Spatially constrained disulfide bond shuffling delays insulin aggregation and enhances neurotoxicity
Abstract Disulfide bond shuffling (DBS) critically influences protein aggregation and stability, yet its spatial constraints and biological implications remain poorly understood. Here, we demonstrate that insulin undergoes DBS within an extended spatial range up to ~19 Å, generating heterogeneous cr...
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| Autori principali: | , , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Portfolio
2025-07-01
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| Serie: | Nature Communications |
| Accesso online: | https://doi.org/10.1038/s41467-025-62257-0 |
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