Peptidomimetics based on natural cinnamic acid scaffold: Synthesis, bio-evaluation and structure-activity relationships
文献类型： 外文期刊
作者： Guo, Lirong 1 ; Wang, Hexiang 1 ; Liu, Fang 1 ; Duan, Liping 3 ; Bao, Longzhu 1 ; Wu, Zhaoyuan 1 ; Ye, Ting 1 ; Zhang, Yani 1 ; Wang, Yueying 1 ; Cao, Xiufang 2 ; Fang, Wei 1 ; Ke, Shaoyong 1 ;
作者机构： 1.Hubei Acad Agr Sci, Natl Biopesticide Engn Res Ctr, Hubei Biopesticide Engn Res Ctr, Key Lab Microbial Pesticides,Minist Agr & Rural Af, Wuhan 430064, Peoples R China
2.Huazhong Agr Univ, Coll Chem, Wuhan 430070, Peoples R China
3.Chinese Ctr Dis Control & Prevent, Chinese Ctr Trop Dis Res, Natl Inst Parasit Dis, Shanghai 200025, Peoples R China
4.NHC Key Lab Parasite & Vector Biol, Shanghai 200025, Peoples R China
5.WHO Collaborating Ctr Trop Dis, Shanghai 200025, Peoples R China
6.Natl Ctr Int Res Trop Dis, Shanghai 200025, Peoples R China
关键词： Natural product; Peptidomimetics; Cinnamic acid; Conjugates; Biological activity; SARs
期刊名称：PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：4.0； 五年影响因子：4.5 ）
ISSN： 0048-3575
年卷期： 2025 年 213 卷
页码：
收录情况： SCI
摘要： A total of twenty-one peptidomimetics based on cinnamic acid scaffold were synthesized through structureactivity relationship driven (SAR-driven) optimization of natural molecule (CSDK450160). Systematic bioevaluation against twelve phytopathogenic fungi for these compounds revealed structure-dependent antifungal specificity, with cinnamic acid-peptide conjugates demonstrating pronounced inhibitory efficacy against Botrytis cinerea and Sclerotinia sclerotiorum. In planta antifungal assays showed that compound I-1 exhibited superior inhibitory potency against S. sclerotiorum. Scanning electron microscopy (SEM) analysis confirmed significant morphological disruption of S. sclerotiorum hyphae by I-1, including mycelial collapse and septation defects, effectively arresting mycelial proliferation. The mechanism of interaction between compound I-1 and potential target protein was described by integrating molecular docking technology and quantum chemistry theory. The theoretical results show that compound I-1 exhibits unique spatial structure specificity and achieves accurate recognition and highly selective binding with target proteins through it-it stacking.
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