| DOI | Resolve DOI: https://doi.org/10.1021/bm5004515 |
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| Author | Search for: Kabiri, Maryam; Search for: Unsworth, Larry D.1 |
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| Affiliation | - National Research Council of Canada. Security and Disruptive Technologies
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| Format | Text, Article |
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| Subject | biomolecular interactions; isothermal titration calorimetry; peptide self assemblies; protein adsorption; thermodynamic parameter; peptide; polymer; protein; adiabaticity; adsorption; enthalpy; entropy; equilibrium constant; isothermal titration calorimetry; macromolecule; molecular interaction; protein analysis; surface plasmon resonance; theory; thermodynamics |
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| Abstract | The complex nature of macromolecular interactions usually makes it very hard to identify the molecular-level mechanisms that ultimately dictate the result of these interactions. This is especially evident in the case of biological systems, where the complex interaction of molecules in various situations may be responsible for driving biomolecular interactions themselves but also has a broader effect at the cell and/or tissue level. This review will endeavor to further the understanding of biomolecular interactions utilizing the isothermal titration calorimetry (ITC) technique for thermodynamic characterization of two extremely important biomaterial systems, viz., peptide self-assembly and nonfouling polymer-modified surfaces. The advantages and shortcomings of this technique will be presented along with a thorough review of the recent application of ITC to these two areas. Furthermore, the controversies associated with the enthalpy-entropy compensation effect as well as thermodynamic equilibrium state for such interactions will be discussed. |
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| Publication date | 2014-08-18 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21272657 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | e55f80fd-9f1d-4686-9b90-407f8edc2cf8 |
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| Record created | 2014-12-03 |
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| Record modified | 2020-04-22 |
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