Before considering the different questions related to this interview, we need to know about the definition of “Bioanalysis”: “Bioanalysis is a sub-discipline of analytical chemistry covering the quantitative determination of xenobiotics (e.g. drugs, metabolites, and biological molecules in atypical locations or concentrations) and biotics (e.g. macromolecules, proteins, DNA, large molecule drugs, metabolites, biopharmaceuticals) in biological systems. Its main focus in the pharmaceutical field is to provide quantitative information about the active drug and/or its metabolite(s) for pharmacokinetics, toxicokinetics, bioequivalence, exposure-response, and adsorption/distribution/ metabolism/excretion (ADME). Bioanalysis also applies to drugs used for non-specific purposes, forensic investigations, anti-doping testing, and environmental concerns”. University “G. d’ Annunzio” of Chieti-Pescara, Department of Pharmacy, Chieti, Italy.
{"title":"Perspectives on the Multidisciplinary role of Bioanalysis: an Interview with Prof. Marcello Locatelli","authors":"M. Locatelli","doi":"10.17145/jab.20.009","DOIUrl":"https://doi.org/10.17145/jab.20.009","url":null,"abstract":"Before considering the different questions related to this interview, we need to know about the definition of “Bioanalysis”: “Bioanalysis is a sub-discipline of analytical chemistry covering the quantitative determination of xenobiotics (e.g. drugs, metabolites, and biological molecules in atypical locations or concentrations) and biotics (e.g. macromolecules, proteins, DNA, large molecule drugs, metabolites, biopharmaceuticals) in biological systems. Its main focus in the pharmaceutical field is to provide quantitative information about the active drug and/or its metabolite(s) for pharmacokinetics, toxicokinetics, bioequivalence, exposure-response, and adsorption/distribution/ metabolism/excretion (ADME). Bioanalysis also applies to drugs used for non-specific purposes, forensic investigations, anti-doping testing, and environmental concerns”. University “G. d’ Annunzio” of Chieti-Pescara, Department of Pharmacy, Chieti, Italy.","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84269860","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Perspectives on Microsampling in Bioanalysis: Opportunities and Challenges in the era of the COVID-19 pandemic-an Interview with Dr. Kevin P. Bateman","authors":"K. Bateman","doi":"10.17145/JAB.21.005","DOIUrl":"https://doi.org/10.17145/JAB.21.005","url":null,"abstract":"","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86625436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M. Amaral, Soraya Hölper, Christian Lange, Jennifer Jung, H. Sjuts, Sandra Weil, M. Fischer, Katarina Radoevic, Ercole Rao
The idea of designing multispecific antibodies capable of simultaneously engaging two or more epitopes on the same or different antigens was developed more than 50 years ago. However, the molecular complexity of such molecules may pose significant challenges for their development and clinical use. Particularly challenging is to obtain the correctly assembled combination of different polypeptide chains, which places significant demand on downstream process development, analytical characterization and control strategy. Here, we review the progress made in protein engineering to force the correct assembly of different heavy and light chains, as well as upstream and downstream processes currently applied to control generation of unwanted byproduct species. We cover in-depth the analytical methods available to characterize such complex molecules, focusing on mispairing analysis and functional characterization.
{"title":"Engineered Technologies and Bioanalysis of multispecific Antibody Formats","authors":"M. Amaral, Soraya Hölper, Christian Lange, Jennifer Jung, H. Sjuts, Sandra Weil, M. Fischer, Katarina Radoevic, Ercole Rao","doi":"10.17145/jab.20.005","DOIUrl":"https://doi.org/10.17145/jab.20.005","url":null,"abstract":"The idea of designing multispecific antibodies capable of simultaneously engaging two or more epitopes on the same or different antigens was developed more than 50 years ago. However, the molecular complexity of such molecules may pose significant challenges for their development and clinical use. Particularly challenging is to obtain the correctly assembled combination of different polypeptide chains, which places significant demand on downstream process development, analytical characterization and control strategy. Here, we review the progress made in protein engineering to force the correct assembly of different heavy and light chains, as well as upstream and downstream processes currently applied to control generation of unwanted byproduct species. We cover in-depth the analytical methods available to characterize such complex molecules, focusing on mispairing analysis and functional characterization.","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73012418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Meet our Editorial Board Member: Dr. William van Dongen","authors":"WD van Dongen","doi":"10.17145/jab.20.002","DOIUrl":"https://doi.org/10.17145/jab.20.002","url":null,"abstract":"","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90877750","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
I welcome you to the journal’s fifth volume. As I also did in previous three years, I’ll start this foreword article with taking the opportunity to wish all of you a successful 2019. A special “thank you” is going out to all our authors, and reviewers, as well to the journal’s editorial board for their continued professional support. I hope that 2019 will hold for your success and good fortune in any endeavor you will pursue in the year that’s ahead of you. In the this foreword article, I’ll look back at the journal’s past year’s achievements and special moments.
