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Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins
The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functiona...
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| Published in: | Molecules (Basel, Switzerland) Switzerland), 2023-01, Vol.28 (3), p.1083 |
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| Main Authors: | , |
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| cited_by | cdi_FETCH-LOGICAL-c560t-409901cb3a96abee0e2d6523b3293404f1dad164e7e54f11becc02565a77d0053 |
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| cites | cdi_FETCH-LOGICAL-c560t-409901cb3a96abee0e2d6523b3293404f1dad164e7e54f11becc02565a77d0053 |
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| container_issue | 3 |
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| container_title | Molecules (Basel, Switzerland) |
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| creator | Tantipanjaporn, Ajcharapan Wong, Man-Kin |
| description | The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods. |
| doi_str_mv | 10.3390/molecules28031083 |
| format | article |
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Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods.</description><identifier>ISSN: 1420-3049</identifier><identifier>EISSN: 1420-3049</identifier><identifier>DOI: 10.3390/molecules28031083</identifier><identifier>PMID: 36770752</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino Acids ; Amino groups ; Antibody-drug conjugates ; Biocompatibility ; bioconjugation ; Biological products ; Biomaterials ; Biomedical materials ; Carbohydrates ; Chemical bonds ; Chemical modification ; Chemistry ; Composition ; Health aspects ; Lysine ; Lysine - chemistry ; Materials science ; Medical research ; Methods ; N-terminal modification ; N-Terminus ; peptide ; Peptides ; Peptides - chemistry ; Post-translation ; Post-translational modification ; protein ; Protein folding ; Protein Processing, Post-Translational ; Proteins ; Proteins - chemistry ; Reaction time ; Reagents ; Residues ; Review ; Selectivity ; site-selectivity</subject><ispartof>Molecules (Basel, Switzerland), 2023-01, Vol.28 (3), p.1083</ispartof><rights>COPYRIGHT 2023 MDPI AG</rights><rights>2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). 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Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods.</description><subject>Amino Acids</subject><subject>Amino groups</subject><subject>Antibody-drug conjugates</subject><subject>Biocompatibility</subject><subject>bioconjugation</subject><subject>Biological products</subject><subject>Biomaterials</subject><subject>Biomedical materials</subject><subject>Carbohydrates</subject><subject>Chemical bonds</subject><subject>Chemical modification</subject><subject>Chemistry</subject><subject>Composition</subject><subject>Health aspects</subject><subject>Lysine</subject><subject>Lysine - chemistry</subject><subject>Materials science</subject><subject>Medical research</subject><subject>Methods</subject><subject>N-terminal modification</subject><subject>N-Terminus</subject><subject>peptide</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Post-translation</subject><subject>Post-translational modification</subject><subject>protein</subject><subject>Protein folding</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Reaction time</subject><subject>Reagents</subject><subject>Residues</subject><subject>Review</subject><subject>Selectivity</subject><subject>site-selectivity</subject><issn>1420-3049</issn><issn>1420-3049</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>COVID</sourceid><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptUk1v1DAQjRCIlsIP4IIiceGSMrZje3NB2pavSiuoUDlbjj1ZvErsxU5W6r_H2S2lC8gHj2fee6N5nqJ4SeCcsQbeDqFHM_WY6AIYgQV7VJySmkLFoG4eP4hPimcpbQAoqQl_WpwwISVITk8L_R532IftgH4stbflNzRzuLQ77Q2m0vlydZucx331S3WDcXBe9-WFCyb4zbTWowu-7EIsr3E7OptJM_Q6hhGdT8-LJ53uE764u8-K7x8_3Fx-rlZfP11dLleV4QLGqoamAWJaphuhW0RAagWnrGW0YTXUHbHaElGjRJ4fpEVjgHLBtZQWgLOz4uqga4PeqG10g463Kmin9okQ10rH0ZkelWEcsRWikVrUxnBtOgoMcjNooLNt1np30NpO7YB2diTq_kj0uOLdD7UOO9U0nDHJssCbO4EYfk6YRjW4ZLDvtccwJUWl5IIsOMzQ139BN2GK2eE9qm5qshD8D2qt8wDOdyH3NbOoWsqaUUIJmVHn_0HlY3Fw-bewczl_RCAHgokhpYjd_YwE1Lxj6p8dy5xXD825Z_xeKvYLHUvN9w</recordid><startdate>20230121</startdate><enddate>20230121</enddate><creator>Tantipanjaporn, Ajcharapan</creator><creator>Wong, Man-Kin</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>COVID</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-1574-6860</orcidid></search><sort><creationdate>20230121</creationdate><title>Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins</title><author>Tantipanjaporn, Ajcharapan ; Wong, Man-Kin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c560t-409901cb3a96abee0e2d6523b3293404f1dad164e7e54f11becc02565a77d0053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Amino Acids</topic><topic>Amino groups</topic><topic>Antibody-drug conjugates</topic><topic>Biocompatibility</topic><topic>bioconjugation</topic><topic>Biological products</topic><topic>Biomaterials</topic><topic>Biomedical materials</topic><topic>Carbohydrates</topic><topic>Chemical bonds</topic><topic>Chemical modification</topic><topic>Chemistry</topic><topic>Composition</topic><topic>Health aspects</topic><topic>Lysine</topic><topic>Lysine - chemistry</topic><topic>Materials science</topic><topic>Medical research</topic><topic>Methods</topic><topic>N-terminal modification</topic><topic>N-Terminus</topic><topic>peptide</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Post-translation</topic><topic>Post-translational modification</topic><topic>protein</topic><topic>Protein folding</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Reaction time</topic><topic>Reagents</topic><topic>Residues</topic><topic>Review</topic><topic>Selectivity</topic><topic>site-selectivity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tantipanjaporn, Ajcharapan</creatorcontrib><creatorcontrib>Wong, Man-Kin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Coronavirus Research Database</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals (Open Access)</collection><jtitle>Molecules (Basel, Switzerland)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tantipanjaporn, Ajcharapan</au><au>Wong, Man-Kin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins</atitle><jtitle>Molecules (Basel, Switzerland)</jtitle><addtitle>Molecules</addtitle><date>2023-01-21</date><risdate>2023</risdate><volume>28</volume><issue>3</issue><spage>1083</spage><pages>1083-</pages><issn>1420-3049</issn><eissn>1420-3049</eissn><abstract>The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>36770752</pmid><doi>10.3390/molecules28031083</doi><orcidid>https://orcid.org/0000-0003-1574-6860</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecules (Basel, Switzerland), 2023-01, Vol.28 (3), p.1083 |
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| subjects | Amino Acids Amino groups Antibody-drug conjugates Biocompatibility bioconjugation Biological products Biomaterials Biomedical materials Carbohydrates Chemical bonds Chemical modification Chemistry Composition Health aspects Lysine Lysine - chemistry Materials science Medical research Methods N-terminal modification N-Terminus peptide Peptides Peptides - chemistry Post-translation Post-translational modification protein Protein folding Protein Processing, Post-Translational Proteins Proteins - chemistry Reaction time Reagents Residues Review Selectivity site-selectivity |
| title | Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins |
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