UM  > Institute of Chinese Medical Sciences
Affiliated with RCfalse
Host-Guest Protein Assembly for Affinity Purification of Methyllysine Proteomes
Li,Linting1; Liu,Min1; Yue,Ludan2; Wang,Rui3; Zhang,Ning4; Liang,Yujie1; Zhang,Liang5; Cheng,Lixin4; Xia,Jiang1; Wang,Ruibing2
Source PublicationAnalytical Chemistry

Protein-protein interactions drive self-assembly of biomacromolecules and thus enable important physiological functions at a cellular level. Supramolecular chemists have developed artificial host-guest interactions that are similar with, yet distinct from and orthogonal to, the natural protein-protein interactions. For instance, cucurbit[n]urils are synthetic receptors that can specifically recognize proteins with N-terminal aromatic residues with high affinities, yet this interaction can be reversed by the competition of small molecules such as amantadine. Herein, we develop a site-specific, oriented protein-display method by combining the host-guest interaction based on cucurbit[7]uril and a covalent protein-peptide reaction. A methyllysine-binding protein HP1β chromodomain (CD) is immobilized via host-guest interactions and used as the "bait"to capture methyllysine proteomes from cancer cells. The captured "fish"- methyllysine-containing proteins - can be released via competitive displacement by amantadine in a nondenaturing and traceless manner. This affinity purification method found 73 novel methyllysine sites from 101 identified sites among 66 methylated proteins from 255 HP1β CD-binding proteins in cancer cells via subsequent mass spectrometric analysis. This work thereby presents a new strategy of artificial host-guest protein assembly in affinity purification of methyllysine proteins in coupling to mass spectrometry.

URLView the original
Indexed BySCIE
WOS Research AreaChemistry
WOS SubjectChemistry, Analytical 6.986
WOS IDWOS:000548541200090
Scopus ID2-s2.0-85089279726
Fulltext Access
Citation statistics
Cited Times [WOS]:10   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionInstitute of Chinese Medical Sciences
Corresponding AuthorCheng,Lixin; Xia,Jiang; Wang,Ruibing
Affiliation1.Department of Chemistry,Chinese University of Hong Kong,Shatin,Hong Kong
2.State Key Laboratory of Quality Research in Chinese Medicine,Institute of Chinese Medical Sciences,University of Macau,Taipa,999078,Macao
3.Pingshan Translational Medicine Center,Shenzhen Bay Laboratory,Shenzhen,518000,China
4.Department of Critical Care Medicine,Shenzhen People's Hospital,Second Clinical Medicine College of Jinan University,Shenzhen,518000,China
5.Department of Biomedical Sciences,City University of Hong Kong,Kowloon,Hong Kong
Corresponding Author AffilicationInstitute of Chinese Medical Sciences
Recommended Citation
GB/T 7714
Li,Linting,Liu,Min,Yue,Ludan,et al. Host-Guest Protein Assembly for Affinity Purification of Methyllysine Proteomes[J]. Analytical Chemistry,2020,92(13):9322-9329.
APA Li,Linting,Liu,Min,Yue,Ludan,Wang,Rui,Zhang,Ning,Liang,Yujie,Zhang,Liang,Cheng,Lixin,Xia,Jiang,&Wang,Ruibing.(2020).Host-Guest Protein Assembly for Affinity Purification of Methyllysine Proteomes.Analytical Chemistry,92(13),9322-9329.
MLA Li,Linting,et al."Host-Guest Protein Assembly for Affinity Purification of Methyllysine Proteomes".Analytical Chemistry 92.13(2020):9322-9329.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Li,Linting]'s Articles
[Liu,Min]'s Articles
[Yue,Ludan]'s Articles
Baidu academic
Similar articles in Baidu academic
[Li,Linting]'s Articles
[Liu,Min]'s Articles
[Yue,Ludan]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Li,Linting]'s Articles
[Liu,Min]'s Articles
[Yue,Ludan]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.