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TitleEffect of melanomal proteins on sepia melanin assembly
Author(s)Srisuk, Pathomthat
Correlo, V. M.
Leonor, I. B.
Palladino, Pasquale
Reis, R. L.
KeywordsAmyloid fibrils
Atomic force microscopy
Cephalopod ink
Scanning electron microscopy
Scanning transmission electron microscopy
Sepia melanin self-assembly
Issue dateOct-2015
PublisherTaylor & Francis
JournalJournal of Macromolecular Science Part B Physics
CitationSrisuk P., Correlo V. M., Leonor I. B., Palladino P., Reis R. L. Effect of Melanomal Proteins on Sepia Melanin Assembly, Journal of Macromolecular Science, Part B: Physics, doi:10.1080/00222348.2015.1103430, 2015
Abstract(s)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 physico-chemical properties of this ubiquitous pigment
DescriptionAccepted manuscript
Publisher version
AccessOpen access
Appears in Collections:3B’s - Artigos em revistas/Papers in scientific journals

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