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Protein Transduction Domain Mimics: The Role of Aromatic Functionality
Author(s) -
Som Abhigyan,
Reuter Anika,
Tew Gregory N.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104624
Subject(s) - transduction (biophysics) , domain (mathematical analysis) , side chain , chemistry , computer science , computational biology , stereochemistry , biochemistry , polymer , organic chemistry , biology , mathematics , mathematical analysis
For better or worse : Protein transduction domain mimics built from synthetic polymers demonstrate that aromatic side chains provide better transduction than aliphatic groups at the same relative hydrophobicity. Similarly, a less hydrophobic aromatic side chain is more active than the corresponding aliphatic one containing the same number of carbon atoms (see picture).