Investigation of pH-induced protein conformation changes by nanomechanical deflection
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...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 30(2014), 8 vom: 04. März, Seite 2109-16 |
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| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Serum Albumin |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 20.10.2014 Date Revised 05.03.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la403981t |