{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,21]],"date-time":"2026-02-21T07:18:51Z","timestamp":1771658331492,"version":"3.50.1"},"reference-count":62,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2021,12,10]],"date-time":"2021-12-10T00:00:00Z","timestamp":1639094400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>\u03b1-synuclein (\u03b1-syn) is a major culprit of Parkinson\u2019s disease (PD), although lipoprotein metabolism is very important in the pathogenesis of PD. \u03b1-syn was expressed and purified using the pET30a expression vector from an E. coli expression system to elucidate the physiological effects of \u03b1-syn on lipoprotein metabolism. The human \u03b1-syn protein (140 amino acids) with His-tag (8 amino acids) was expressed and purified to at least 95% purity. Isoelectric focusing gel electrophoresis showed that the isoelectric point (pI) of \u03b1-syn and apoA-I were pI = 4.5 and pI = 6.4, respectively. The lipid-free \u03b1-syn showed almost no phospholipid-binding ability, while apoA-I showed rapid binding ability with a half-time (T1\/2) = 8 \u00b1 0.7 min. The \u03b1-syn and apoA-I could be incorporated into the reconstituted HDL (rHDL, molar ratio 95:5:1:1, palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC):cholesterol:apoA-I:\u03b1-syn with the production of larger particles (92 \u00c5) than apoA-I-rHDL (86 and 78 \u00c5) and \u03b1-syn-rHDL (65 \u00c5). An rHDL containing both apoA-I and \u03b1-syn showed lower \u03b1-helicity around 45% with a red shift of the Trp wavelength maximum fluorescence (WMF) from 339 nm, while apoA-I-HDL showed 76% \u03b1-helicity and 337 nm of WMF. The denaturation by urea addition showed that the incorporation of \u03b1-syn in rHDL caused a larger increase in the WMF than apoA-I-rHDL, suggesting that the destabilization of the secondary structure of apoA-I by the addition of \u03b1-syn. On the other hand, the addition of \u03b1-syn induced two-times higher resistance to rHDL glycation at apoA-I:\u03b1-syn molar ratios of 1:1 and 1:2. Interestingly, low \u03b1-syn in rHDL concentrations, molar ratio of 1:0.5 (apoA-I:\u03b1-syn), did not prevent glycation with more multimerization of apoA-I. In the lipid-free and lipid-bound state, \u03b1-syn showed more potent antioxidant activity than apoA-I against cupric ion-mediated LDL oxidation. On the other hand, microinjection of \u03b1-syn (final 2 \u03bcM) resulted in 10% less survival of zebrafish embryos than apoA-I. A subcutaneous injection of \u03b1-syn (final 34 \u03bcM) resulted in less tail fin regeneration than apoA-I. Interestingly, incorporation of \u03b1-syn at a low molar ratio (apoA-I:\u03b1-syn, 1:0.5) in rHDL resulted destabilization of the secondary structure and impairment of apoA-I functionality via more oxidation and glycation. However, at a higher molar ratio of \u03b1-syn in rHDL (apoA-I:\u03b1-syn = 1:1 or 1:2) exhibited potent antioxidant and anti-glycation activity without aggregation. In conclusion, there might be a critical concentration of \u03b1-syn and apoA-I in HDL-like complex to prevent the aggregation of apoA-I via structural and functional enhancement.<\/jats:p>","DOI":"10.3390\/molecules26247485","type":"journal-article","created":{"date-parts":[[2021,12,10]],"date-time":"2021-12-10T08:17:58Z","timestamp":1639124278000},"page":"7485","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Structural and Functional Changes of Reconstituted High-Density Lipoprotein (HDL) by Incorporation of \u03b1-synuclein: A Potent Antioxidant and Anti-Glycation Activity of \u03b1-synuclein and apoA-I in HDL at High Molar Ratio of \u03b1-synuclein"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1198-4140","authenticated-orcid":false,"given":"Kyung-Hyun","family":"Cho","sequence":"first","affiliation":[{"name":"LipoLab, Department of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Korea"},{"name":"Korea Research Institute of Lipoproteins, Medical Innovation Complex, Daegu 41061, Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,12,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S0140-6736(14)61393-3","article-title":"Parkinson\u2019s disease","volume":"386","author":"Kalia","year":"2015","journal-title":"Lancet"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1007\/s10571-018-0587-4","article-title":"Parkinson disease from mendelian forms to genetic susceptibility: New molecular insights into the neurodegeneration process","volume":"38","author":"Charsouei","year":"2018","journal-title":"Cell. 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