{"title":"Welcome to the sixth Volume of Journal of Applied Bioanalysis","authors":"R. Meesters","doi":"10.17145/jab.20.001","DOIUrl":"https://doi.org/10.17145/jab.20.001","url":null,"abstract":"I welcome you to the journal’s fifth volume. As I also did in previous three years, I’ll start this foreword article with taking the opportunity to wish all of you a successful 2019. A special “thank you” is going out to all our authors, and reviewers, as well to the journal’s editorial board for their continued professional support. I hope that 2019 will hold for your success and good fortune in any endeavor you will pursue in the year that’s ahead of you. In the this foreword article, I’ll look back at the journal’s past year’s achievements and special moments.","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79452655","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Catherine E. DelGuidice, O. Ismaiel, William R. Mylott Jr, M. Halquist
As biologic drugs become an increasing segment in the overall pharmaceutical market, it is important to develop accurate and reliable methods to analyze these drugs in biological matrices. With advancements in technology, biologics’ complex molecular structures can now be selectivity distinguished and quantified using high-resolution mass spectrometry and deconvolution software. Intact (top-down) mass spectrometric techniques have been established as alternative or complementary bioanalytical techniques for instances when ligand binding assays (LBAs) alone were not well suited, as it can provide additional structural information, in its pharmacologically active form.
{"title":"Quantitative Bioanalysis of Intact Large Molecules using Mass Spectrometry","authors":"Catherine E. DelGuidice, O. Ismaiel, William R. Mylott Jr, M. Halquist","doi":"10.17145/jab.20.006","DOIUrl":"https://doi.org/10.17145/jab.20.006","url":null,"abstract":"As biologic drugs become an increasing segment in the overall pharmaceutical market, it is important to develop accurate and reliable methods to analyze these drugs in biological matrices. With advancements in technology, biologics’ complex molecular structures can now be selectivity distinguished and quantified using high-resolution mass spectrometry and deconvolution software. Intact (top-down) mass spectrometric techniques have been established as alternative or complementary bioanalytical techniques for instances when ligand binding assays (LBAs) alone were not well suited, as it can provide additional structural information, in its pharmacologically active form.","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73693018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
entering clinical studies [1]. The popularity is attributed to the high selectivity of these drugs which enhances their efficacy and reduces systemic toxicity, in turn, increasing the therapeutic index. In addition, antibody-based biotherapeutics have long circulatory half-lives and are less likely to undergo significant biotransformation in vivo. Since the approval of the first monoclonal antibody (mAb) drug (Orthoclone OKT3®) in the 1980s, the number of antibody-based biotherapeutics on the market and in development has reached several hundred. Recent advancements in antibody engineering and manufacturing techniques have led to generation of new biotherapeutic modalities such as multispecific mAbs, antibody-drug conjugates, ProbodyTM therapeutics and ProbodyTM drug conjugates, PEGylated antibody fragments and fragment crystallizable (Fc)-fusion proteins. The increasing complexity of the new biotherapeutic modalities pose newer bioanalytical challenges. In some instances, multiple bioanalytical assays using different analytical platforms are required to address the pharmacokinetic characterization of these new modalities.
