Literature DB >> 26052191

Super-secondary structure peptidomimetics: design and synthesis of an α-α hairpin analogue.

Laura Nevola1, Johanna M Rodriguez1, Sam Thompson2, Andrew D Hamilton3.   

Abstract

The α-α helix motif presents key recognition domains in protein-protein and protein-oligonucleotide binding, and is one of the most common super-secondary structures. Herein we describe the design, synthesis and structural characterization of an α-α hairpin analogue based on a tetra-coordinated Pd(II) bis-(iminoisoquinoline) complex as a template for the display of two α-helix mimics. This approach is exemplified by the attachment of two biphenyl peptidomimetics to reproduce the side-chains of the i and i+4 residues of two helices.

Entities:  

Keywords:  alpha helix, side chain, GCN4; protein-protein interaction; structural mimicry

Year:  2013        PMID: 26052191      PMCID: PMC4454340          DOI: 10.1080/10610278.2013.817581

Source DB:  PubMed          Journal:  Supramol Chem        ISSN: 1026-7816            Impact factor:   1.688


  29 in total

1.  De novo design and characterization of an apolar helical hairpin peptide at atomic resolution: Compaction mediated by weak interactions.

Authors:  U A Ramagopal; S Ramakumar; D Sahal; V S Chauhan
Journal:  Proc Natl Acad Sci U S A       Date:  2001-01-30       Impact factor: 11.205

2.  Amphiphilic α-helix mimetics based on a benzoylurea scaffold.

Authors:  Sam Thompson; Andrew D Hamilton
Journal:  Org Biomol Chem       Date:  2012-04-25       Impact factor: 3.876

Review 3.  Advances in methods and algorithms in a modern quantum chemistry program package.

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Journal:  Phys Chem Chem Phys       Date:  2006-06-12       Impact factor: 3.676

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Journal:  J Mol Biol       Date:  1976-08-15       Impact factor: 5.469

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Journal:  J Protein Chem       Date:  1996-10

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Journal:  J Mol Biol       Date:  1973-05-15       Impact factor: 5.469

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Journal:  FEBS Lett       Date:  1994-12-05       Impact factor: 4.124

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Journal:  FEBS Lett       Date:  1984-01-23       Impact factor: 4.124

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Authors:  A V Efimov
Journal:  FEBS Lett       Date:  1991-06-24       Impact factor: 4.124

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Journal:  J Org Chem       Date:  2000-01-28       Impact factor: 4.354

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  1 in total

1.  Non-covalent S···O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation.

Authors:  Hayden Peacock; Jinghui Luo; Tohru Yamashita; James Luccarelli; Sam Thompson; Andrew D Hamilton
Journal:  Chem Sci       Date:  2016-07-01       Impact factor: 9.825

  1 in total

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