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April 1, 2026ACS Chemical NeuroscienceOpen Access

Transient Interactions of α-Synuclein N- and C-Termini

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Authors

LOLei Ortigosa-PascualNCNoemi Ferrante CarranteKBKatja Bernfur

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Overview

Demonstrates transient interactions of alpha-synuclein in various conformational states, suggesting key insights into its role in neurodegenerative diseases.

Key Points

  • The research aims to investigate the transient interactions between the N- and C-termini of alpha-synuclein and their implications in protein behavior.
  • Employed photoinduced cross-linking of unmodified proteins (PICUP)
  • Utilized tyrosine-to-phenylalanine mutations to block reactivity of specific amino acids
  • Examined cross-linking in various states: monomers, oligomers, and fibrils
  • Identified internal contacts in monomers and intermonomer contacts in oligomers
  • Cross-linking between C-terminal regions persists on membranes while internal cross-linking is blocked
  • In fibrils, cross-linking mainly occurs between adjacent C-termini, significantly reduced compared to other states

Cite This Study

Ortigosa-Pascual et al. (2026) studied this question.

synapsesocial.com/papers/69cd79915652765b073a6818https://doi.org/10.1021/acschemneuro.6c00108
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