PMID: 12767835May 28, 2003Paper

The sequence dependence of fiber organization. A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29

Journal of Molecular Biology
David Zanuy, Ruth Nussinov

Abstract

Amyloid fiber formation and the possible polymorphism of molecular arrangements depend on the polypeptide length and composition. Here, we seek the chemical clues underlying these processes. Our starting point is based on the experimental observation that some short peptide segments are able to develop fibers that are very similar to those of their original parent proteins. We focus our study on the NFGAILSS peptide, derived from the human islet amyloid polypeptide (residues 22-29). This peptide turned out to be a perfect example, illustrating the fact that the amyloid microscopic organization is highly complex, rather than simply involving hydrogen bond formation. Furthermore, obtaining a reliable molecular model has allowed us to analyze the differences between the amyloid structure we have obtained for this peptide and that obtained for the previously studied, two residues shorter, segment (residues 22-27, NFGAIL). This comparative study yields some clues about chemical events that govern the aggregation of proteins into oriented fibers, such as molecular packing between sheets and the degree of interaction specificity. We characterize the important role played by the hydrophobic and aromatic residues in the inter-sheet asso...Continue Reading

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Citations

Feb 9, 2006·Journal of the American Chemical Society·Hung D Nguyen, Carol K Hall
Jul 7, 2007·The Journal of Chemical Physics·Giovanni Bellesia, Joan-Emma Shea
May 25, 2005·The Journal of Chemical Physics·Adrien MelquiondPhilippe Derreumaux
Sep 24, 2005·Proceedings of the National Academy of Sciences of the United States of America·Sarah A Petty, Sean M Decatur
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Oct 16, 2010·Structure·Jason Greenwald, Roland Riek
Nov 29, 2011·Journal of Molecular Biology·Buyong Ma, Ruth Nussinov
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Nov 30, 2006·Journal of Peptide Science : an Official Publication of the European Peptide Society·Inta LiepinaAdam Liwo

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