Literature DB >> 27317951

Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.

Kalkena Sivanesam1, Irene Shu1, Kelly N L Huggins1, Marianna Tatarek-Nossol2, Aphrodite Kapurniotu3, Niels H Andersen1.   

Abstract

Versions of a previously discovered β-hairpin peptide inhibitor of IAPP aggregation that are stabilized in that conformation, or even forced to remain in the hairpin conformation by a backbone cyclization constraint, display superior activity as inhibitors. The cyclized hairpin, cyclo-WW2, displays inhibitory activity at substoichiometric concentrations relative to this amyloidogenic peptide. The hairpin-binding hypothesis stands confirmed.
© 2016 Federation of European Biochemical Societies.

Entities:  

Keywords:  amyloid fibril formation; circular dichroism; cyclic β-hairpins; cytotoxicity inhibition; human pancreatic amylin; thioflavin T fluorescence; type II diabetes

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Substances：

Year:  2016        PMID： 27317951      PMCID： PMC4992449          DOI： 10.1002/1873-3468.12261

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  35 in total

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Authors:  Fanling Meng; Andisheh Abedini; Annette Plesner; Chris T Middleton; Kathryn J Potter; Martin T Zanni; C Bruce Verchere; Daniel P Raleigh
Journal:  J Mol Biol       Date:  2010-05-07       Impact factor: 5.469

2.  Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

Authors:  P Westermark; U Engström; K H Johnson; G T Westermark; C Betsholtz
Journal:  Proc Natl Acad Sci U S A       Date:  1990-07       Impact factor: 11.205

Review 3.  Islet amyloid polypeptide, islet amyloid, and diabetes mellitus.

Authors:  Per Westermark; Arne Andersson; Gunilla T Westermark
Journal:  Physiol Rev       Date:  2011-07       Impact factor: 37.312

4.  Full-length rat amylin forms fibrils following substitution of single residues from human amylin.

Authors:  Janelle Green; Claire Goldsbury; Thierry Mini; Shabir Sunderji; Peter Frey; Joerg Kistler; Garth Cooper; Ueli Aebi
Journal:  J Mol Biol       Date:  2003-02-28       Impact factor: 5.469

5.  Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus.

Authors:  A Lorenzo; B Razzaboni; G C Weir; B A Yankner
Journal:  Nature       Date:  1994-04-21       Impact factor: 49.962

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

Authors:  Jessica A Williamson; J Patrick Loria; Andrew D Miranker
Journal:  J Mol Biol       Date:  2009-07-30       Impact factor: 5.469

7.  Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus.

Authors:  A N Roberts; B Leighton; J A Todd; D Cockburn; P N Schofield; R Sutton; S Holt; Y Boyd; A J Day; E A Foot
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

8.  Pore formation by the cytotoxic islet amyloid peptide amylin.

Authors:  T A Mirzabekov; M C Lin; B L Kagan
Journal:  J Biol Chem       Date:  1996-01-26       Impact factor: 5.157

9.  Dynamic alpha-helix structure of micelle-bound human amylin.

Authors:  Sharadrao M Patil; Shihao Xu; Sarah R Sheftic; Andrei T Alexandrescu
Journal:  J Biol Chem       Date:  2009-02-24       Impact factor: 5.157

10.  Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor.

Authors:  Chris T Middleton; Peter Marek; Ping Cao; Chi-cheng Chiu; Sadanand Singh; Ann Marie Woys; Juan J de Pablo; Daniel P Raleigh; Martin T Zanni
Journal:  Nat Chem       Date:  2012-03-11       Impact factor: 24.427
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  6 in total

1.  Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.

Authors:  Karunakar Kar; Matthew A Baker; George A Lengyel; Cody L Hoop; Ravindra Kodali; In-Ja Byeon; W Seth Horne; Patrick C A van der Wel; Ronald Wetzel
Journal:  J Mol Biol       Date:  2016-12-13       Impact factor: 5.469

2.  Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities.

Authors:  Nikolaos Louros; Gabriele Orlando; Matthias De Vleeschouwer; Frederic Rousseau; Joost Schymkowitz
Journal:  Nat Commun       Date:  2020-07-03       Impact factor: 14.919

Review 3.  Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus.

Authors:  Pratiksha H Roham; Shreyada N Save; Shilpy Sharma
Journal:  J Pharm Anal       Date:  2022-04-07

Review 4.  Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms.

Authors:  Sofia Giorgetti; Claudio Greco; Paolo Tortora; Francesco Antonio Aprile
Journal:  Int J Mol Sci       Date:  2018-09-09       Impact factor: 5.923

Review 5.  Peptide-Based Molecular Strategies To Interfere with Protein Misfolding, Aggregation, and Cell Degeneration.

Authors:  Valentina Armiento; Anna Spanopoulou; Aphrodite Kapurniotu
Journal:  Angew Chem Int Ed Engl       Date:  2019-11-28       Impact factor: 15.336

Review 6.  Pre-structured hydrophobic peptide β-strands: A universal amyloid trap?

Authors:  Kalkena Sivanesam; Niels Andersen
Journal:  Arch Biochem Biophys       Date:  2019-01-29       Impact factor: 4.013
  6 in total

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