Kagan Kerman

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Electrochemical-based protein sensors offer sensitivity, selectivity and reliability at a low cost, making them very attractive tools for protein detection. Although the sensors use a broad range of different chemistries, they all depend on the solid electrode surface, interactions with the target protein and the molecular recognition layer. Traditionally,(More)
Recent trends and challenges in the electrochemical methods for the detection of DNA hybridization are reviewed. Electrochemistry has superior properties over the other existing measurement systems, because electrochemical biosensors can provide rapid, simple and low-cost on-field detection. Electrochemical measurement protocols are also suitable for mass(More)
Alzheimer's disease (AD) is a complex neurodegenerative disorder marked by numerous causative factors of disease progression, termed pathologies. We report here the synthesis of a small library of novel sym-triazine compounds designed for targeted modulation of multiple pathologies related to AD, specifically human acetylcholinesterase (AChE),(More)
We herein report the design and synthesis of the first nanomolar binding inhibitor of STAT5 protein. Lead compound 13a, possessing a phosphotyrosyl-mimicking salicylic acid group, potently and selectively binds to STAT5 over STAT3, inhibits STAT5-SH2 domain complexation events in vitro, silences activated STAT5 in leukemic cells, as well as STAT5's(More)
The interaction of dopamine (DA) and α-synuclein (α-S) can lead to protein misfolding and neuronal death triggered by oxidative stress relevant to the progression of Parkinson's disease (PD). In this study, interfacial properties associated with DA-induced α-S aggregation under various solution conditions (i.e., pH, ionic strength) were investigated in(More)
The bioactivities of two novel compounds (TAE-1 and TAE-2) that contain a sym-triazine scaffold with acetylcholine-like substitutions are examined as promising candidate agents against Alzheimer's disease. Inhibition of amyloid-β fibril formation in the presence of Aβ1-42, evaluated by Thioflavin T fluorescence, demonstrated comparable or improved activity(More)
Self-aggregation of amyloid-β (Aβ) plays an important role in the pathogenesis of Alzheimer's disease (AD). Small molecule inhibitors of Aβ fibril formation reduce the Aβ-mediated neurotocixity. In this report, the interaction of amyloid-β (Aβ) with well-described modulators, (-)epigallocatechin-3-gallate (EGCG) and Zn(ii), was detected using a LED-based(More)
Alzheimer's disease (AD) is marked by the accumulation of neuronal plaques from insoluble amyloid-beta (Aβ) peptides. Growing evidence for the role of Aβ oligomers in neuronal cell cytotoxicity and pathogenesis has prompted the development of novel techniques to better understand the early stages of aggregation. Near infrared (NIR) optical trapping was(More)
The electrochemical oxidation of the benzothiazole dye Thioflavin T (ThT) was found to be modulated by its interaction with electric eel acetylcholinesterase (AChE). Modifications of AChE by trace amounts of small molecule inhibitors such as carbachol and paraoxon were detectable electrochemically using minimal reagents and with greater sensitivity than(More)