Evidence map›Paper›PMID 36944950›Full record

ArticleJournal of nanobiotechnology2023

Harnessing protein sensing ability of electrochemical biosensors via a controlled peptide receptor-electrode interface.

Ji Hong Kim, Jae Hwan Shin, Bumjun Park, Chae Hwan Cho, Yun Suk Huh, Chang-Hyung Choi, Jong Pil Park

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Article in Journal of nanobiotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Ji Hong KimBasic Research Laboratory, Department of Food Science and Technology, Chung-Ang University, Anseong, 17546, Republic of Korea.
Jae Hwan ShinBasic Research Laboratory, Department of Food Science and Technology, Chung-Ang University, Anseong, 17546, Republic of Korea.
Bumjun ParkNanoBio High-Tech Materials Research Center, Department of Biological Sciences and Bioengineering, Inha University, 100 Inha-Ro, Incheon, 22212, Republic of Korea.
Chae Hwan ChoBasic Research Laboratory, Department of Food Science and Technology, Chung-Ang University, Anseong, 17546, Republic of Korea.
Yun Suk HuhNanoBio High-Tech Materials Research Center, Department of Biological Sciences and Bioengineering, Inha University, 100 Inha-Ro, Incheon, 22212, Republic of Korea.
Chang-Hyung ChoiSchool of Chemical Engineering, Yeungnam University, 280 Daehak-ro, Gyeongsan, Gyeongbuk, 38541, Republic of Korea.
Jong Pil ParkBasic Research Laboratory, Department of Food Science and Technology, Chung-Ang University, Anseong, 17546, Republic of Korea. jppark@cau.ac.kr.

Funding

Ministry of Food and Drug Safety 21153MFDS605National Research Foundation of Korea 2021R1A4A1022206
6 · The paper itself

Abstract

backgroundCathepsin B, a cysteine protease, is considered a potential biomarker for early diagnosis of cancer and inflammatory bowel diseases. Therefore, more feasible and effective diagnostic method may be beneficial for monitoring of cancer or related diseases.

resultsA phage-display library was biopanned against biotinylated cathepsin B to identify a high-affinity peptide with the sequence WDMWPSMDWKAE. The identified peptide-displaying phage clones and phage-free synthetic peptides were characterized using enzyme-linked immunosorbent assays (ELISAs) and electrochemical analyses (impedance spectroscopy, cyclic voltammetry, and square wave voltammetry). Feasibilities of phage-on-a-sensor, peptide-on-a-sensor, and peptide-on-a-AuNPs/MXene sensor were evaluated. The limit of detection and binding affinity values of the peptide-on-a-AuNPs/MXene sensor interface were two to four times lower than those of the two other sensors, indicating that the peptide-on-a-AuNPs/MXene sensor is more specific for cathepsin B (good recovery (86-102%) and %RSD (< 11%) with clinical samples, and can distinguish different stages of Crohn's disease. Furthermore, the concentration of cathepsin B measured by our sensor showed a good correlation with those estimated by the commercially available ELISA kit.

conclusionIn summary, screening and rational design of high-affinity peptides specific to cathepsin B for developing peptide-based electrochemical biosensors is reported for the first time. This study could promote the development of alternative antibody-free detection methods for clinical assays to test inflammatory bowel disease and other diseases.

Indexed as

Biosensing TechniquesMetal NanoparticlesCathepsin BEnzyme-Linked Immunosorbent AssayGoldNitritesPeptide LibraryPeptidesTransition ElementsCathepsin BGoldMXeneNitritesPeptide LibraryPeptidesTransition ElementsAffinity peptideBiomarkerCathepsin BDiagnosisElectrochemistry

Identifiers

PMID36944950
PMCPMC10029155

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.