{"id":448,"date":"2019-01-29T10:05:13","date_gmt":"2019-01-29T15:05:13","guid":{"rendered":"http:\/\/elements.chem.umass.edu\/kaltashovlab\/?page_id=448"},"modified":"2023-07-13T10:20:33","modified_gmt":"2023-07-13T14:20:33","slug":"design-of-novel-methods-for-the-biopharmaceutical-analysis","status":"publish","type":"page","link":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/design-of-novel-methods-for-the-biopharmaceutical-analysis\/","title":{"rendered":"Design of novel methods for the biopharmaceutical analysis"},"content":{"rendered":"

 <\/p>\n

Our group had been involved in collaborative work with several biopharmaceutical companies for over a decade. Working in close partnership with analytical chemists at Biogen IDEC and Shire Human Genetic Therapies, we were the first group to use hydrogen\/deuterium exchange with MS detection as a means of assessing conformational integrity of protein therapeutics and the impact of stress-related post-translational modifications on the stability of biopharmaceutical products.<\/p>\n

We continue to advance the field of bioanalysis in the BioPharma sector and work with our industrial partners on characterizing a range of complex therapeutic products ranging from PEGylated interferon<\/a> and monoclonal antibodies<\/a> (Biogen) to extensively glycosylated proteins used in enzyme replacement therapies<\/a> (Shire) and protein-haptene conjugates in vaccines<\/a> (Pfizer).<\/p>\n

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The analytical methods developed in our laboratory have been widely adopted by the industry<\/a>. Close collaboration with the BioPharma sector also provides excellent opportunities for both undergraduate and graduate students to make connections to potential employers and gain meaningful “industrial experience” prior to graduation. This is one of the main reasons the vast majority of our alumni have successful careers in the BioPharma.<\/p>\n

Representative publications<\/strong>:<\/p>\n

    \n
  1. M.J. Chang, M. Ollivault-Shiflett, R. Schuman, S. Ngoc Nguyen, I.A. Kaltashov, C. Bobst, S.P. Rajagopal, A. Przedpelski, J.T. Barbieri, A. Lees. Genetically detoxified tetanus toxin as a vaccine and conjugate carrier protein<\/u><\/a>. Vaccine <\/em>2022<\/strong>, 40<\/em>, 5103-5113<\/li>\n
  2. C.E. Bobst, J. Sperry, O. Friese and I.A. Kaltashov. Simultaneous evaluation of a vaccine component micro-heterogeneity and conformational integrity using native mass spectrometry and limited charge reduction<\/a>. J. Am. Soc. Mass Spectrom<\/em>. 2021<\/strong>, 32<\/span><\/em>, <\/span>1631\u20131637<\/span><\/li>\n
  3. I.A. Kaltashov, C.E. Bobst, J.W. Pawlowski and G. Wang. Mass spectrometry-based methods in characterization of the higher order structure of protein therapeutics<\/a>. J. Pharm. Biomed. Anal.<\/em>, 2020<\/strong>, 184<\/em>, 113169<\/li>\n
  4. J.W. Pawlowski, A. Bajardi-Taccioli, D. Houde, M. Feschenko, T. Carlage, I.A. Kaltashov. Influence of glycan modification on IgG1 biochemical and biophysical properties<\/u>. J. Pharm. Biomed. Anal.<\/em>, 2018<\/strong>, 151<\/em>, 133-144<\/li>\n
  5. G. Wang, P.V. Bondarenko and I.A. Kaltashov. Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry<\/u>. Analyst<\/em>, 2018<\/strong>, 143<\/em>, 670-677<\/li>\n
  6. K. Muneeruddin, C.E. Bobst, R. Frenkel, D. Houde, I. Turyan, Z. Sosic and I.A. Kaltashov. Characterization of a PEGylated protein therapeutic by ion exchange chromatography with on-line detection by native ESI MS and MS\/MS<\/u>. Analyst<\/em> 2017<\/strong>, 142, 336<\/li>\n
  7. K. Muneeruddin, J.J. Thomas, P.A. Salinas and I.A. Kaltashov. Characterization of small protein aggregates and oligomers using size exclusion chromatography with on-line detection by native electrospray ionization mass spectrometry<\/u>. Anal. Chem<\/em>. 2014<\/strong>, 86<\/em>, 10692-10699<\/li>\n
  8. R.R. Abzalimov, C.E. Bobst, P.A. Salinas, P. Savickas, J.J. Thomas, and I.A. Kaltashov. Studies of pH-dependent self-association of a recombinant form of arylsulfatase A with electrospray ionization mass spectrometry and size-exclusion chromatography<\/u>. Anal. Chem<\/em>. <\/em>2013<\/strong>, 85<\/em>, 1591-1596<\/li>\n
  9. I.A. Kaltashov, C.E. Bobst, R.R. Abzalimov, G. Wang, B. Baykal, S. Wang. Advances and challenges in analytical characterization of biotechnology products: Mass spectrometry-based approaches to study properties and behavior of protein therapeutics<\/u>. Biotechnol. Adv<\/em>., 2012<\/strong>, 30<\/em>, 210-222<\/li>\n
  10. C.E. Bobst, J.J. Thomas, P.A. Salinas, P. Savickas, I.A. Kaltashov. Impact of oxidation on protein therapeutics: Conformational dynamics of intact and oxidized acid-\u03b2-glucocerebrosidase at near-physiological pH<\/u>. Protein Sci<\/em>.<\/em> 2010<\/strong>, 19<\/em>, 2366-2378<\/li>\n
  11. I.A. Kaltashov, C.E. Bobst, R.R. Abzalimov, S.A. Berkowitz, D. Houde. Conformation and dynamics of biopharmaceuticals: transition of mass spectrometry<\/u>-based tools from academe to industry<\/u>. J. Am. Soc. Mass Spectrom<\/em>. 2010<\/strong>, 21<\/em>, 323-337<\/li>\n
  12. C.E. Bobst, R.R. Abzalimov, D. Houde, M. Kloczewiak, R. Mhatre, S.A. Berkowitz, I.A. Kaltashov. Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches<\/u>. Anal. Chem<\/em>. 2008<\/strong>, 80<\/em>, 7473-7481<\/li>\n<\/ol>\n

    \"\"<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"

      Our group had been involved in collaborative work with several biopharmaceutical companies for over a decade. Working in close partnership with analytical chemists at Biogen IDEC and Shire Human Genetic Therapies, we were the first group to use hydrogen\/deuterium exchange with MS detection as a means of assessing conformational integrity of protein therapeutics and … Continue reading Design of novel methods for the biopharmaceutical analysis<\/span><\/a><\/p>\n","protected":false},"author":71,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-448","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages\/448","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/users\/71"}],"replies":[{"embeddable":true,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/comments?post=448"}],"version-history":[{"count":17,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages\/448\/revisions"}],"predecessor-version":[{"id":1342,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages\/448\/revisions\/1342"}],"wp:attachment":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/media?parent=448"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}