کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5031341 1470933 2018 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Selection of affinity peptides for interference-free detection of cholera toxin
ترجمه فارسی عنوان
انتخاب پپتید های متفاوتی برای تشخیص تداخل توکسین کولر
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی


- A sensitive and interference-free plasmonic-based peptide sensor was developed.
- The detection performance for cholera toxin was monitored by LSPR and SERS.
- The limit of detection obtained by LSPR was 1.89 ng/mL, while SERS had 3.51 pg/mL.

Cholera toxin is a major virulent agent of Vibrio cholerae, and it can rapidly lead to severe dehydration, shock, causing death within hours without appropriate clinical treatments. In this study, we present a method wherein unique and short peptides that bind to cholera toxin subunit B (CTX-B) were selected through M13 phage display. Biopanning over recombinant CTX-B led to rapid screening of a unique peptide with an amino acid sequence of VQCRLGPPWCAK, and the phage-displayed peptides analyzed using ELISA, were found to show specific affinities towards CTX-B. To address the use of affinity peptides in development of the biosensor, sequences of newly selected peptides were modified and chemically synthesized to create a series of affinity peptides. Performance of the biosensor was studied using plasmonic-based optical techniques: localized surface plasmon resonance (LSPR) and surface-enhanced Raman scattering (SERS). The limit of detection (LOD) obtained by LSPR with 3σ-rule was 1.89 ng/mL, while SERS had a LOD of 3.51 pg/mL. In both cases, the sensitivity was much higher than the previously reported values, and our sensor system was specific towards actual CTX-B secreted from V. cholera, but not for CTX-AB5.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biosensors and Bioelectronics - Volume 99, 15 January 2018, Pages 289-295
نویسندگان
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