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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| Format: | Article |
| Language: | English |
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MDPI AG
2023-01-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/3/1083 |
| _version_ | 1797623786538795008 |
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| author | Ajcharapan Tantipanjaporn Man-Kin Wong |
| author_facet | Ajcharapan Tantipanjaporn Man-Kin Wong |
| author_sort | Ajcharapan Tantipanjaporn |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-11T09:33:42Z |
| format | Article |
| id | doaj.art-c35eeb6697a64cc5acf203023b090fdb |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T09:33:42Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-c35eeb6697a64cc5acf203023b090fdb2023-11-16T17:27:26ZengMDPI AGMolecules1420-30492023-01-01283108310.3390/molecules28031083Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and ProteinsAjcharapan Tantipanjaporn0Man-Kin Wong1State Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hum, Hong Kong, ChinaState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hum, Hong Kong, ChinaThe 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.https://www.mdpi.com/1420-3049/28/3/1083bioconjugationlysineN-terminal modificationpeptideproteinsite-selectivity |
| spellingShingle | Ajcharapan Tantipanjaporn Man-Kin Wong Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins Molecules bioconjugation lysine N-terminal modification peptide protein site-selectivity |
| title | Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins |
| title_full | Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins |
| title_fullStr | Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins |
| title_full_unstemmed | Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins |
| title_short | Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins |
| title_sort | development and recent advances in lysine and n terminal bioconjugation for peptides and proteins |
| topic | bioconjugation lysine N-terminal modification peptide protein site-selectivity |
| url | https://www.mdpi.com/1420-3049/28/3/1083 |
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