Biochem Biophys Res Commun. 2006 Nov 3;349(4):1198-205. Epub 2006 Aug 30.

Identification of human alpha-synuclein specific single chain antibodies.

Maguire-Zeiss KA, Wang CI, Yehling E, Sullivan MA, Short DW, Su X, Gouzer G, Henricksen LA, Wuertzer CA, Federoff HJ.

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Department of Neurology and the Center for Aging and Developmental Biology, University of Rochester School of Medicine and Dentistry, NY 14642, USA.

Abstract

Parkinson's disease (PD) is a common neurodegenerative disease of unknown etiology. Evidence suggests a role for protein misfolding in disease pathogenesis. One pathologic feature observed in dopaminergic neurons is the intracytoplasmic eosinophilic inclusions known as Lewy bodies. One component of Lewy bodies, the presynaptic protein, alpha-synuclein forms oligomers and higher order aggregates and is proposed to be involved in dopaminergic neuronal death. In an effort to discriminate between alpha-synuclein conformational forms as well as design potential disruptors of pathogenic misfolding we panned a human phage antibody library for anti-synuclein single chain antibodies (scFvs). We identified six scFvs which recognize different conformers of alpha-synuclein in both an ELISA and Western blot analysis. These scFvs may further our understanding of alpha-synuclein's role in PD.

PMID:: 16973126; [PubMed - indexed for MEDLINE]

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