Conjugated detergent micelles as a platform for IgM purification
Immunoglobulin M (IgM) antibodies hold promise as anticancer drugs and as agents for promoting immune homeostasis. This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of protein A chromatography for IgM purification. Here...
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| Veröffentlicht in: | Biotechnology and bioengineering 2022-07, Vol.119 (7), p.1997-2003 |
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| container_issue | 7 |
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| container_title | Biotechnology and bioengineering |
| container_volume | 119 |
| creator | Dhandapani, Gunasekaran Wachtel, Ellen Das, Ishita Sheves, Mordechai Patchornik, Guy |
| description | Immunoglobulin M (IgM) antibodies hold promise as anticancer drugs and as agents for promoting immune homeostasis. This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of protein A chromatography for IgM purification. Here, we describe a nonchromatographic platform for quantitatively capturing IgMs at neutral pH, which is then recovered with 86%–94% yield and >95% purity at pH 3. The platform contains micelles conjugated with the [(bathophenanthroline)3:Fe2+] amphiphilic complex. Inclusion of amino acid monomers, for example, phenylalanine or tyrosine, during conjugation of detergent micelles, allows subsequent extraction of IgMs at close to neutral pH. With the successful implementation of this purification platform for both polyclonal humans and bovine IgMs, we anticipate similar results for monoclonal IgMs, most relevant for the pharmaceutical industry.
Immunoglobulin M (IgM) antibodies are rarely used in medicine due to difficulties associated with their expression and purification. A potentially (a) general, (b) nonchromatographic, (c) ligand‐free, and (d) simple‐to‐implement platform capable of quantitatively capturing IgMs (pH 7) and recovering these in pure form (>95%) at pH 3 (>95% yield) is presented. Unlike other purification methodologies, specially designed micelles conjugated via amphiphilic [metal:chelator] complexes are used. |
| doi_str_mv | 10.1002/bit.28089 |
| format | Article |
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Immunoglobulin M (IgM) antibodies are rarely used in medicine due to difficulties associated with their expression and purification. A potentially (a) general, (b) nonchromatographic, (c) ligand‐free, and (d) simple‐to‐implement platform capable of quantitatively capturing IgMs (pH 7) and recovering these in pure form (>95%) at pH 3 (>95% yield) is presented. Unlike other purification methodologies, specially designed micelles conjugated via amphiphilic [metal:chelator] complexes are used.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.28089</identifier><identifier>PMID: 35324016</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>[metal:chelator] complexes ; Amino acids ; Animals ; Antibodies ; Antibodies, Monoclonal - metabolism ; Anticancer properties ; Antineoplastic drugs ; Antitumor agents ; Cattle ; Communication ; conjugated micelles ; Conjugation ; Detergents ; Homeostasis ; Humans ; hydrophobic amino acids ; IgM purification ; Immunoglobulin M ; Immunoglobulin M - metabolism ; Immunosuppressive agents ; Iron ; ligand free ; Mammalian cells ; Mammals - metabolism ; Micelles ; Monomers ; nonchromatographic ; pH effects ; Pharmaceutical industry ; Phenylalanine ; Protein A ; Protein purification ; Purification ; Staphylococcal Protein A ; Tyrosine</subject><ispartof>Biotechnology and bioengineering, 2022-07, Vol.119 (7), p.1997-2003</ispartof><rights>2022 The Authors. published by Wiley Periodicals LLC.</rights><rights>2022 The Authors. Biotechnology and Bioengineering published by Wiley Periodicals LLC.</rights><rights>2022. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3739-a7f2f53f62618d7d4e042946d8a0e6e5e0e075e55f1037be7afa4fcfc4bf07573</citedby><cites>FETCH-LOGICAL-c3739-a7f2f53f62618d7d4e042946d8a0e6e5e0e075e55f1037be7afa4fcfc4bf07573</cites><orcidid>0000-0002-6472-8354 ; 0000-0002-1402-3620</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbit.28089$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.28089$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35324016$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dhandapani, Gunasekaran</creatorcontrib><creatorcontrib>Wachtel, Ellen</creatorcontrib><creatorcontrib>Das, Ishita</creatorcontrib><creatorcontrib>Sheves, Mordechai</creatorcontrib><creatorcontrib>Patchornik, Guy</creatorcontrib><title>Conjugated detergent micelles as a platform for IgM purification</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol Bioeng</addtitle><description>Immunoglobulin M (IgM) antibodies hold promise as anticancer drugs and as agents for promoting immune homeostasis. This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of protein A chromatography for IgM purification. Here, we describe a nonchromatographic platform for quantitatively capturing IgMs at neutral pH, which is then recovered with 86%–94% yield and >95% purity at pH 3. The platform contains micelles conjugated with the [(bathophenanthroline)3:Fe2+] amphiphilic complex. Inclusion of amino acid monomers, for example, phenylalanine or tyrosine, during conjugation of detergent micelles, allows subsequent extraction of IgMs at close to neutral pH. With the successful implementation of this purification platform for both polyclonal humans and bovine IgMs, we anticipate similar results for monoclonal IgMs, most relevant for the pharmaceutical industry.
Immunoglobulin M (IgM) antibodies are rarely used in medicine due to difficulties associated with their expression and purification. A potentially (a) general, (b) nonchromatographic, (c) ligand‐free, and (d) simple‐to‐implement platform capable of quantitatively capturing IgMs (pH 7) and recovering these in pure form (>95%) at pH 3 (>95% yield) is presented. 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This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of protein A chromatography for IgM purification. Here, we describe a nonchromatographic platform for quantitatively capturing IgMs at neutral pH, which is then recovered with 86%–94% yield and >95% purity at pH 3. The platform contains micelles conjugated with the [(bathophenanthroline)3:Fe2+] amphiphilic complex. Inclusion of amino acid monomers, for example, phenylalanine or tyrosine, during conjugation of detergent micelles, allows subsequent extraction of IgMs at close to neutral pH. With the successful implementation of this purification platform for both polyclonal humans and bovine IgMs, we anticipate similar results for monoclonal IgMs, most relevant for the pharmaceutical industry.
Immunoglobulin M (IgM) antibodies are rarely used in medicine due to difficulties associated with their expression and purification. A potentially (a) general, (b) nonchromatographic, (c) ligand‐free, and (d) simple‐to‐implement platform capable of quantitatively capturing IgMs (pH 7) and recovering these in pure form (>95%) at pH 3 (>95% yield) is presented. Unlike other purification methodologies, specially designed micelles conjugated via amphiphilic [metal:chelator] complexes are used.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>35324016</pmid><doi>10.1002/bit.28089</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-6472-8354</orcidid><orcidid>https://orcid.org/0000-0002-1402-3620</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | [metal:chelator] complexes Amino acids Animals Antibodies Antibodies, Monoclonal - metabolism Anticancer properties Antineoplastic drugs Antitumor agents Cattle Communication conjugated micelles Conjugation Detergents Homeostasis Humans hydrophobic amino acids IgM purification Immunoglobulin M Immunoglobulin M - metabolism Immunosuppressive agents Iron ligand free Mammalian cells Mammals - metabolism Micelles Monomers nonchromatographic pH effects Pharmaceutical industry Phenylalanine Protein A Protein purification Purification Staphylococcal Protein A Tyrosine |
| title | Conjugated detergent micelles as a platform for IgM purification |
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