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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2024.11
- 수록면
- 101 - 110 (10page)
이용수
초록· 키워드
Serum- and glucocorticoid-regulated kinase 1 (SGK1) is considered a potential therapeutic target for cancer as its overexpression leads to uncontrolled cell proliferation and tumor formation. This study focuses on the structural modifications of SGK1 inhibitors, particularly 1H-pyrrolo[2,3-b]pyridine analogs, in which the carboxyl group is expected to interact with the ε-amino group of lysine at the SGK1 catalytic site. We investigated alternative functional groups to replace the carboxyl group and found that, while most substitutions reduced the inhibitory activity, the hydroxycarbamoyl group enhanced it. Additionally, the positions of these substituents are crucial, with para-substituents generally showing higher activity than meta-substituents. Interestingly, typical hydrogen bond acceptors did not improve activity, suggesting that hydrogen bonding may not be the primary interaction between the carboxyl group and lysine. Docking studies have provided further insights into binding interactions, enhancing our understanding of the molecular determinants essential for SGK1 inhibition.
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목차
- ABSTRACT
- 1. Introduction
- 2. Experimental
- 3. Results and Discussion
- 4. Conclusion
- References
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