Premium
Tuning the Inter‐nanofibril Interaction To Regulate the Morphology and Function of Peptide/DNA Co‐assembled Viral Mimics
Author(s) -
Ni Rong,
Chau Ying
Publication year - 2017
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.201703596
Subject(s) - peptide , capsid , complementarity (molecular biology) , dna , function (biology) , transfection , protein subunit , biophysics , chemistry , microbiology and biotechnology , gene , biology , biochemistry , genetics
The ability to tune the inter‐subunit interaction within the virus capsid may be critical to assembly and biological function. This process was extended here with peptide/DNA co‐assembled viral mimics. The resulting co‐assemblies, formed and stabilized by both peptide nanofibril–DNA and peptide nanofibril–nanofibril interactions, were tuned through hydrophobic packing interactions of the peptide sequences. By strengthening peptide side‐chain complementarity and/or elongating the peptide chain (from 4 to 8 residues), we report strengthening the inter‐nanofibril interaction to create stable nanococoons that give high gene‐transfection efficacy.