Transthyretin Acid Induced Denaturation is Required for Amyloid Fibril Formation in Vitro

  • Wilfredo Colon
  • Jeffery W. Kelly
Part of the Industry-University Cooperative Chemistry Program Symposia book series (IUCC)

Abstract

The human plasma protein transthyretin (TTR), implicated as the causative agent in Familial Amyloid Polyneuropathy and Senile Systemic Amyloidosis, was transformed into amyloid fibrils in vitro under conditions that mimic the environment of a lysosome (pH 4.5). During the course of acid (HC1) induced denaturation, a folding intermediate associates to form amyloid fibrils. This procedure for making amyloid fibrils appears to be physiologically relevant and general in that IgG2 λ, another amyloidogenic protein which is associated with primary amyloidosis, was also transformed into amyloid fibrils at pH 4.5. This preliminary work suggests that denaturation is an integral part of the amyloid fibril formation mechanism in vivo.

Keywords

Amyloid Fibril Familial Amyloid Polyneuropathy Amyloidogenic Protein Form Amyloid Fibril Primary Amyloidosis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • Wilfredo Colon
    • 1
  • Jeffery W. Kelly
    • 1
  1. 1.Department of ChemistryTexas A&M UniversityCollege StationUSA

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