Abstract
ZIF-8 and Au/ZIF-8 were synthesized and utilized to evaluate their biocompatibility with hemoglobin (Hb). Conformational changes were introduced by both materials in the native structure of Hb after interaction. Evidently, Au/ZIF-8 had greater structural influence than ZIF-8. The protein thermal stability was stabilized by both ZIF-8 and Au/ZIF-8 only at lower concentrations.
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