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Title: Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization

Here, polybasic helical peptides, such as peptide p5, bind human amyloid extracts and synthetic amyloid fibrils. When radio labeled, peptide p5 has been shown to specifically bind amyloid in vivo thereby allowing imaging of the disease. Structural requirements for heparin and amyloid binding have been studied using analogues of p5 that modify helicity and chirality.
Authors:
 [1] ;  [1] ;  [1] ;  [1] ;  [2] ;  [1] ;  [1]
  1. Univ. of Tennessee, Knoxville, TN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
OSTI Identifier:
1327690
Grant/Contract Number:
AC05-00OR22725
Type:
Accepted Manuscript
Journal Name:
Biochemistry and Biophysics Reports
Additional Journal Information:
Journal Volume: 8; Journal Issue: C; Journal ID: ISSN 2405-5808
Publisher:
Elsevier
Research Org:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Org:
ME USDOE - Office of Management, Budget, and Evaluation; ORNL work for others
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES polybasic peptides; amyloid binding; heparin; amino acid spacing; CD; molecular dynamics