Lee, KH Shin, BH Shin, KJ Kim, DJ Yu, J 2024-01-21T05:12:40Z 2024-01-21T05:12:40Z 2021-09-03 2005-03-25 0006-291X https://pubs.kist.re.kr/handle/201004/136631 Inhibition of oligomeric amyloid (A) peptide or fibril formation has emerged as a major therapeutic target for developing new drugs for Alzheimer's disease. We focused on developing inhibitors by synthesizing hybrid molecules of ferulic acid and styryl benzene, which has been known as a fibril binder. Initially, cell-based assay was carried out to evaluate the effective compound. A selected effector, 1, alleviated the Abeta-induced neuronal toxicity in differentiated SH-SY5Y human neuroblastoma cells. The effector could also inhibit Abeta fibril formation, monitored by thioflavin T fluorescence intensity assay and transmitted electron microscopic images. A strong binding affinity of I to non-fibrous monomer-like Abeta, which was immobilized to a surface chip, was measured using a surface plasmon resonance technique. The data suggest that the effector shifts the equilibrium of multimeric Abeta, inhibiting the pathogenic oligomer or fibril formation. (C) 2005 Elsevier Inc. All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE ALZHEIMERS-DISEASE IN-VITRO THERAPEUTIC STRATEGIES PEPTIDE OLIGOMERIZATION POTENTIATION INHIBITION HYPOTHESIS DISORDERS MECHANISM A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by beta-amyloid (1-42) Article 10.1016/j.bbrc.2005.01.030 1 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.328, no.4, pp.816 - 823 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 328 4 816 823 scie scopus 000227233000002 2-s2.0-13744252140 Biochemistry & Molecular Biology Biophysics Biochemistry & Molecular Biology Biophysics Article ALZHEIMERS-DISEASE IN-VITRO THERAPEUTIC STRATEGIES PEPTIDE OLIGOMERIZATION POTENTIATION INHIBITION HYPOTHESIS DISORDERS MECHANISM synthesis of styryl benzene-ferulic acid hybrid molecules inhibitor for toxic amyloid beta peptide