Challenging drug target for Parkinson's disease: Pathological complex of the chameleon TPPP/p25 and alpha-synuclein proteins

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• 作者：Tibor Szé ; n&aacute ; si^a ; ¹ ; ^{szenasi.tibor@ttk.mta.hu} ; Judit Ol&aacute ; h^a ; ¹ ; ^{olah.judit@ttk.mta.hu} ; Adé ; l Szabó ; ^a ; ^{szabo.adel@ttk.mta.hu} ; S&aacute ; ndor Szunyogh^a ; ^{szunyogh.sandor@ttk.mta.hu} ; Andr&aacute ; s L&aacute ; ng^b ; ^{langax@chem.elte.hu} ; Andr&aacute ; s Perczel^b ; ^c ; ^{perczel@chem.elte.hu} ; Attila Lehotzky^a ; ^{lehotzky.attila@ttk.mta.hu} ; Vladimir N. Uversky^d ; ^e ; ^{vuversky@health.usf.edu} ; Judit Ov&aacute ; di^a ; ^{ovadi.judit@ttk.mta.hu}
• 关键词：Tubulin Polymerization Promoting Protein/p25 ; α-Synuclein ; Deletion mutants ; Protein chameleon ; Drug target ; Bimolecular fluorescence complementation
• 刊名：Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1863
• 期：1
• 页码：310-323
• 全文大小：1610 K
• 卷排序：1863

文摘

TPPP/p25 is co-enriched and co-localized with SYN in brain inclusions of Parkinson’s disease patients. Interaction of SYN with various deletion mutants and fragments of TPPP/p25 were characterized. Chameleon feature of TPPP/p25 has been established at molecular and cellular level as well as by bioinformatics’ approach. New innovative strategy is based upon the targeting of the interface of TPPP/p25 complexed with SYN but not with tubulin.