TY - JOUR
T1 - Biophysical characterization of DNA and RNA aptamer interactions with hen egg lysozyme
AU - Potty, Ajish S.R.
AU - Kourentzi, Katerina
AU - Fang, Han
AU - Schuck, Peter
AU - Willson, Richard C.
N1 - Funding Information:
This research was funded in part by grants from NASA (Grant NNJ04HF43G ), NSF (Grant CTS-0004544 ) and the Welch Foundation (Grant E-1264 ). This work was also supported in part by the Intramural Research Program of the NIH, NIBIB.
PY - 2011/4/1
Y1 - 2011/4/1
N2 - This work characterized the binding of an RNA aptamer recognizing hen egg white lysozyme, as well as a literature-reported single-stranded DNA analog of sequence identical to the original RNA aptamer, using fluorescence anisotropy, isothermal titration calorimetry (ITC) and analytical ultracentrifugation. The polyanionic DNA aptamer analog is selective for lysozyme even over cationic cytochrome c and has been reported to be successfully used in biosensing applications. The association however, is predominantly of electrostatic character, strongly salt-sensitive and entropically-driven, in contrast to previously described enthalpically-driven antibody-lysozyme and DNA aptamer-VEGF interactions. With a moderate selectivity for their target, high salt-sensitivity along with fast association and dissociation behavior, these molecules might serve as pseudo-affinity ligands for biomolecular separations.
AB - This work characterized the binding of an RNA aptamer recognizing hen egg white lysozyme, as well as a literature-reported single-stranded DNA analog of sequence identical to the original RNA aptamer, using fluorescence anisotropy, isothermal titration calorimetry (ITC) and analytical ultracentrifugation. The polyanionic DNA aptamer analog is selective for lysozyme even over cationic cytochrome c and has been reported to be successfully used in biosensing applications. The association however, is predominantly of electrostatic character, strongly salt-sensitive and entropically-driven, in contrast to previously described enthalpically-driven antibody-lysozyme and DNA aptamer-VEGF interactions. With a moderate selectivity for their target, high salt-sensitivity along with fast association and dissociation behavior, these molecules might serve as pseudo-affinity ligands for biomolecular separations.
KW - Aptamers
KW - Fluorescence anisotropy
KW - Hen egg white lysozyme
KW - Isothermal titration calorimetry
UR - http://www.scopus.com/inward/record.url?scp=79952101633&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79952101633&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2010.12.007
DO - 10.1016/j.ijbiomac.2010.12.007
M3 - Article
C2 - 21167858
AN - SCOPUS:79952101633
SN - 0141-8130
VL - 48
SP - 392
EP - 397
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
IS - 3
ER -