Design of ultrahigh-affinity and dual-specificity peptide antagonists of MDM2 and MDMX for P53 activation and tumor suppression.
10.1016/j.apsb.2021.06.010
- Author:
Xiang LI
1
;
Neelakshi GOHAIN
2
;
Si CHEN
3
;
Yinghua LI
4
;
Xiaoyuan ZHAO
4
;
Bo LI
5
;
William D TOLBERT
2
;
Wangxiao HE
6
;
Marzena PAZGIER
2
;
Honggang HU
4
;
Wuyuan LU
7
Author Information
1. School of Pharmacy, Second Military Medical University, Shanghai 200433, China.
2. Institute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
3. School of Medicine, Shanghai University, Shanghai 200444, China.
4. Institute of Translational Medicine, Shanghai University, Shanghai 200444, China.
5. State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China.
6. Department of Talent Highland, the First Affiliated Hospital of Xi'an Jiaotong University, Xi'an 710061, China.
7. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS) of School of Basic Medical Sciences and Shanghai Institute of Infectious Disease and Biosecurity of School of Public Health, Fudan University, Shanghai 200032, China.
- Publication Type:Journal Article
- Keywords:
Antitumor peptide;
FP, fluorescence polarization;
ITC, isothermal titration calorimetry;
MDM2;
MDM2, murine double minute 2;
MDMX;
MDMX, murine double minute X;
P53;
PMI, P53‒MDM2/MDMX inhibitor;
SAR, structure‒activity relationship;
SPR, surface plasmon resonance;
Systematic mutational analysis
- From:
Acta Pharmaceutica Sinica B
2021;11(9):2655-2669
- CountryChina
- Language:English
-
Abstract:
Peptide inhibition of the interactions of the tumor suppressor protein P53 with its negative regulators MDM2 and MDMX activates P53
