{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T03:00:49Z","timestamp":1784257249917,"version":"3.55.0"},"reference-count":19,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2023,11,30]],"date-time":"2023-11-30T00:00:00Z","timestamp":1701302400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2024,4]]},"abstract":"<jats:p>Alpha\u2010synuclein (\u03b1Syn) is a small presynaptic protein (14\u2009kDa) that is involved in synucleinopathies including Parkinson's disease (PD). In its native state, the \u03b1Syn monomer exists in an unfolded state, and its folding is highly dependent on variations of environmental conditions, mutations and interactions with endogenous and\/or exogenous molecules. Recently, there is increasing evidence for a direct interplay between \u03b1Syn and microtubules (MTs), whose defects are linked to neurodegenerative diseases, such as PD. Understanding the correlation between \u03b1Syn and MTs could be fundamental for the correct comprehension of the undergoing mechanisms of PD. Hence, we chemically synthesized a library of peptides, deriving from both native and PD mutated sequences of the N\u2010terminal domain of \u03b1Syn. Their secondary structure was characterized by circular dichroism and Fourier transform infrared (FTIR) experiments, in order to evaluate the effect of PD mutations. Finally, the kinetics of polymerizing tubulin in vitro in the presence of the peptides was evaluated.<\/jats:p>","DOI":"10.1002\/psc.3556","type":"journal-article","created":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T05:28:52Z","timestamp":1701408532000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Breaking down and building up alpha\u2010synuclein: An insight on its N\u2010terminal domain"],"prefix":"10.1002","volume":"30","author":[{"given":"Kaliroi","family":"Peqini","sequence":"first","affiliation":[{"name":"DISFARM, Dipartimento di Scienze Farmaceutiche, Sezione Chimica Generale e Organica \u201cA. Marchesini\u201d Universit\u00e0 degli Studi di Milano  Milan Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simone","family":"Attanasio","sequence":"additional","affiliation":[{"name":"Department of Biosciences Universit\u00e0 degli Studi di Milano  Milan Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucia","family":"Feni","sequence":"additional","affiliation":[{"name":"DISFARM, Dipartimento di Scienze Farmaceutiche, Sezione Chimica Generale e Organica \u201cA. 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