Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry-Reference-Cited by-同舟云学术

Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry

Published:2018 Issue:3 Volume:143 Page:670-677
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Wang Guanbo¹²³⁴⁵^ORCID,Bondarenko Pavel V.⁶⁷⁸⁹¹⁰,Kaltashov Igor A.¹¹¹²¹³¹⁴

Affiliation:

1. Jiangsu Collaborative Innovation Center of Biomedical Functional Materials

2. Jiangsu Key Laboratory of Biomedical Materials

3. and School of Chemistry and Materials Science

4. Nanjing Normal University

5. Nanjing

6. Attribute Sciences

7. Process Development

8. Amgen

9. Inc.

10. Thousand Oaks

11. Department of Chemistry

12. University of Massachusetts-Amherst

13. Amherst

14. USA

Abstract

Sequential and small-scale conformational changes of monoclonal antibodies and antithrombin are characterized in real time in a temperature-controlled fashion.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/AN/C7AN01655G

Reference83 articles.

1. Comprehensive Characterization of Relationship Between Higher-Order Structure and FcRn Binding Affinity of Stress-Exposed Monoclonal Antibodies

2. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life

3. Protein aggregation and its inhibition in biopharmaceutics

4. W. Wang and C. J.Roberts , Aggregation of Therapeutic Proteins , John Wiley & Sons, Inc. , 2010

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