Int. J. Mol. Sci. 2013, 14(7), 14287-14300; doi:10.3390/ijms140714287
Review

Misfolding and Amyloid Aggregation of Apomyoglobin

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Received: 23 April 2013; in revised form: 19 June 2013 / Accepted: 20 June 2013 / Published: 9 July 2013
(This article belongs to the Special Issue Protein Folding 2015)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: Apomyoglobin is an excellent example of a monomeric all α-helical globular protein whose folding pathway has been extensively studied and well characterized. Structural perturbation induced by denaturants or high temperature as well as amino acid substitution have been described to induce misfolding and, in some cases, aggregation. In this article, we review the molecular mechanism of the aggregation process through which a misfolded form of a mutated apomyoglobin aggregates at physiological pH and room temperature forming an amyloid fibril. The results are compared with data showing that either amyloid or aggregate formation occurs under particular denaturing conditions or upon cleavage of the residues corresponding to the C-terminal helix of apomyoglobin. The results are discussed in terms of the sequence regions that are more important than others in determining the amyloid aggregation process.
Keywords: apomyoglobin folding; apomyoglobin misfolding; amyloid aggregation
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MDPI and ACS Style

Iannuzzi, C.; Maritato, R.; Irace, G.; Sirangelo, I. Misfolding and Amyloid Aggregation of Apomyoglobin. Int. J. Mol. Sci. 2013, 14, 14287-14300.

AMA Style

Iannuzzi C, Maritato R, Irace G, Sirangelo I. Misfolding and Amyloid Aggregation of Apomyoglobin. International Journal of Molecular Sciences. 2013; 14(7):14287-14300.

Chicago/Turabian Style

Iannuzzi, Clara; Maritato, Rosa; Irace, Gaetano; Sirangelo, Ivana. 2013. "Misfolding and Amyloid Aggregation of Apomyoglobin." Int. J. Mol. Sci. 14, no. 7: 14287-14300.

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