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Effect of Melanomal Proteins on Sepia Melanin Assembly
Authors:Pathomthat Srisuk  Vitor M Correlo  Isabel B Leonor
Institution:1. 3B's Research Group, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, S. Cláudio do Barco Caldas das Taipas, Guimar?es, Portugal;2. ICVS/3B's, PT Government Associate Laboratory, Braga/Guimar?es, Portugal;3. Faculty of Pharmaceutical Sciences, Khon Kaen University, Muang District, Khon Kaen, Thailand
Abstract:Melanins are phenol-based pigments with the potential for widespread applications, including bioelectronics and tissue engineering. The concentration-dependent structural transition of sepia melanin in water is analyzed. This biopolymer at high concentration gives the well-known nanospheres, whereas sample dilution gives unforeseen nanofibres exhibiting the structural features of mature amyloid fibrils. We propose a mechanism of pigment self-assembly dependent on the interaction of residual melanosomal protein(s) with eumelanin heteropolymer. Our results contribute to understanding the peculiar physicochemical properties of this ubiquitous pigment.
Keywords:amyloid fibrils  atomic force microscopy  cephalopod ink  scanning electron microscopy  scanning transmission electron microscopy  sepia melanin self-assembly
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