20.500.12556/RUL-138811 A new fibrillization mechanism of ß-lactoglobulin in glycine solutions Even though amyloid aggregates were discovered many years ago the mechanism of their formation is still a mystery. Because of their connection to many of untreatable neurodegenerative diseases the motivation for finding a common aggregation path is high. We report a new high heat induced fibrillization path of a model protein β-lactoglobulin (BLG) when incubated in glycine instead of water at pH 2. By combining atomic force microscopy (AFM), transmission emission microscopy (TEM), dynamic light scattering (DLS) and circular dichroism (CD) we predict that the basic building blocks of fibrils made in glycine are not peptides, but rather spheroid oligomers of different height that form by stacking of ring-like structures. Spheroid oligomers linearly align to form fibrils by opening up and combining. We suspect that glycine acts as an hydrolysation inhibitor which consequently promotes a different fibrillization path. By combining the known data on fibrillization in water with our experimental conclusions we come up with a new fibrillization scheme for BLG. We show that by changing the fibrillization conditions just by small changes in buffer composition can dramatically change the aggregation pathway and the effect of buffer shouldn't be neglected. Fibrils seen in our study are also gaining more and more attention because of their pore-like structure and a possible cytotoxic mechanism by forming pernicious ion-channels. By preparing them in a simple model system as BLG we opened a new way to study their formation. ß-lactoglobulin fibrillization mechanism buffer specific effects spheroid oligomers ß-laktoglobulin fibrilizacijski mehanizem pufer specifični efekt sferoidni oligomeri true false true Angleški jezik Slovenski jezik Članek v reviji 2022-08-19 09:05:02 2022-08-19 09:05:03 2022-09-21 09:49:56 0000-00-00 00:00:00 2022 0 0 Str. 414-425 Vol. 216 1 Sep. 2022 0000-00-00 Zaloznikova Objavljeno NiDoloceno 0000-00-00 0000-00-00 0000-00-00 577.322 0141-8130 10.1016/j.ijbiomac.2022.06.182 114740483 1-s2.0-S0141813022013952-main.pdf 1-s2.0-S0141813022013952-main.pdf 1 2B3DCAB209B229AF79D73B9A76246216 6b85ba16c57914dbaf407aeab529d4337a94de1c3805f03004b736c5c69e2a9e ccec5bae-1f8e-11ed-92af-00155dcfd717 https://repozitorij.uni-lj.si/Dokument.php?lang=slv&id=159268 https://www.sciencedirect.com/science/article/pii/S0141813022013952 1 3c25da43-1f8d-11ed-92af-00155dcfd717 https://repozitorij.uni-lj.si/Dokument.php?lang=slv&id=159267 Fakulteta za kemijo in kemijsko tehnologijo 0 0 0