O'Donohue, Matthew Ghimire, Madhav L. Lee, Sangyoup Kim, Min Jun 2024-02-07T05:11:38Z 2024-02-07T05:11:38Z 2024-02-07 2024-01 0021-9606 https://pubs.kist.re.kr/handle/201004/148524 Transferrin, a central player in iron transport, has been recognized not only for its role in binding iron but also for its interaction with other metals, including titanium. This study employs solid-state nanopores to investigate the binding of titanium ions [Ti(IV)] to transferrin in a single-molecule and label-free manner. We demonstrate the novel application of solid-state nanopores for single-molecule discrimination between apo-transferrin (metal-free) and Ti(IV)-transferrin. Despite their similar sizes, Ti(IV)-transferrin exhibits a reduced current drop, attributed to differences in translocation times and filter characteristics. Single-molecule analysis reveals Ti(IV)-transferrin's enhanced stability and faster translocations due to its distinct conformational flexibility compared to apo-transferrin. Furthermore, our study showcases solid-state nanopores as real-time monitors of biochemical reactions, tracking the gradual conversion of apo-transferrin to Ti(IV)-transferrin upon the addition of titanium citrate. This work offers insights into Ti(IV) binding to transferrin, promising applications for single-molecule analysis and expanding our comprehension of metal-protein interactions at the molecular level. English American Institute of Physics Real-time monitoring of Ti(IV) metal ion binding of transferrin using a solid-state nanopore Article 10.1063/5.0185590 1 The Journal of Chemical Physics, v.160, no.4 The Journal of Chemical Physics 160 4 N scie scopus 001151329300005 2-s2.0-85183503692 Chemistry, Physical Physics, Atomic, Molecular & Chemical Chemistry Physics Article CITRATE SERUM SPECIATION COMPLEXES TRANSPORT IRON PROTEIN