Switching-peptides for one-step immunoassay and its application to the diagnosis of human hepatitis B

Authors
Bong, Ji-HongKim, Hong-RaeJung, JaeyongPark, Jun-HeeSung, Jeong SooLee, Chang KyuChoi, Kyung-HakShin, Seong-ShickKang, Min-JungKim, Hyun OkLee, Do YoungPyun, Jae-Chul
Issue Date
2021-04-15
Publisher
ELSEVIER ADVANCED TECHNOLOGY
Citation
BIOSENSORS & BIOELECTRONICS, v.178
Abstract
Herein, we present switching-peptides for a one-step immunoassay, without the need for additional antibody treatment or washing steps to detect antigen-antibody interactions. Fluorescently labeled switching-peptides were dissociated from the immobilized antibody soon after the antigens were bound to the binding pockets. In this study, four different parts of the antibody (IgG) frame regions were chemically synthesized, and these peptides were bound to immobilized antibodies as switching-peptides. We presented the design principle of switching-peptides and used Pymol software, based on the changes in thermodynamic parameters, to study the interaction between antibodies and switching-peptides. The binding properties of switching-peptides were analyzed based on Forster resonance energy transfer between switching-peptides as well as between switching-peptides and antibodies (IgGs) isolated from different animals. The binding constants of the four switching-peptides to antibodies were estimated to be in the range of 1.48-3.29 mu M. Finally, the feasibility of using switching-peptides for the quantitative one-step immunoassay was demonstrated by human hepatitis B surface antigen (hHBsAg) detection and statistical comparison of the assay results with those of conventional ELISA. The limit of detection for HBsAg was determined to be 56 ng/mL, and the dynamic range was estimated to be 136 ng/mL-33 mu g/mL. These results demonstrate the feasibility of the one-step immunoassay for HBsAg.
Keywords
Switching-peptide; One-step immunoassay; Frame region; Hepatitis; Medical diagnosis
ISSN
0956-5663
URI
https://pubs.kist.re.kr/handle/201004/117126
DOI
10.1016/j.bios.2021.112996
Appears in Collections:
KIST Article > 2021
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