Label-free analysis of protein biomarkers using pattern-optimized graphene-nanopyramid SERS for rapid diagnosis of Alzheimer’s disease

dc.contributor.authorWu, Heping
dc.contributor.authorDuan, Yan
dc.contributor.authorJiang, Luyue
dc.contributor.authorCao, Xinhao
dc.contributor.authorXie, Zhen
dc.contributor.authorQuan, Yi
dc.contributor.authorRen, Matthew Xinhu
dc.contributor.authorWu, Shengli
dc.contributor.authorZhang, Nan
dc.contributor.authorYang, Zhugen
dc.contributor.authorZhao, Libo
dc.contributor.authorJiang, Zhuangde
dc.contributor.authorZhao, Gang
dc.contributor.authorRen, Wei
dc.contributor.authorNiu, Gang
dc.date.accessioned2024-04-19T13:04:27Z
dc.date.available2024-04-19T13:04:27Z
dc.date.issued2024-04-05
dc.description.abstractThe quantitative and highly sensitive detection of biomarkers such as Tau proteins and Aβ polypeptides is considered one of the most effective methods for the early diagnosis of Alzheimer’s disease (AD). Surface-enhanced Raman spectroscopy (SERS) detection is a promising method that faces, however, challenges like insufficient sensitivity due to the non-optimized nanostructures for specialized analyte sizes and insufficient control of the location of SERS hot spots. Thus, the SERS detection of AD biomarkers is restricted. We reported here an in-depth study of the analytical Raman enhancement factor (EF) of the wafer-scale graphene-Au nanopyramid hybrid SERS substrates using a combination of both theoretical calculation and experimental measurements. Experimental results show that larger nanopyramids and smaller gap spacing lead to a larger SERS EF, with an optimized analytical EF up to 1.1 × 1010. The hybrid SERS substrate exhibited detection limits of 10–15 M for Tau and phospho-Tau (P-Tau) proteins and 10–14 M for Aβ polypeptides, respectively. Principal component analysis correctly categorized the SERS spectra of different biomarkers at ultralow concentrations (10–13 M) using the optimized substrate. Amide III bands at 1200–1300 cm–1 reflect different structural conformations of proteins or polypeptides. Tau and P-Tau proteins are inherently disordered with a few α-helix residuals. The structure of Aβ42 polypeptides transitioned from the α-helix to the β-sheet as the concentration increased. These results demonstrate that the hybrid SERS method could be a simple and effective way for the label-free detection of protein biomarkers to enable the rapid early diagnosis of AD and other diseases.en_UK
dc.identifier.citationWu H, Duan Y, Jiang L, et al., (2024) Label-free analysis of protein biomarkers using pattern-optimized graphene-nanopyramid SERS for rapid diagnosis of Alzheimer’s disease. ACS Applied Nano Materials, Volume 7, Issue 8, April 2024, pp. 8377-9815en_UK
dc.identifier.eissn2574-0970
dc.identifier.urihttps://doi.org/10.1021/acsanm.4c00674
dc.identifier.urihttps://dspace.lib.cranfield.ac.uk/handle/1826/21232
dc.language.isoen_UKen_UK
dc.publisherAmerican Chemical Societyen_UK
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectlabel-free detectionen_UK
dc.subjectsurface-enhanced Raman spectroscopyen_UK
dc.subjectAlzheimer’s diseaseen_UK
dc.subjectphospho-Tau proteinen_UK
dc.subjectAβ42 polypeptideen_UK
dc.subjectprotein secondary structureen_UK
dc.titleLabel-free analysis of protein biomarkers using pattern-optimized graphene-nanopyramid SERS for rapid diagnosis of Alzheimer’s diseaseen_UK
dc.typeArticleen_UK
dcterms.dateAccepted2024-03-26

Files

Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
Label-free_analysis_of_protein_biomarkers-2024.pdf
Size:
4.12 MB
Format:
Adobe Portable Document Format
Description:
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.63 KB
Format:
Item-specific license agreed upon to submission
Description: