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?-Strand mimics based on tetrahydropyridazinedione (tpd) peptide stitching.


ABSTRACT: Short peptides featuring a tetrahydropyridazinedione (tpd) backbone tether exhibit reduced conformational flexibility external to the heterocyclic constraint. Analysis by NMR, molecular modeling and X-ray crystallography suggests both covalent and non-covalent stabilization of extended peptide conformations. An efficient solid-phase protocol was developed for the synthesis of a new class of ?-strand mimics based on oligomeric tpd subunits.

SUBMITTER: Kang CW 

PROVIDER: S-EPMC5561724 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

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β-Strand mimics based on tetrahydropyridazinedione (tpd) peptide stitching.

Kang Chang Won CW   Sarnowski Matthew P MP   Ranatunga Sujeewa S   Wojtas Lukasz L   Metcalf Rainer S RS   Guida Wayne C WC   Del Valle Juan R JR  

Chemical communications (Cambridge, England) 20151101 90


Short peptides featuring a tetrahydropyridazinedione (tpd) backbone tether exhibit reduced conformational flexibility external to the heterocyclic constraint. Analysis by NMR, molecular modeling and X-ray crystallography suggests both covalent and non-covalent stabilization of extended peptide conformations. An efficient solid-phase protocol was developed for the synthesis of a new class of β-strand mimics based on oligomeric tpd subunits. ...[more]

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