The Key Features of Catechols and α,β Unsaturated Carbonyl Moieties: Interaction With α-syn Hydrophobic peptide and Activation of Catecholamines Pathway in Cells

Simple item page
dc.article.numbere202301106
dc.catalogadorvzp
dc.contributor.authorMonroy-Moya, S.
dc.contributor.authorCaballero, J.
dc.contributor.authorGonzalez-Norambuena, F.
dc.contributor.authorSimirgiotis, M.
dc.contributor.authorSanchez, E.
dc.contributor.authorAreche, C.
dc.contributor.authorFuentealba Patino, Denis Alberto
dc.contributor.authorCornejo, A.
dc.date.accessioned2024-04-15T08:00:36Z
dc.date.available2024-04-15T08:00:36Z
dc.date.issued2023
dc.description.abstractParkinson's disease (PD) is the second most prevalent neurodegenerative disorder worldwide, and the treatment focuses on delivering L-DOPA. In this work, we isolated and tested several compounds against alpha-synuclein and the hydrophobic peptide (71)VTGVTAVAQKTV(82) including flavonols (kaempferol, quercetin, and isorhamnetin), isoflavone (genistein) and flavone (luteolin), and compounds with alpha, beta unsaturated carbonyl moieties such as chlorogenic acid and the depsidone fumarprotocetraric acid. Most compounds inhibit both alpha-synuclein and hydrophobic peptide fibrillization. Moreover, ITC experiments showed a Kd varying from 9 to 20 mu M, and Delta H values vary from -1.94 to -10.5 among the compounds. Docking experiments showed the intermolecular interactions within the sites 2, 9, and 3/13 of alpha-synuclein, and with the hydrophobic peptide. In cultured cells, the presence of the compounds showed that most of them can promote cell proliferation and differentiation. Considering that treatments for neurodegenerative disorders, including PD, is only palliative the evaluation of these compounds that can prevent the fibrillization of alpha-synuclein and stimulate the catecholamines pathway is promising.
dc.description.funderAgencia Nacional de Investigación y Desarrollo
dc.description.funderFondo Nacional de Ciencia y Tecnología
dc.description.funderFONDAP
dc.format.extent25 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1002/slct.202301106
dc.identifier.eissn0718-8358
dc.identifier.issn2365-6549
dc.identifier.pubmedidMEDLINE:34800746
dc.identifier.scopusidSCOPUS_ID:85116295653
dc.identifier.urihttps://doi.org/10.1002/slct.202301106
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/85104
dc.identifier.wosidWOS:000988035700001
dc.information.autorucEscuela de Química; Fuentealba Patino, Denis Alberto; 0000-0003-4798-7204; 160255
dc.issue.numero19
dc.language.isoen
dc.nota.accesoContenido parcial
dc.pagina.final72
dc.pagina.inicio49
dc.revistaCHEMISTRYSELECT
dc.rightsacceso restringido
dc.subjectCell differentiation
dc.subjectHydrophobic region
dc.subjectNon-covalent interactions
dc.subjectParkinson's disease
dc.subjectTyrosine hydroxylase
dc.subject.ddc510
dc.subject.deweyMatemática física y químicaes_ES
dc.subject.ods03 Good health and well-being
dc.subject.odspa03 Salud y bienestar
dc.titleThe Key Features of Catechols and α,β Unsaturated Carbonyl Moieties: Interaction With α-syn Hydrophobic peptide and Activation of Catecholamines Pathway in Cells
dc.title.alternativeThe Key Features of Catechols and alpha,beta Unsaturated Carbonyl Moieties: Interaction With alpha-syn Hydrophobic peptide and Activation of Catecholamines Pathway in Cells
dc.typeartículo
dc.volumen8
sipa.codpersvinculados160255
sipa.indexWOS
sipa.trazabilidadWOS;2023-07-06
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
The Key Features of Catechols and α,β Unsaturated Carbonyl Moieties - Interaction With α-syn Hydrophobic peptide and Activation of Catecholamines Pathway in Cells.pdf
Size:
3.06 KB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Artículos de revistas