{"title":"Addressing Bioanalytical Needs of Antibody-Based Biotherapeutics by LC-MS","authors":"Morse Faria","doi":"10.17145/jab.20.003","DOIUrl":"https://doi.org/10.17145/jab.20.003","url":null,"abstract":"entering clinical studies [1]. The popularity is attributed to the high selectivity of these drugs which enhances their efficacy and reduces systemic toxicity, in turn, increasing the therapeutic index. In addition, antibody-based biotherapeutics have long circulatory half-lives and are less likely to undergo significant biotransformation in vivo. Since the approval of the first monoclonal antibody (mAb) drug (Orthoclone OKT3®) in the 1980s, the number of antibody-based biotherapeutics on the market and in development has reached several hundred. Recent advancements in antibody engineering and manufacturing techniques have led to generation of new biotherapeutic modalities such as multispecific mAbs, antibody-drug conjugates, ProbodyTM therapeutics and ProbodyTM drug conjugates, PEGylated antibody fragments and fragment crystallizable (Fc)-fusion proteins. The increasing complexity of the new biotherapeutic modalities pose newer bioanalytical challenges. In some instances, multiple bioanalytical assays using different analytical platforms are required to address the pharmacokinetic characterization of these new modalities.","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81135244","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Investigation of Potential in vivo Cleavage of Biotherapeutic Protein by Immunocapture-LC/MS","authors":"Lin-Zhi Chen, Shan Jiang, D. Roos, Hongbin Yu","doi":"10.17145/jab.20.004","DOIUrl":"https://doi.org/10.17145/jab.20.004","url":null,"abstract":"","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87651372","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
E. Jurgens, EJ Knaven, N. Zheng, EC Hegeman, MW van Gemert, JM Emmen, I Willemen, Y. Mulder, L Ijsselstijn, B. D. Rooij, TH Noij
Table S1. Obervations for the investigated potential interferences. Name [M+H]+ (m/z) Retention time (min.) Potentially interference tested for Retention time difference 11α-hydroxyprogesterone 331.2 17α-hydroxyprogesterone 11β-hydroxyprogesterone 331.2 10.50 17α-hydroxyprogesterone 1.10 21-hydroxyprogesterone 331.2 10.16 17α-hydroxyprogesterone 1.44 β-estradiol-6-one 287.2 Androstenedione Aldosterone 361.2 4.94 Cortisone 0.86 Corticosterone 347.2 7.31 21-deoxycortisol 0.00 11-deoxycortisol 0.29 Dehydroepiandrosterone 289.2 Testosterone Epitestosterone 289.2 11.30 Testosterone 1.90 Estriol 289.2 Testosterone Fenofibrate 361.8 Cortisone Prednisolone 361.2 5.57 Cortisone 0.23 = indicates that the analysis of that component did not result in a response in the current method.
{"title":"Quantitative Profiling of Seven Steroids in Saliva using LC-MS/MS","authors":"E. Jurgens, EJ Knaven, N. Zheng, EC Hegeman, MW van Gemert, JM Emmen, I Willemen, Y. Mulder, L Ijsselstijn, B. D. Rooij, TH Noij","doi":"10.17145/JAB.19.006","DOIUrl":"https://doi.org/10.17145/JAB.19.006","url":null,"abstract":"Table S1. Obervations for the investigated potential interferences. Name [M+H]+ (m/z) Retention time (min.) Potentially interference tested for Retention time difference 11α-hydroxyprogesterone 331.2 17α-hydroxyprogesterone 11β-hydroxyprogesterone 331.2 10.50 17α-hydroxyprogesterone 1.10 21-hydroxyprogesterone 331.2 10.16 17α-hydroxyprogesterone 1.44 β-estradiol-6-one 287.2 Androstenedione Aldosterone 361.2 4.94 Cortisone 0.86 Corticosterone 347.2 7.31 21-deoxycortisol 0.00 11-deoxycortisol 0.29 Dehydroepiandrosterone 289.2 Testosterone Epitestosterone 289.2 11.30 Testosterone 1.90 Estriol 289.2 Testosterone Fenofibrate 361.8 Cortisone Prednisolone 361.2 5.57 Cortisone 0.23 = indicates that the analysis of that component did not result in a response in the current method.","PeriodicalId":15014,"journal":{"name":"Journal of Applied Bioanalysis","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80266794","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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