Double distinguished iNANO Lecture by Dr. Niki Baccile and Associate Professor Annette Eva Langkilde

Biosurfactant metallogels, current status and perspectives & Self-association and stacking of CaMKllα hub domains

Info about event

Time

Friday 7 February 2025,  at 10:00 - 11:00

Location

iNANO AUD (1593-012)

Organizer

Daniel Otzen og Jan Skov Pedersen

PhD, full-time CNRS Reseacher Niki Baccile, Sorbonne Université, Paris, France

Biosurfactant metallogels, current status and perspectives

The talk show the non-conventional use of a microbial glycolipid detergent in the field of nanoscience, namely the development of metallogels.

This presentation will show a non-conventional use of the so-called microbial glycolipid biosurfactants, biobased amphiphiles with great potential in many fields, including nanoscience. [1] Here, it will be shown how glycolipids can be used to prepare metallogels with a number of cations. [2] Current development shows the possibility to obtain a long-range ordered two-dimensional, highly anisotropic, array of monodispersed 2.8 nm nanoparticles (see figure) or even nanowires. When controlled, the three-dimensional organization combined with the metal wires can lead to electron-conductive gels, as probed by impedance spectroscopy.

The present work shows a simple and convenient way to prepare, in a single step in water, biobased metallogels with electron conductive properties. However, tuning the nanostructure composition and morphology could tune the metallogel properties.

 

Associate Professor Annette Eva Langkilde, University of Copenhagen

Self-association and stacking of CaMKIIα hub domains

Calcium/calmodulin-dependent protein kinase II subtype alpha (CaMKIIα) holds a key role in synaptic plasticity, learning, and memory. The discovery of a γ-hydroxybutyrate (GHB) binding site in the CaMKIIa hub domain [1], has led to investigation of GHB analogues as potential therapeutic compounds. In a recent study [2] one such analogue, 2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid (PIPA), was shown to modulate CaMKIIα stability and activity. The CaMKIIα is a multimeric protein, existing in dodecameric and/or tetradecamic assemblies. The structural influence of ligand binding was investigated and small-angle scattering experiments revealed a highly ordered ligand-induced self-association of the CaMKIIa hub domains.

I will present the discovery and modelling of these self-associated stacks - the behindthe-scenes story - as well as the potential impact on the regulation of activity.

 

Host: Daniel Otzen & Jan Skov Pedersen

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