ARN

@article{,

title = {Thermodynamic study of aptamers binding to their target proteins},

author = {T Sakamoto and E Ennifar and Y Nakamura},

url = {https://www.ncbi.nlm.nih.gov/pubmed/29054802?dopt=Abstract},

doi = {10.1016/j.biochi.2017.10.010},

isbn = {29054802},

year  = {2018},

date = {2018-01-01},

journal = {Biochimie},

volume = {145},

pages = {91-97},

abstract = {Aptamers are nucleic acids that bind to a target molecule with high affinity and specificity, which are selected from systematic evolution of ligands by exponential enrichment (SELEX). Aptamers feature high affinity and specificity to their target molecule and a large structural diversity; biophysical tools, together with structural studies, are essential to reveal the mechanism of aptamers recognition. Furthermore, understanding the mechanism of action would also contribute to their development for therapeutic applications. Isothermal titration calorimetry (ITC) is a fast and robust method to study the physical basis of molecular interactions. In a single experiment, it provides all thermodynamic parameters of a molecular interaction, including dissociation constant, Kd; Gibbs free energy change, ΔG; enthalpy change, ΔH; entropy change, ΔS; and stoichiometry, N. The development of modern microcalorimeters significantly contributed to the expansion of the ITC use in biological systems. Therefore, ITC has been applied to the development of small therapeutic agents that bind to target proteins and is increasingly being used to study aptamer-target protein interactions. This review focuses on thermodynamic approaches for understanding the molecular principles of aptamer-target interactions.},

keywords = {Aptamer Conformation Interaction Isothermal titration calorimetry Thermodynamics, ENNIFAR, Unité ARN},

pubstate = {published},

tppubtype = {article}

}