PAN, Instytutu Fizyki PAN,
i Zakładu Biofizyki UW

Wednesday, 23.04.2025, 15:15 (3.15 p.m. CET)

Auditory

Intitute of Physics, Polish Academy of Sciences
Al. Lotników 32/46, Warszawa

and

https://zoom.us/j/91976153012?pwd=azNiMWE4UnhPN3lRQlY2UHZHOXVkQT09

„Synthesis of multifunctional magnetite-based nanoparticles for anticancer applications”

Dr inż. Adrian Radoń
Łukasiewicz Research Network – Institute of Non-Ferrous Metals, Gliwice, Poland

Bogdan Lesyng (UW)
Anna Niedźwiecka (IF PAN)
Piotr Zielenkiewicz (IBB)

Zapraszamy na posiedzenie naukowe Wrocławskiego Oddziału Polskiego Towarzystwa Biofizycznego współorganizowane z Komisją Chemii i Fizyki w Biologii i Medycynie Wrocławskiego Oddziału PAN.

Podczas posiedzenia wykład  pt. „W poszukiwaniu mechanizmów funkcjonowania wybranych przedstawicieli rodziny czynników transkrypcyjnych bHLH-PAS” wygłosi dr hab. inż. Beata Greb-Markiewicz, prof. uczelni z Katedry Biochemii, Biologii Molekularnej i Biotechnologii, Wydziału Chemicznego, Politechniki Wrocławskiej (beata.greb-markiewicz@pwr.edu.pl).

Posiedzenie odbędzie się w dniu 9.04.2025 w sali 236, w budynku A2 Uniwersytetu Przyrodniczego we Wrocławiu, ul. Norwida 25 (II piętro).
Łączę wyrazy szacunku,
Sylwia Cyboran-Mikołajczyk