NDLI: Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid.

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Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Koo, Bon W. Miranker, Andrew D.
Description	Country affiliation: United States Author Affiliation: Koo BW ( Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Ave., New Haven, CT 06520-8114, USA.)
Abstract	Amyloidogenesis from soluble protein requires conformational and oligomeric assembly steps. In systems where the precursor protein is natively unfolded, such as islet amyloid polypeptide (IAPP), forces and structural changes relevant to protein unfolding are not thought to participate in the assembly mechanism. Thus, fiber core structure elements should provide the dominant contributions to assembly kinetics. Here we show, however, that residues outside the amyloid core can influence the mechanism of IAPP fiber assembly. IAPP possesses an intramolecular disulfide bond between residues 2 and 7. This short-range disulfide prohibits the N-terminal region from adopting the beta-strand structure of an amyloid. We examined the role of this disulfide in fiber formation by generating a truncated construct (IAPP(8-37)) and a stable reduced form of the full-length protein (IAPP(CAM)). The fiber structures and assembly kinetics of these variants were assessed via optical and mass spectroscopy. Our data confirm that the disulfide does not contribute to the amyloid fiber core structure. Remarkably, however, it plays a central role in the assembly mechanism. First, loss of the disulfide substantially reduces fiber formation by secondary nucleation, i.e., the ability of pre-existing fibers to participate in the formation of new fibers. Second, the bypass of nucleation by seed addition is a two-step process, termed activation. Loss of the disulfide eliminates this two-step nature of seeded kinetics.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	14
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2005-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Chemistry Disulfides Amino Acid Sequence Islet Amyloid Polypeptide Kinetics Molecular Sequence Data Protein Binding Sequence Homology, Amino Acid Time Factors Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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