Academic Journal

To What Extent Do Fluorophores Bias the Biological Activity of Peptides? A Practical Approach Using Membrane-Active Peptides as Models

التفاصيل البيبلوغرافية
العنوان: To What Extent Do Fluorophores Bias the Biological Activity of Peptides? A Practical Approach Using Membrane-Active Peptides as Models
المؤلفون: Marco Cavaco, Clara Pérez-Peinado, Javier Valle, Rúben D. M. Silva, João D. G. Correia, David Andreu, Miguel A. R. B. Castanho, Vera Neves
المصدر: Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
بيانات النشر: Frontiers Media S.A., 2020.
سنة النشر: 2020
المجموعة: LCC:Biotechnology
مصطلحات موضوعية: anticancer peptides, BBB peptide shuttles, fluorescence, fluorophore, labeling, Biotechnology, TP248.13-248.65
الوصف: The characterization of biologically active peptides relies heavily on the study of their efficacy, toxicity, mechanism of action, cellular uptake, or intracellular location, using both in vitro and in vivo studies. These studies frequently depend on the use of fluorescence-based techniques. Since most peptides are not intrinsically fluorescent, they are conjugated to a fluorophore. The conjugation may interfere with peptide properties, thus biasing the results. The selection of the most suitable fluorophore is highly relevant. Here, a comprehensive study with blood–brain barrier (BBB) peptide shuttles (PepH3 and PepNeg) and antimicrobial peptides (AMPs) (vCPP2319 and Ctn[15-34]), tested as anticancer peptides (ACPs), having different fluorophores, namely 5(6)-carboxyfluorescein (CF), rhodamine B (RhB), quasar 570 (Q570), or tide fluor 3 (TF3) attached is presented. The goal is the evaluation of the impact of the selected fluorophores on peptide performance, applying routinely used techniques to assess cytotoxicity/toxicity, secondary structure, BBB translocation, and cellular internalization. Our results show that some fluorophores significantly modulate peptide activity when compared with unlabeled peptides, being more noticeable in hydrophobic and charged fluorophores. This study highlights the need for a careful experimental design for fluorescently labeled molecules, such as peptides.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2296-4185
Relation: https://www.frontiersin.org/article/10.3389/fbioe.2020.552035/full; https://doaj.org/toc/2296-4185
DOI: 10.3389/fbioe.2020.552035
URL الوصول: https://doaj.org/article/81a72c5e46694efeb31a6a682b0c2663
رقم الانضمام: edsdoj.81a72c5e46694efeb31a6a682b0c2663
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:22964185
DOI:10.3389/fbioe.2020.552035