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Direct force measurement of single DNA–peptide interactions using atomic force microscopy
Author(s) -
Chung Ji W.,
Shin Dongjin,
Kwak June M.,
Seog Joonil
Publication year - 2013
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2269
Subject(s) - peptide , leucine zipper , dna , chemistry , folding (dsp implementation) , atomic force microscopy , force spectroscopy , zipper , biophysics , crystallography , molecule , sequence (biology) , nanotechnology , peptide sequence , materials science , biochemistry , biology , mathematics , organic chemistry , algorithm , electrical engineering , gene , engineering
The selective interactions between DNA and miniature (39 residues) engineered peptide were directly measured at the single‐molecule level by using atomic force microscopy. This peptide (p007) contains an α‐helical recognition site similar to leucine zipper GCN4 and specifically recognizes the ATGAC sequence in the DNA with nanomolar affinity. The average rupture force was 42.1 pN, which is similar to the unbinding forces of the digoxigenin–antidigoxigenin complex, one of the strongest interactions in biological systems. The single linear fit of the rupture forces versus the logarithm of pulling rates showed a single energy barrier with a transition state located at 0.74 nm from the bound state. The smaller k off compared with that of other similar systems was presumably due to the increased stability of the helical structure by putative folding residues in p007. This strong sequence‐specific DNA–peptide interaction has a potential to be utilized to prepare well‐defined mechanically stable DNA–protein hybrid nanostructures. Copyright © 2013 John Wiley & Sons, Ltd.