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Evaluation of a novel EphA2 targeting peptide for triple negative breast cancer based on radionuclide molecular imaging
- Source :
- Arabian Journal of Chemistry, Vol 15, Iss 11, Pp 104211- (2022)
- Publication Year :
- 2022
- Publisher :
- Elsevier, 2022.
-
Abstract
- A new strategy for the early diagnosis of triple-negative breast cancer (TNBC) is urgently needed however specific targets are lacking. EphA2 has been reported to be over-expressed in a variety of tumors, including TNBC, and is closely related to tumor progression. In this study, we designed a novel peptide, SD01, and tested its potential in the diagnosis of TNBC. FITC-SD01 and FITC-YSA were prepared and found to bind to the 4T1 TNBC cell line, the former showing greater affinity. 125I-SD01 and 125I-YSA were obtained with high radiochemical yield and radiochemical purity, and both showed a high binding affinity to 4T1 cells, with a higher Bmax in 125I-SD01. Whole-body phosphoautoradiography showed clearer imaging of tumors in the group of 125I-SD01 than in 125I-YSA. Biodistribution demonstrated higher tumor accumulation in the 125I-SD01 group. In group of 125I-SD01, the tumor to the opposite muscle tissue (T/NT) ratio was 5.998 ± 0.37, in contrast to 4.69 ± 0.18 in 125I-YSA group. Our results indicated that 125I-SD01 could selectively and specifically target 4T1 cells in vitro and in vivo, and showed higher binding affinity and better imaging compared to 125I-YSA. Therefore, SD01 was deemed to be a novel peptide with more favorable properties in terms of targeting EphA2.
- Subjects :
- Peptide
EphA2
TNBC
Radionuclide
Molecular imaging
Chemistry
QD1-999
Subjects
Details
- Language :
- English
- ISSN :
- 18785352
- Volume :
- 15
- Issue :
- 11
- Database :
- Directory of Open Access Journals
- Journal :
- Arabian Journal of Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.73d68370a41e465ebcef81b2c4dd0139
- Document Type :
- article
- Full Text :
- https://doi.org/10.1016/j.arabjc.2022.104211