ArticleMolecules (Basel, Switzerland)2026
Affibody Complex Formation: An In-Depth Thermodynamic Analysis Using Isothermal Titration Calorimetry.
Article in Molecules (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
This study investigates the thermodynamics of binding between the affibody proteins ZTaq and anti-ZTaq across a broad temperature range, aiming to deepen the understanding of the underlying mechanisms governing their interaction. Affibodies are small, engineered proteins of notable stability and practical utility, serving as robust models for molecular recognition processes. Here, the anti-idiotypic binders ZTaq and anti-ZTaq were expressed and purified, and their interaction was characterized using isothermal titration calorimetry (ITC). The analysis revealed that the formation of the ZTaq:anti-ZTaq complex is marked by a large negative free energy of binding Δ
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