Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Andrew Semple"'
1
FTIR Spectroscopy Detects Intermolecular β-Sheet Formation Above the High Temperature Tm for Two Monoclonal Antibodies
Autor: Garrett Baird, Jeffery Blue, Jason K. Cheung, Andrew Semple, Chris Farrell, Patrick L. Ahl
Publikováno v: The Protein Journal. 39:318-327
The temperature-dependent secondary structure of two monoclonal IgG antibodies, anti-IGF1R and anti-TSLP, were examined by transmission mode Fourier Transform Infrared (FTIR) spectroscopy. Anti-IGF1R and anti-TSLP are IgG monoclonal antibodies (mAbs)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::092fb0096a7c8b0a3e89f32d801babc9
https://doi.org/10.1007/s10930-020-09907-y
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2
FTIR Spectroscopy Detects Intermolecular β-Sheet Formation Above the High Temperature T
Autor: Garrett, Baird, Chris, Farrell, Jason, Cheung, Andrew, Semple, Jeffery, Blue, Patrick L, Ahl
Publikováno v: The Protein Journal
The temperature-dependent secondary structure of two monoclonal IgG antibodies, anti-IGF1R and anti-TSLP, were examined by transmission mode Fourier Transform Infrared (FTIR) spectroscopy. Anti-IGF1R and anti-TSLP are IgG monoclonal antibodies (mAbs)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9fc066810565c07a3b40fa1d7861afcf
https://pubmed.ncbi.nlm.nih.gov/32656609
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3
A comparison of biophysical characterization techniques in predicting monoclonal antibody stability
Autor: Geetha Thiagarajan, Andrew Semple, Jose K. James, Mohammed Shameem, Jason K. Cheung
Publikováno v: mAbs. 8:1088-1097
With the rapid growth of biopharmaceutical product development, knowledge of therapeutic protein stability has become increasingly important. We evaluated assays that measure solution-mediated interactions and key molecular characteristics of 9 formu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efe21d969b8c9a29b0b9f920c7ea2ce5
https://doi.org/10.1080/19420862.2016.1189048
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4
Application of a High-Throughput Relative Chemical Stability Assay to Screen Therapeutic Protein Formulations by Assessment of Conformational Stability and Correlation to Aggregation Propensity
Autor: Daisy Richardson, Shuai Shi, Andrew Semple, Yunsong Li, Valentyn Antochshuk, Joseph M. Rizzo, Mohammed Shameem, Jessica J. Esposito, Shenjiang Yu
Publikováno v: Journal of Pharmaceutical Sciences. 104:1632-1640
In this study, an automated high-throughput relative chemical stability (RCS) assay was developed in which various therapeutic proteins were assessed to determine stability based on the resistance to denaturation post introduction to a chaotrope titr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06641857fae58ca16bc14feac0bba8c9
https://doi.org/10.1002/jps.24408
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5
Overcoming Challenges With Intravenous Administration of an Investigational Protein Therapeutic
Autor: Valentyn Antochshuk, Venus Hashemi, Chakravarthy Nachu Narasimhan, Monica Mei Yang, Jiong Yang, Shao-Chun Wang, Shuai Shi, Andrew Semple
Publikováno v: Journal of pharmaceutical sciences. 106(12)
Piggyback infusion has been widely used in the clinic with most applications in a nonconcurrent fashion for the purpose of administration convenience. In the present study, we demonstrated the application of concurrent piggyback to overcome challenge
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8cfadd4b9607cf03e9b5b3e7971e8fd
https://pubmed.ncbi.nlm.nih.gov/28778425
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6
DSF Method Optimization and Its Application in Predicting Protein Thermal Aggregation Kinetics
Autor: Andrew Semple, Shuai Shi, Jason K. Cheung, Mohammed Shameem
Publikováno v: Journal of Pharmaceutical Sciences. 102:2471-2483
Differential scanning fluorimetry (DSF) has gained wide acceptance in the therapeutic protein development. However, the effects of dyes and surfactants that may affect structural transitions have not been studied thoroughly to date. We therefore firs
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17fcafcc55bed88f63b3cf8b9d2399d8
https://doi.org/10.1002/jps.23633
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7
A Highly Sensitive Method for the Quantitation of Polysorbate 20 and 80 to Study the Compatibility between Polysorbates and m-Cresol in the Peptide Formulation
Autor: Shuai Shi, Jason K. Cheung, Sarita Mittal, Zhi Chen, Valentyn Antochshuk, Mohammed Shameem, Daisy Richardson, Andrew Semple, Joseph M. Rizzo
Publikováno v: Journal of Analytical & Bioanalytical Techniques.
A highly sensitive method has been developed for the quantitation of polysorbate 20 (PS20) and 80 (PS80) in therapeutic peptide formulations. A mixed-mode HPLC column was used to separate polysorbates from the peptide and other excipients, and a char
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f22211b742897c68d1a4dc0052c5d6f7
https://doi.org/10.4172/2155-9872.1000245
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