Progress in Top-Down LC-MS Analysis of Antibodies: Review
Antibodies are large heterogenous proteins due to post-translational modifications, including glycosylation. Structural analysis of antibodies by mass spectrometry has been of great interest recently, especially in the pharmaceutical industry. Over the past decade, bottom-up mass spectrometry has be...
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| Published in | Biotechnology and bioprocess engineering Vol. 28; no. 1; pp. 226 - 233 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Seoul
The Korean Society for Biotechnology and Bioengineering
01.02.2023
Springer Nature B.V 한국생물공학회 |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1226-8372 1976-3816 |
| DOI | 10.1007/s12257-023-0011-x |
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| Abstract | Antibodies are large heterogenous proteins due to post-translational modifications, including glycosylation. Structural analysis of antibodies by mass spectrometry has been of great interest recently, especially in the pharmaceutical industry. Over the past decade, bottom-up mass spectrometry has been widely used to identify single protein targets and whole proteomes from a biological system such as a cell, tissue, or organism. However, due to the protein inference problem in bottom-up mass spectrometry, this approach has intrinsic limitations for characterizing the post-translationally modified forms of proteins such as antibodies. In contrast to bottom-up mass spectrometry measuring peptides produced from proteins by proteolytic digestion, top-down mass spectrometry is a powerful technology that allows measuring proteins without proteolysis, thus characterizing intact forms of proteins, which provides information on primary sequences, including modifications characterization. In this review, we outline some progress in the separation, ionization, and fragmentation of intact proteins for top-down mass spectrometry and the growing power of intact protein-resolved measurements in biotechnology. |
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| AbstractList | Antibodies are large heterogenous proteins due to post-translational modifications, including glycosylation. Structural analysis of antibodies by mass spectrometry has been of great interest recently, especially in the pharmaceutical industry. Over the past decade, bottom-up mass spectrometry has been widely used to identify single protein targets and whole proteomes from a biological system such as a cell, tissue, or organism. However, due to the protein inference problem in bottom-up mass spectrometry, this approach has intrinsic limitations for characterizing the post-translationally modified forms of proteins such as antibodies. In contrast to bottom-up mass spectrometry measuring peptides produced from proteins by proteolytic digestion, top-down mass spectrometry is a powerful technology that allows measuring proteins without proteolysis, thus characterizing intact forms of proteins, which provides information on primary sequences, including modifications characterization. In this review, we outline some progress in the separation, ionization, and fragmentation of intact proteins for top-down mass spectrometry and the growing power of intact proteinresolved measurements in biotechnology. KCI Citation Count: 0 Antibodies are large heterogenous proteins due to post-translational modifications, including glycosylation. Structural analysis of antibodies by mass spectrometry has been of great interest recently, especially in the pharmaceutical industry. Over the past decade, bottom-up mass spectrometry has been widely used to identify single protein targets and whole proteomes from a biological system such as a cell, tissue, or organism. However, due to the protein inference problem in bottom-up mass spectrometry, this approach has intrinsic limitations for characterizing the post-translationally modified forms of proteins such as antibodies. In contrast to bottom-up mass spectrometry measuring peptides produced from proteins by proteolytic digestion, top-down mass spectrometry is a powerful technology that allows measuring proteins without proteolysis, thus characterizing intact forms of proteins, which provides information on primary sequences, including modifications characterization. In this review, we outline some progress in the separation, ionization, and fragmentation of intact proteins for top-down mass spectrometry and the growing power of intact protein-resolved measurements in biotechnology. |
| Author | Park, Hae-Min You, Jiwon |
| Author_xml | – sequence: 1 givenname: Jiwon surname: You fullname: You, Jiwon organization: Department of Chemical Engineering and Applied Chemistry, Chungnam National University – sequence: 2 givenname: Hae-Min surname: Park fullname: Park, Hae-Min email: haemin.park@cnu.ac.kr organization: Department of Chemical Engineering and Applied Chemistry, Chungnam National University |
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| CitedBy_id | crossref_primary_10_1021_acs_analchem_4c04677 crossref_primary_10_1038_s43586_024_00318_2 crossref_primary_10_1007_s12257_024_00104_7 |
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| SubjectTerms | Antibodies Biotechnology Chemistry Chemistry and Materials Science Glycosylation Industrial and Production Engineering Ionization Ions Mass spectrometry Mass spectroscopy Peptides Pharmaceutical industry Post-translation Proteins Proteolysis proteome Proteomes Review Paper Scientific imaging Structural analysis 생물공학 |
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