Double Distinguished iNANO Lectures by Raffaele Mezzenga, ETH Zurich & David Alsteens, Université catholique de Louvain
10:15 Amyloid-Metal Hybrids for Health and Environmental Remediation 10:35 Deciphering the role of glycans as attachment factors in viral infection using AFM
Info about event
Time
Location
iNANO AUD, 1593-012
Organizer
10:15 Prof. Prof. Dr. Raffaele Mezzenga, ETH Zurich, Switzerland
Amyloid-Metal Hybrids for Health and Environmental Remediation
Amyloid fibrils interact with metal ions via metal-ligand supramolecular interactions whose energy is of the order of tens to hundreds of KBT. The occurrence and abundance of the 20 essential amino acids in food-based amyloid fibrils derived from inexpensive animal and plant proteins, including from food waste and agricultural side streams, combined with the extreme aspect ratio of the amyloids, allow for an affordable, yet universal toolbox to produce multifunctional hybrids which can serve in a multitude of applications and technologies. In this talk I will provide several examples of food amyloid fibrils interacting with metal ions and nanoparticles for both health and environmental remediation, some of which have made it into real technologies. Taking b-lactoglobulin amyloids as a model amyloid system derived from whey, a by-product of cheese making process, I will show how metal ions can be adsorbed from water and wastewater solutions by amyloid-based filters for water purification purposes, or how gold ions can be adsorbed and processed from amyloid aerogels to recycle gold from e-waste; I will also show how iron atoms can be coordinated to blactoglobulin amyloids to deliver highly bioavailable Fe(ii) for iron fortification, or to design hydrogels capable of performing cascade enzymatic reactions for alcohol detoxification in vivo.
10:50 Prof. Dr. David Alsteens, NanoBioPhysics Lab, Université catholique de Louvain, Belgium
Deciphering the role of glycans as attachment factors in viral infection using AFM
During the last three decades, a series of key technological improvements turned atomic force microscopy (AFM) into a nanoscopic laboratory to directly observe and chemically characterize molecular and cellular biological systems under physiological conditions. I will present the key technological improvements that enable us to apply AFM as analytical laboratory to observe and quantify living biological systems at the nanoscale. I will report the use of advanced FD-based technology combined with chemically functionalized tips to probe the localization and interactions of chemical and biological sites on single native proteins and on living cells at high-resolution. I will present how an atomic force and confocal microscopy set-up allows the surface receptor landscape of cells to be imaged and the virus binding events within the first millisecond of contact with the cell to be mapped at high resolution (<50 nm). I will also highlight theoretical approaches to contour the free-energy landscape of early binding events between virus and cell surface receptors.