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| 001 | 1033770 | ||
| 005 | 20241212210725.0 | ||
| 024 | 7 | _ | |a 10.1101/2024.01.10.574993 |2 doi |
| 024 | 7 | _ | |a 10.34734/FZJ-2024-06611 |2 datacite_doi |
| 037 | _ | _ | |a FZJ-2024-06611 |
| 100 | 1 | _ | |a Lenton, Samuel |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Amyloid Morphology is Encoded in H-bonds and Electrostatics Interactions Ruling Protein Phase Separation |
| 260 | _ | _ | |c 2024 |
| 336 | 7 | _ | |a Preprint |b preprint |m preprint |0 PUB:(DE-HGF)25 |s 1734000571_5474 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a WORKING_PAPER |2 ORCID |
| 336 | 7 | _ | |a Electronic Article |0 28 |2 EndNote |
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| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a Output Types/Working Paper |2 DataCite |
| 520 | _ | _ | |a We report the mechanisms by which H-bonds and electrostatic interactions in ion- protein systems determine phase separation and amyloid formation. Using microscopy, small-angle X-ray scattering and atomistic molecular dynamics simulations, we found that anions interacting with insulin induced phase separation by neutralising the pro- tein charge and forming H-bonds between insulin molecules. The same interaction was responsible for an enhanced insulin conformational stability and resistance to oligomeri- sation. Under aggregation conditions, the anion-protein interaction translated into the activation of a coalescence process, leading to amyloid-like microparticles. This reaction is alternative to conformationally-driven pathways, which give rise to amyloid-like fibrils and core-shell structures, and occur instead in the absence of ion-protein binding. Our findings depict a scenario in which common interactions dictated both phase separation at low temperatures and the occurrence of heterogeneity in the amyloid morphology at high temperatures, similar to what has been reported for protein crystallisation. |
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| 700 | 1 | _ | |a Chaaban, Hussein |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Khaled, Mohammed |0 P:(DE-Juel1)180535 |b 2 |
| 700 | 1 | _ | |a Van de Weert, Marco |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 4 |e Corresponding author |u fzj |
| 700 | 1 | _ | |a Fodera, Vito |0 P:(DE-HGF)0 |b 5 |
| 773 | _ | _ | |a 10.1101/2024.01.10.574993 |p 40 |t bioRxiv |y 2024 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1033770/files/BioRxiv_2024.01.10.574993v1.full.pdf |y OpenAccess |
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