南方科技大学知识苑(SUSTech KC): Disruption of SND1-MTDH Interaction by a High Affinity Peptide Results in SND1 Degradation and Cytotoxicity to Breast Cancer Cells In Vitro and In Vivo

题名	Disruption of SND1-MTDH Interaction by a High Affinity Peptide Results in SND1 Degradation and Cytotoxicity to Breast Cancer Cells In Vitro and In Vivo
作者	Li, Peng 1,2; He, Yunjiao1,2,4 ; Chen, Teng 1,2; Choy, Kit-Ying 1,2; Chow, Tsun Sing 1,2; Wong, Iris L. K.1,2; Yang, Xinqing 1,2; Sun, Wenqin 1,2; Su, Xiaochun 1,2; Chan, Tak-Hang 1,2,3; Chow, Larry M. C.1,2
通讯作者	Chan, Tak-Hang; Chow, Larry M. C.
发表日期	2021
DOI	10.1158/1535-7163.MCT-20-0130
发表期刊	MOLECULAR CANCER THERAPEUTICS 影响因子和分区
ISSN	1535-7163
EISSN	1538-8514
卷号	20 期号:1
摘要	Staphylococcal nuclease domain-containing protein 1 (SND1) is a multifunctional oncoprotein overexpressed in breast cancer. Binding of metadherin (MTDH) to SND1 results in the stabilization of SND1 and is important in the initiation and progression of breast cancer. Disruption of such interaction is a potential therapeutic for breast cancer. SN1/2 domain of SND1 was used as bait in a phage display screening to identify a 12-amino acid peptide 4-2. The activity of peptide 4-2 was evaluated by ELISA, coimmunoprecipitation, MTS, Western blot analysis, and xenograft mouse model. Peptide 4-2 could disrupt SND1-MTDH interaction. Cell penetrating derivative of peptide 4-2 (CPP-4-2) could penetrate and kill breast cancer cells by disrupting SND1-MTDH interaction and degrading SND1. Tryptophan 10 (W10) of peptide 4-2 was essential in mediating cytotoxicity, SND1 interaction, SND1-MTDH disruption, and SND1 degradation. CPP-4-2 could inhibit the growth of breast cancer in a xenograft mouse model. The SND1-interacting peptide 4-2 could kill breast cancer cells both in vitro and in vivo by interacting with SND1, disrupting SND1-MTDH interaction, and inducing SND1 degradation. W10 was an essential amino acid in the activity of peptide 4-2.
相关链接	[来源记录]
收录类别	SCI
语种	英语
学校署名	其他
资助项目	Area of Strategic Importance grant from the Hong Kong Polytechnic University[1-ZE22] ; University Grants Committee of Hong Kong[C5012-15E]
WOS研究方向	Oncology
WOS类目	Oncology
WOS记录号	WOS:000607000100007
出版者	AMER ASSOC CANCER RESEARCH
ESI学科分类	CLINICAL MEDICINE
来源库	Web of Science
引用统计	被引频次[WOS]：10
成果类型	期刊论文
条目标识符	http://sustech.caswiz.com/handle/2SGJ60CL/221166
专题	南方科技大学医学院
作者单位	1.Hong Kong Polytech Univ, Dept Appl Biol & Chem Technol, Hung Hom, Hong Kong, Peoples R China 2.Hong Kong Polytech Univ, State Key Lab Chem Biol & Drug Discovery, Hung Hom, Hong Kong, Peoples R China 3.McGill Univ, Dept Chem, Montreal, PQ, Canada 4.Southern Univ Sci & Technol, Sch Med, Shenzhen, Guangdong, Peoples R China
推荐引用方式 GB/T 7714	Li, Peng,He, Yunjiao,Chen, Teng,et al. Disruption of SND1-MTDH Interaction by a High Affinity Peptide Results in SND1 Degradation and Cytotoxicity to Breast Cancer Cells In Vitro and In Vivo[J]. MOLECULAR CANCER THERAPEUTICS,2021,20(1).
APA	Li, Peng.,He, Yunjiao.,Chen, Teng.,Choy, Kit-Ying.,Chow, Tsun Sing.,...&Chow, Larry M. C..(2021).Disruption of SND1-MTDH Interaction by a High Affinity Peptide Results in SND1 Degradation and Cytotoxicity to Breast Cancer Cells In Vitro and In Vivo.MOLECULAR CANCER THERAPEUTICS,20(1).
MLA	Li, Peng,et al."Disruption of SND1-MTDH Interaction by a High Affinity Peptide Results in SND1 Degradation and Cytotoxicity to Breast Cancer Cells In Vitro and In Vivo".MOLECULAR CANCER THERAPEUTICS 20.1(2021).