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Exploiting Protein N-Terminus for Site-Specific Bioconjugation
被引:23
作者:
De Rosa, Lucia
[1
]
Di Stasi, Rossella
[1
]
Romanelli, Alessandra
[2
]
D'Andrea, Luca Domenico
[3
]
机构:
[1] CNR, Ist Biostrutture & Bioimmagini, Via Mezzocannone 16, I-80134 Naples, Italy
[2] Univ Milan, Dipartimento Sci Farmaceut, Via Venezian 21, I-20133 Milan, Italy
[3] CNR, Ist Sci & Tecnol Chim Giulio Natta, Via M Bianco 9, I-20131 Milan, Italy
来源:
MOLECULES
|
2021年
/
26卷
/
12期
关键词:
protein labeling;
chemo-selective reaction;
molecular probe;
chemical ligation;
click-chemistry;
aldehyde protein;
azide protein;
BIOCOMPATIBLE CONDENSATION REACTION;
SUBSTRATE-SPECIFICITY;
MYRISTOYL TRANSFERASE;
CHEMICAL-MODIFICATION;
ESCHERICHIA-COLI;
NATIVE PROTEINS;
PEPTIDE-BONDS;
ACID ANALOGS;
BUTELASE;
LIGATION;
D O I:
10.3390/molecules26123521
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Although a plethora of chemistries have been developed to selectively decorate protein molecules, novel strategies continue to be reported with the final aim of improving selectivity and mildness of the reaction conditions, preserve protein integrity, and fulfill all the increasing requirements of the modern applications of protein conjugates. The targeting of the protein N-terminal alpha-amine group appears a convenient solution to the issue, emerging as a useful and unique reactive site universally present in each protein molecule. Herein, we provide an updated overview of the methodologies developed until today to afford the selective modification of proteins through the targeting of the N-terminal alpha-amine. Chemical and enzymatic strategies enabling the selective labeling of the protein N-terminal alpha-amine group are described.
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页数:20
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