An easily accessible, lower rim substituted calix[4]arene selectively binds N,N-dimethyllysine

被引：2

作者：

Shaurya, Alok ^{[1
,2
]}

Garnett, Graham A. E. ^{[1
,2
]}

Starke, Melissa J. ^{[1
,2
]}

Grasdal, Mark C. ^{[1
,2
]}

Dewar, Charlotte C. ^{[1
,2
]}

Kliuchynskyi, Anton Y. ^{[1
,2
]}

Hof, Fraser ^{[1
,2
]}

机构：

[1] Univ Victoria, Dept Chem, 3800 Finnerty Rd, Victoria, BC V8P 5C2, Canada

[2] Univ Victoria, Ctr Adv Mat & Related Technol CAMTEC, 3800 Finnerty Rd, Victoria, BC V8P 5C2, Canada

来源：

ORGANIC & BIOMOLECULAR CHEMISTRY | 2021年 / 19卷 / 21期

关键词：

HISTONE LYSINE METHYLATION; MOLECULAR RECOGNITION; SYNTHETIC RECEPTOR; AMINO-ACIDS; TRIMETHYLLYSINE; CALIXARENES; COMPLEXATION; INHIBITION; CHROMATIN; INSIGHTS;

D O I：

10.1039/d1ob00524c

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Post-translational modifications (PTMs) are critical controllers of protein functions. One set of important PTMs are N-methylated side chains of lysine and arginine, which exist in several functionally distinct forms. Multiple groups have demonstrated the selective binding of the most hydrophobic family member, trimethyllysine (Kme3), using various macrocyclic hosts, but the selective binding of lower methylation states remains challenging. Herein we report that the installation of a sulfonate ester on the lower rim phenol of p-sulfonatocalix[4]arene efficiently generates a potent, N,N-dimethyllysine (Kme2)-selective host in one step from commercially available starting materials. We characterize its binding behaviors in solution, and examine the relationship between its unusual conformational dynamics and its guest-binding properties.

引用

页码：4691 / 4696

页数：6

共 37 条

[1] Molecular Insights into Inhibition of the Methylated Histone-Plant Homeodomain Complexes by Calixarenes [J].