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000022156 084__ $$2WoS$$aBiology
000022156 1001_ $$0P:(DE-Juel1)VDB101069$$aFunke, S.A.$$b0$$uFZJ
000022156 245__ $$aDevelopment of a small D-enantiomeric Alzheimer's amyloid-beta binding peptide ligand for future in vivo imaging applications
000022156 260__ $$aLawrence, Kan.$$bPLoS$$c2012
000022156 300__ $$ae41457
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000022156 520__ $$aAlzheimer's disease (AD) is a devastating disease affecting predominantly the aging population. One of the characteristic pathological hallmarks of AD are neuritic plaques, consisting of amyloid-β peptide (Aβ). While there has been some advancement in diagnostic classification of AD patients according to their clinical severity, no fully reliable method for pre-symptomatic diagnosis of AD is available. To enable such early diagnosis, which will allow the initiation of treatments early in the disease progress, neuroimaging tools are under development, making use of Aβ-binding ligands that can visualize amyloid plaques in the living brain. Here we investigate the properties of a newly designed series of D-enantiomeric peptides which are derivatives of ACI-80, formerly called D1, which was developed to specifically bind aggregated Aβ1-42. We describe ACI-80 derivatives with increased stability and Aβ binding properties, which were characterized using surface plasmon resonance and enzyme-linked immunosorbent assays. The specific interactions of the lead compounds with amyloid plaques were validated by ex vivo immunochemistry in transgenic mouse models of AD. The novel compounds showed increased binding affinity and are promising candidates for further development into in vivo imaging compounds.
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000022156 7001_ $$0P:(DE-Juel1)VDB65461$$aBartnik, D.$$b1$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB89237$$aGlück, J.M.$$b2$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB107715$$aPirkowska, K.$$b3$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b4$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB2942$$aWeber, U.$$b5$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB6998$$aGulyas, B.$$b6$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB6276$$aHalldin, C.$$b7$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB72767$$aPfeifer, A.$$b8$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB104788$$aSpenger, C.$$b9$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)VDB72753$$aMuhs, A.$$b10$$uFZJ
000022156 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b11$$uFZJ
000022156 773__ $$0PERI:(DE-600)2267670-3$$a10.1371/journal.pone.0041457$$gVol. 7, p. e41457$$n7$$pe41457$$q7<e41457$$tPLoS one$$v7$$x1932-6203$$y2012
000022156 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3404088
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000022156 9141_ $$y2012
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