BibTex format

author = {Nuttall, P and Lee, K and Ciccarella, P and Carminati, M and Ferrari, G and Kim, KB and Albrecht, T},
doi = {10.1021/acs.jpcb.5b11076},
journal = {Journal of Physical Chemistry B},
pages = {2106--2114},
title = {Single-Molecule Studies of Unlabeled Full-Length p53 Protein Binding to DNA.},
url = {},
volume = {120},
year = {2016}

RIS format (EndNote, RefMan)

AB - p53 is an antitumor protein that plays an important role in apoptosis, preserving genomic stability and preventing angiogenesis, and it has been implicated in a large number of human cancers. For this reason it is an interesting target for both fundamental studies, such as the mechanism of interaction with DNA, and applications in biosensing. Here, we report a comprehensive study of label-free, full length p53 (flp53) and its interaction with engineered double-stranded DNA in vitro, at the single-molecule level, using atomic force microscopy (AFM) imaging and solid-state nanopore sensing. AFM data show that dimeric and tetrameric p53 bind to the DNA in a sequence-specific manner, confirming previously reported relative binding affinities. The statistical significance is tested using both the Grubbs test and stochastic simulations. For the first time, ultralow noise solid-state nanopore sensors are employed for the successful differentiation between bare DNA and p53/DNA complexes. Furthermore, translocation statistics reflect the binding affinities of different DNA sequences, in accordance with AFM data. Our results thus highlight the potential of solid-state nanopore sensors for single-molecule biosensing, especially when labeling is either not possible or at least not a viable option.
AU - Nuttall,P
AU - Lee,K
AU - Ciccarella,P
AU - Carminati,M
AU - Ferrari,G
AU - Kim,KB
AU - Albrecht,T
DO - 10.1021/acs.jpcb.5b11076
EP - 2114
PY - 2016///
SN - 1520-6106
SP - 2106
TI - Single-Molecule Studies of Unlabeled Full-Length p53 Protein Binding to DNA.
T2 - Journal of Physical Chemistry B
UR -
UR -
VL - 120
ER -