New covalent bonding ability for proteins
To expand protein's covalent bonding ability, latent bioreactive unnatural amino acids have been designed and genetically encoded into proteins, which react with specific natural amino acid residues through proximity‐enabled bioreactivity. The resultant new covalent bonds can be selectively cre...
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| Published in | Protein science Vol. 31; no. 2; pp. 312 - 322 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Hoboken, USA
John Wiley & Sons, Inc
01.02.2022
Wiley Subscription Services, Inc |
| Subjects | |
| Online Access | Get full text |
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| Abstract | To expand protein's covalent bonding ability, latent bioreactive unnatural amino acids have been designed and genetically encoded into proteins, which react with specific natural amino acid residues through proximity‐enabled bioreactivity. The resultant new covalent bonds can be selectively created within and between proteins in vitro, in cells, and in vivo. Offering diverse properties previously unattainable, these covalent linkages have been harnessed to enhance protein properties, to modulate protein function, to probe ligand–receptor binding, to identify elusive protein interactions, and to develop covalent protein drugs. Selective introduction of covalent bonds into proteins is affording novel avenues for biological studies, synthetic biology, and biotherapeutics. |
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| AbstractList | To expand protein's covalent bonding ability, latent bioreactive unnatural amino acids have been designed and genetically encoded into proteins, which react with specific natural amino acid residues through proximity‐enabled bioreactivity. The resultant new covalent bonds can be selectively created within and between proteins in vitro, in cells, and in vivo. Offering diverse properties previously unattainable, these covalent linkages have been harnessed to enhance protein properties, to modulate protein function, to probe ligand–receptor binding, to identify elusive protein interactions, and to develop covalent protein drugs. Selective introduction of covalent bonds into proteins is affording novel avenues for biological studies, synthetic biology, and biotherapeutics. To expand protein's covalent bonding ability, latent bioreactive unnatural amino acids have been designed and genetically encoded into proteins, which react with specific natural amino acid residues through proximity-enabled bioreactivity. The resultant new covalent bonds can be selectively created within and between proteins in vitro, in cells, and in vivo. Offering diverse properties previously unattainable, these covalent linkages have been harnessed to enhance protein properties, to modulate protein function, to probe ligand-receptor binding, to identify elusive protein interactions, and to develop covalent protein drugs. Selective introduction of covalent bonds into proteins is affording novel avenues for biological studies, synthetic biology, and biotherapeutics.To expand protein's covalent bonding ability, latent bioreactive unnatural amino acids have been designed and genetically encoded into proteins, which react with specific natural amino acid residues through proximity-enabled bioreactivity. The resultant new covalent bonds can be selectively created within and between proteins in vitro, in cells, and in vivo. Offering diverse properties previously unattainable, these covalent linkages have been harnessed to enhance protein properties, to modulate protein function, to probe ligand-receptor binding, to identify elusive protein interactions, and to develop covalent protein drugs. Selective introduction of covalent bonds into proteins is affording novel avenues for biological studies, synthetic biology, and biotherapeutics. |
| Author | Wang, Lei Cao, Li |
| AuthorAffiliation | 1 Department of Pharmaceutical Chemistry and the Cardiovascular Research Institute University of California San Francisco San Francisco California USA |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34761448$$D View this record in MEDLINE/PubMed |
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| Keywords | latent bioreactive unnatural amino acid genetic code expansion protein-protein interaction protein therapeutics proximity-enabled bioreactivity covalent drug |
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| SubjectTerms | Amino acids Amino Acids - chemistry Bonding Chemical bonds Covalence Covalent bonds covalent drug Genetic code genetic code expansion latent bioreactive unnatural amino acid Ligands Protein Binding Protein Engineering Protein interaction protein therapeutics Proteins Proteins - chemistry protein–protein interaction proximity‐enabled bioreactivity Review |
| Title | New covalent bonding ability for proteins |
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