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Steric Zipper Formed by Hydrophobic Peptide Fragment of Syrian Hamster Prion Protein

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Hsin-Mei Cheng, Tim W. T. Tsai, William Y. C. Huang, Hsin-Kuan Lee, Huei-Ying Lian, Fang-Chieh Chou, Yun Mou, and Jerry C. C. Chan*

Department of Chemistry, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei 106, Taiwan

Biochemistry, 2011, 50 (32), pp 6815–6823

DOI: 10.1021/bi200712z

Publication Date (Web): July 13, 2011

Phone: 886-2-33662994. Fax: 886-2-23636359. E-mail: chanjcc@ntu.edu.tw.

Funding Statement

This work was supported by grants from the National Science Council and the Ministry of Education.

Section:

General Biochemistry

Abstract

Steric zippers, where the residues of two neighboring β-sheet layers are tightly interdigitated, have been proposed as fundamental structural units of amyloid fibrils by Eisenberg and co-workers. The steric zipper formed by polypeptides containing the palindromic sequence AGAAAAGA has a distinctive feature that the distance between two interdigitated β-sheet layers is comparable to the interstrand distance of the individual β-sheet. This structural motif is of great interest in the study of prion disease because the AGAAAAGA sequence is highly conserved in prion proteins of different species. In this work, the amyloid fibrils formed by the polypeptides of PrP(113–127), viz. Ac-AGAAAAGAVVGGLGG-NH₂, are taken as the model compound to investigate the biophysical principles governing the steric zipper formation. The target fibrils adopt the structural motif of class 7 steric zipper, which is formed by stacking of antiparallel β-sheet layers with residue 117 + k forming backbone hydrogen bonds to residue 120 – k. Implication of our results in the infectivity of scrapie prion is briefly discussed.

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History

Published In Issue August 16, 2011
Article ASAPJuly 13, 2011
Received: May 09, 2011
Revised: June 30, 2011

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Article

Steric Zipper Formed by Hydrophobic Peptide Fragment of Syrian Hamster Prion Protein

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Recommend & Share

Related Content

Relative and Regional Stabilities of the Hamster, Mouse, Rabbit, and Bovine Prion Proteins toward Urea Unfolding Assessed by Nuclear Magnetic Resonance and Circular Dichroism Spectroscopies

Structural Insights into the Pre-Amyloid Tetramer of β-2-Microglobulin from Covalent Labeling and Mass Spectrometry

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