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Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide.

Abstract：

:Islet amyloid polypeptide (IAPP) is an unstructured polypeptide hormone that is cosecreted with insulin. In patients with type 2 diabetes, IAPP undergoes a transition from its natively disordered state to a highly ordered, all-beta-strand amyloid fiber. Although predominantly disordered, IAPP transiently samples alpha-helical structure in solution. IAPP adopts a fully helical structure when bound to membrane surfaces in a process associated with catalysis of amyloid formation. Here, we use spectroscopic techniques to study the structure of full-length, monomeric IAPP under amyloidogenic conditions. We observe that the residues with helical propensity in solution (1-22) also form the membrane-associated helix. Additionally, reduction of the N-terminal disulfide bond (Cys2-Cys7) decreases the extent of helix formed throughout this region. Through manipulation of sample conditions to increase or decrease the amount of helix, we show that the degree of helix formed affects the rate of amyloid assembly. Formation of helical structure is directly correlated with enhanced amyloid formation both on the membrane surface and in solution. These observations support suggested mechanisms in which parallel helix associations bring together regions of the peptide that could nucleate beta-strand structure. Remarkably, stabilization of non-amyloid structure appears to be a key intermediate in assembly of IAPP amyloid.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Williamson JA,Loria JP,Miranker AD

doi

10.1016/j.jmb.2009.07.077

subject

Has Abstract

pub_date

2009-10-23 00:00:00

pages

383-96

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(09)00967-X

journal_volume

393

pub_type

杂志文章

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