title: Biomolecule-nanoparticle interactions: Elucidation of the thermodynamics by isothermal titration calorimetry.
abstract: BACKGROUND
  Nanomaterials (NMs) are often exposed to a broad range of biomolecules of different abundances. Biomolecule sorption driven by various interfacial forces determines the surface structure and composition of NMs, subsequently governs their functionality and the reactivity of the adsorbed biomolecules. Isothermal titration calorimetry (ITC) is a nondestructive technique that quantifies thermodynamic parameters through in-situ measurement of the heat absorption or release associated with an interaction.
  
  
  METHODS
  This review highlights the recent applications of ITC in understanding the thermodynamics of interactions between various nanoparticles (NPs) and biomolecules. Different aspects of a typical ITC experiment that are crucial for obtaining accurate and meaningful data, as well as the strengths, weaknesses, and challenges of ITC applications to NP research were discussed.
  
  
  CONCLUSIONS
  ITC reveals the driving forces behind biomolecule-NP interactions and the effects of the physicochemical properties of both NPs and biomolecules by quantifying the crucial thermodynamics parameters (e.g., binding stoichiometry, ΔH, ΔS, and ΔG). Complimentary techniques would strengthen the interpretation of ITC results for a more holistic understanding of biomolecule-NP interactions.
  
  
  CONCLUSIONS
  The thermodynamic information revealed by ITC and its complimentary characterizations is important for understanding biomolecule-NP interactions that are fundamental to the biomedical and environmental applications of NMs and their toxicological effects.
authors: School of Earth and Atmospheric Sciences, Georgia Institute of Technology, 311 Ferst Dr. Atlanta, GA, USA.
authors: Rixiang
authors: R
authors: Huang
authors: Department of Civil and Environmental Engineering, 18B Marston Hall, University of Massachusetts Amherst, 130 Natural Resources Road, Amherst, MA 01003, USA. Electronic address: borislau@engin.umass.edu.
authors: Boris L T
authors: BLT
authors: Lau
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry*; D000818:Animals; D002147:Calmodulin / Q000737:chemistry*; D002151:Calorimetry / Q000379:methods; D002417:Cattle; D003208:Concanavalin A / Q000737:chemistry*; D045304:Cytochromes c / Q000737:chemistry*; D005690:Galactose / Q000737:chemistry; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D037102:Lectins / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013816:Thermodynamics; D017186:Titrimetry
chemical_list: D018829:Adhesins, Bacterial; D002147:Calmodulin; D037102:Lectins; C038692:adhesin, Pseudomonas; D003208:Concanavalin A; D012710:Serum Albumin, Bovine; D045304:Cytochromes c; D005690:Galactose
keywords: Binding affinity; Heat exchange; Isothermal titration calorimetry; Nanoparticles; Protein corona