Production of a phage-displayed mouse ScFv antibody against fumonisin B1 and molecular docking analysis of their interactions

摘要: Fumonisins produced by Fusarium pathogens are mycotoxins present in maize and other grains the field as well during storage worldwide pose a serious threat to humans domestic animals. Fumonisin B consists of different chemotypes, fumonisin B1 (FB1) is most predominant found food/feed commodities. Recombinant antibody can be deployed analyze toxicological mechanism develop simple cost-effective method for detection fumonisins, which vitally important monitoring preventing fumonisins from entering chains. In this study, FB1 conjugated keyhole limpet hemocyanin was used immunize mice, RNA isolated construct recombinant library. Successive panning library phage display select monoclonal clones reactive bovine serum albumin. Subsequent ELISA sequencing analyses revealed four scFv antibodies specific FB1. Soluble expression analysis showed that one antibody, FBMA1, had highest reactivity could purified bacterial cells large quantities. Surface plasmon resonance measurements further FBMA1 binding kinetics K D = 1.89 × 10–7 M. Molecular modeling docking suggested shaped proper cavity embed whole molecule steady-state complex formed relying on intermolecular forces, including hydrogen bonding, electrostatic force hydrophobic interactions. Thus, applied mechanistic studies interactions toxicity, development an immunoassay fumonisin-contaminated samples.