Design, synthesis and biological evaluation of sulfonylamidines as potent c-Met inhibitors by enhancing hydrophobic interaction-Reference-Cited by-同舟云学术

Design, synthesis and biological evaluation of sulfonylamidines as potent c-Met inhibitors by enhancing hydrophobic interaction

Published:2023 Issue:36 Volume:21 Page:7459-7466
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Nan Xiang¹²,Li Xin³,Wu Yanchao³,Li Huijing³,Wang Qiuxu²^ORCID,Xing Shaojun¹,Liang Zhigang²

Affiliation:

1. Guangdong Key Laboratory for Biomedical Measurements and Ultrasound Imaging, National-Regional Key Technology Engineering Laboratory for Medical Ultrasound, School of Biomedical Engineering, Shenzhen University Medical School, Shenzhen 518060, China

2. Department of Stomatology, Shenzhen Second People's Hospital, Shenzhen 518035, China

3. Weihai Marine Organism & Medical Technology Research Institute, Harbin Institute of Technology, Weihai 264209, China

Abstract

Combining SARs with molecular modeling studies, compound 21j with superior activity to lead compound 7 and foretinib was ultimately discovered by enhancement of hydrophobic interaction with the allosteric hydrophobic back pocket of c-Met.

Funder

High-level Hospital Construction Project of Guangdong Provincial People's Hospital

National Key Research and Development Program of China

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/OB/D3OB01156A

Reference30 articles.

1. Probing and Manipulating Noncovalent Interactions in Functional Polymeric Systems

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3. Bridging computational modeling with amino acid replacements to investigate GHS-R1a-peptidomimetic recognition

4. Motifs for molecular recognition exploiting hydrophobic enclosure in protein–ligand binding

5. Adenosine Triphosphate Templated Self-Assembly of Cationic Porphyrin into Chiral Double Superhelices and Enzyme-Mediated Disassembly

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