Santosh Kumar, Srayoshi Roy Chowdhury, Sahabaj Mondal and Debasish Haldar
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引用次数: 0
Abstract
This study examined the role of diphenylalanine (the central hydrophobic cluster of Alzheimer's β-amyloid peptide) in the intermolecular hydrogen-bonded supramolecular sheet and fibril formation. N-phenylglycine appended peptide NPG-Phe-Phe-OMe (1), having a sequence similarity with a diphenylalanine motif, self-aggregates to form entangled fibers. The fibers show green-gold birefringence in a Congo red assay. Moreover, the fibers bind with thioflavin T (ThT) and show an enhanced emission. However, the tyrosine-modified analogues failed to form fibers and rather exhibited a microsphere-like morphology. From X-ray diffraction analysis, the tyrosine-modified analogues, namely, NPG-Phe-Tyr-OMe (2) and NPG-Tyr-Phe-OMe (3), adopt extended conformations and self-aggregate to form sheet-like structures via intermolecular hydrogen bonds and π–π stacking interactions.
期刊介绍：
Molecular Systems Design & Engineering provides a hub for cutting-edge research into how understanding of molecular properties, behaviour and interactions can be used to design and assemble better materials, systems, and processes to achieve specific functions. These may have applications of technological significance and help address global challenges.
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