guest ::
| Home > Publications database > Insulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation > print |
| Home > Publications database > Insulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation > print |
| 001 | 1035302 | ||
| 005 | 20250310131247.0 | ||
| 024 | 7 | _ | |a 10.1016/j.jcis.2024.12.058 |2 doi |
| 024 | 7 | _ | |a 0021-9797 |2 ISSN |
| 024 | 7 | _ | |a 1095-7103 |2 ISSN |
| 024 | 7 | _ | |a 10.34734/FZJ-2025-00360 |2 datacite_doi |
| 024 | 7 | _ | |a 39778472 |2 pmid |
| 024 | 7 | _ | |a WOS:001407781400001 |2 WOS |
| 037 | _ | _ | |a FZJ-2025-00360 |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Lenton, Samuel |0 0009-0005-9244-9538 |b 0 |
| 245 | _ | _ | |a Insulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation |
| 260 | _ | _ | |a Amsterdam [u.a.] |c 2025 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1736434768_29027 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Ion-protein interactions regulate biological processes and are the basis of key strategies of modulating protein phase diagrams and stability in drug development. Here, 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, circular dichroism and atomistic molecular dynamics (MD) simulations, we found that anions specifically interacting with insulin induced phase separation by neutralising the protein charge and forming H-bond bridges between insulin molecules. The same interaction was responsible for an enhanced insulin conformational stability and resistance to oligomerisation. 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, giving rise to elongated amyloid-like fibrils and occurs in the absence of preferential ion-protein binding. Our findings depict a unifying scenario in which common interactions dictated both phase separation at low temperatures and the occurrence of pronounced heterogeneity in the amyloid morphology at high temperatures, similar to what has previously been reported for protein crystal growth. |
| 536 | _ | _ | |a 5241 - Molecular Information Processing in Cellular Systems (POF4-524) |0 G:(DE-HGF)POF4-5241 |c POF4-524 |f POF IV |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, Journals: juser.fz-juelich.de |
| 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 0000-0002-8530-6441 |b 3 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 4 |e Corresponding author |
| 700 | 1 | _ | |a Foderà, Vito |0 0000-0003-2855-0568 |b 5 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.jcis.2024.12.058 |g Vol. 683, p. 1175 - 1187 |0 PERI:(DE-600)1469021-4 |p 1175 - 1187 |t Journal of colloid and interface science |v 683 |y 2025 |x 0021-9797 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1035302/files/1-s2.0-S0021979724029102-main.pdf |y OpenAccess |
| 909 | C | O | |o oai:juser.fz-juelich.de:1035302 |p openaire |p open_access |p VDB |p driver |p dnbdelivery |
| 910 | 1 | _ | |a Forschungszentrum Jülich |0 I:(DE-588b)5008462-8 |k FZJ |b 4 |6 P:(DE-Juel1)132024 |
| 913 | 1 | _ | |a DE-HGF |b Key Technologies |l Natural, Artificial and Cognitive Information Processing |1 G:(DE-HGF)POF4-520 |0 G:(DE-HGF)POF4-524 |3 G:(DE-HGF)POF4 |2 G:(DE-HGF)POF4-500 |4 G:(DE-HGF)POF |v Molecular and Cellular Information Processing |9 G:(DE-HGF)POF4-5241 |x 0 |
| 914 | 1 | _ | |y 2025 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0160 |2 StatID |b Essential Science Indicators |d 2023-10-21 |
| 915 | _ | _ | |a Creative Commons Attribution CC BY 4.0 |0 LIC:(DE-HGF)CCBY4 |2 HGFVOC |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0113 |2 StatID |b Science Citation Index Expanded |d 2023-10-21 |
| 915 | _ | _ | |a OpenAccess |0 StatID:(DE-HGF)0510 |2 StatID |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |d 2024-12-20 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |d 2024-12-20 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Clarivate Analytics Master Journal List |d 2024-12-20 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1150 |2 StatID |b Current Contents - Physical, Chemical and Earth Sciences |d 2024-12-20 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |d 2024-12-20 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0600 |2 StatID |b Ebsco Academic Search |d 2024-12-20 |
| 915 | _ | _ | |a Peer Review |0 StatID:(DE-HGF)0030 |2 StatID |b ASC |d 2024-12-20 |
| 920 | _ | _ | |l yes |
| 920 | 1 | _ | |0 I:(DE-Juel1)IBI-7-20200312 |k IBI-7 |l Strukturbiochemie |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 980 | 1 | _ | |a FullTexts |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|