Abstract
To evaluate the interaction between haloacetonitriles (HANs) and human hemoglobin (Hb), a pipeline was established based on fluorescence spectra, mass spectra and molecular docking. Fluorescence spectra analysis showed the fluorescence of Hb was statically quenched by HANs in the sequence of TCAN > DBAN > DCAN > IAN > BAN > CAN. HANs could combine to multiple surface sites of Hb accounting for “hydrogen bonds” and “van der Waals forces”. The high-resolution mass spectra analysis for Hb with and without HANs further confirmed the formation of multiple HAN-Hb complexes with different conversion rates. With the assistance of MOE molecule docking, the potential combination sites and related interactions parameters between HANs and Hb were filtrated. By analyzing the correlations between the candidate interactions parameters and fluorescence quenching constants/MS conversion rates, the combination sites of HANs were fixed at Asp126 (α1/α2), Lys127 (α1/α2) in the form of “hydrogen bonds” X → Asp126 (α1/α2), N → Lys127 (α1/α2). In this way, the potential interactions between HANs and Hb were effectively evaluated.
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