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Biomolecule-nanoparticle interactions: Elucidation of the thermodynamics by isothermal titration calorimetry

  • University of Massachusetts

Research output: Contribution to journalArticlepeer-review

120 Scopus citations

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. Scope of review 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. Major 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. General significance 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. This article is part of a Special Issue entitled Microcalorimetry in the BioSciences - Principles and Applications, edited by Fadi Bou-Abdallah.

Original languageEnglish
Pages (from-to)945-956
Number of pages12
JournalBiochimica et Biophysica Acta - General Subjects
Volume1860
Issue number5
DOIs
StatePublished - May 1 2016

Keywords

  • Binding affinity
  • Heat exchange
  • Isothermal titration calorimetry
  • Nanoparticles
  • Protein corona

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