@article {18597,
	title = {Effect of Melanomal Proteins on Sepia Melanin Assembly},
	journal = {Journal of Macromolecular Science, Part B: Physics},
	year = {2015},
	month = {2015-10-06 00:00:00},
	publisher = {Taylor and Francis Ltd.},
	abstract = {<p><span>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</span></p>},
	keywords = {amyloid fibrils, atomic force microscopy, cephalopod ink, scanning electron microscopy, Scanning transmission electron microscopy, Sepia melanin self-assembly},
	doi = {10.1080/00222348.2015.1103430},
	url = {http://www.tandfonline.com/doi/abs/10.1080/00222348.2015.1103430},
	author = {Srisuk, P. and Correlo, V. M. and Leonor, I. B. and Palladino, P. and Reis, R. L.}
}
