title: Investigation of pH-induced protein conformation changes by nanomechanical deflection.
abstract: Broad-spectrum biosensing technologies examine sensor signals using biomarkers, such as proteins, DNA, antibodies, specific cells, and macromolecules, based on direct- or indirect-conformational changes. Here, we have investigated the pH-dependent conformational isomerization of human serum albumin (HSA) using microcantilevers as a sensing platform. Native and denatured proteins were immobilized on cantilever surfaces to understand the effect of pH on conformational changes of the protein with respect to the coupling ligand. Our results show that protonation and deprotonation of amino acid residues on proteins play a significant role in generating charge-induced cantilever deflection. Surface plasmon resonance (SPR) was employed as a complementary technique to validate the results.
authors: Department of Chemical and Materials Engineering, University of Alberta , Edmonton, Alberta T6G 2 V4, Canada.
authors: Garima
authors: G
authors: Thakur
authors: Keren
authors: K
authors: Jiang
authors: Dongkyu
authors: D
authors: Lee
authors: Kovur
authors: K
authors: Prashanthi
authors: Seonghwan
authors: S
authors: Kim
authors: Thomas
authors: T
authors: Thundat
mesh_terms: D015374:Biosensing Techniques / Q000379:methods*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*
chemical_list: D012709:Serum Albumin