Academic Journal

Microsphere Peptide-Based Immunoassay for the Detection of Recombinant Bovine Somatotropin in Injection Preparations

التفاصيل البيبلوغرافية
العنوان: Microsphere Peptide-Based Immunoassay for the Detection of Recombinant Bovine Somatotropin in Injection Preparations
المؤلفون: Nathalie G. E. Smits, Toine F. H. Bovee, Sidharam P. Pujari, Leendert A. van Ginkel, Michel W. F. Nielen, Bauke Albada
المصدر: Biosensors, Vol 12, Iss 3, p 138 (2022)
بيانات النشر: MDPI AG, 2022.
سنة النشر: 2022
المجموعة: LCC:Biotechnology
مصطلحات موضوعية: epitope mapping, recombinant bovine somatotropin, peptide-based immunoassay, suspension array, biorecognition, Biotechnology, TP248.13-248.65
الوصف: The use of peptides in immunoassays can be favored over the use of the full protein when more cost effective or less toxic approaches are needed, or when access to the full protein is lacking. Due to restricted access to recombinant bovine somatotropin (rbST), a protein enhancing growth and lactating performances of livestock, which use has been banned in the EU, Canada and Australia (amongst others), we developed a peptide-based biorecognition assay on an imaging planar array analyzer. For this, we identified the rbST epitope that is responsible for binding to the rbST-targeting monoclonal antibody 4H12 (MAb 4H12) to be 115DLEEGILALMR125. This linear peptide was synthesized and coupled to microspheres, after which it was tested in a biorecognition competitive inhibition assay format. We observed IC50 values of approximately 0.11 μg mL−1, which are lower than observed for the full rbST protein (IC50 = 0.20 μg mL−1). Importantly, there was no binding with the scrambled peptide. Preliminary results of directly coupled peptides in a microsphere biorecognition assay for detection of rbST are presented. Real-life applicability for detection of somatotropins (STs) in injection preparations of bovine-, porcine- and equine ST are shown. This newly developed immunoassay strongly supports future developments of peptide-based immunoassays to circumvent the limited access to the full protein.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2079-6374
Relation: https://www.mdpi.com/2079-6374/12/3/138; https://doaj.org/toc/2079-6374
DOI: 10.3390/bios12030138
URL الوصول: https://doaj.org/article/983fb76cbe5940a48de4dc67069d0d17
رقم الانضمام: edsdoj.983fb76cbe5940a48de4dc67069d0d17
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20796374
DOI:10.3390/bios12030138