Supramolecular strategies for protein immobilization and modification

被引:16
作者
Finbloom, Joel A. [1 ]
Francis, Matthew B. [1 ,2 ]
机构
[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA
[2] Lawrence Berkeley Natl Labs, Mat Sci Div, Berkeley, CA 94720 USA
基金
美国国家科学基金会;
关键词
HOST-GUEST INTERACTIONS; BIOTIN-AVIDIN PAIR; MOLECULAR RECOGNITION; CLICK CHEMISTRY; DRUG-DELIVERY; SITE; CONJUGATION; PEGYLATION; PURIFICATION; BIOCONJUGATION;
D O I
10.1016/j.cbpa.2018.05.023
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
Protein immobilization and modification are widely used techniques in the fields of chemical biology and biomaterials science. While covalent strategies based on small molecules are traditionally used, supramolecular chemistry offers numerous useful opportunities for guiding the modification locations on complex protein landscapes and introducing different degrees of reversibility into the products. In this opinion, we highlight recent advances in using supramolecular interactions, particularly host-guest chemistry, for controlling protein modification and immobilization. We discuss supramolecular strategies for protein-conjugate purification and capture, as well as for protein modification via host-guest interactions and metal coordination. Lastly, we address recent advances in utilizing supramolecular interactions to direct covalent protein modification. These examples of supramolecular chemical biology present opportunities to advance a wide range of applications, including proteomics and drug delivery.
引用
收藏
页码:91 / 98
页数:8
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