Article
Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: destabilization of helix bundle and enhancement of fibril formation.
The Journal of biological chemistry - 25 Jan 2013
Adachi Emi, Nakajima Hiroyuki, Mizuguchi Chiharu, Dhanasekaran Padmaja, Kawashima Hiroyuki, Nagao Kohjiro, Akaji Kenichi, Lund-Katz Sissel, Phillips Michael C, Saito Hiroyuki
Abstract excerpt
A number of naturally occurring mutations of apolipoprotein (apo) A-I, the major protein of HDL, are known to be associated with hereditary amyloidosis and atherosclerosis. Here, we examined the effects of the G26R point mutation in apoA-I (apoA-I(Iowa)) on the structure, stability, and aggregation propensity to form amyloid fibril of full-length apoA-I and the N-terminal fragment of apoA-I. Circular dichroism...
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