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Higher Aggregation of β‐Peptide Networks Controlled by Nucleobase Pairing
Author(s) -
Srivastava Ratika,
Kumar Ray Anmol,
Diederichsen Ulf
Publication year - 2009
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200900511
Subject(s) - nucleobase , chemistry , peptide , helix (gastropod) , sequence (biology) , circular dichroism , covalent bond , stereochemistry , crystallography , dna , biochemistry , organic chemistry , ecology , snail , biology
The aggregation and 3D organization of peptide helices are key elements in biology but might also be relevant in nanostructure formation. β‐Peptide helices were used as conformationally stable surrogates of α‐peptides to be organized by covalently attached nucleobases as recognition units. Because the β‐peptide 14‐helix conformation allows addressing individual sides of the helix, the aggregation of helices functionalized on two helix flanks was investigated. Nine helices varying in sequence and nucleobase composition were prepared by solid‐phase peptide synthesis and analyzed by temperature‐dependent UV and CD spectroscopy and FT‐ICR mass spectrometry. Already, sequences of three nucleobases on both sides of the helix provided stable aggregates. Aggregate formation was sequence dependent and led to one complex being stable in water at least up to 80 °C.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)