Posters
First Report of the Peptide Inhibitors of Cancer Cell Migration From MIEN1 Protein Sequence
Presentation Type
Poster
Discipline Track
Clinical Science
Abstract Type
Research/Clinical
Abstract
Background: MIEN1 is a tumor-specific protein that regulates migration and invasion of cancers. It is overexpressed in human breast, prostate, colorectal, ovarian cancers, making this protein a potential therapeutic target for these cancers. Our goal is to identify small inhibitory peptides (iPeps) derived from the MIEN1 protein.
Methods: CASTp server was used to identify the pockets or empty concavities on the MIEN1 protein surface into which potential inhibitory molecules can gain access. The peptides were able to form hydrogen bonding with MIEN1 in chimera which is an indication of their MIEN1 binding. AntiCp server also indicated their anticancer activity. The peptides were synthesized and correct molecular mass was ascertained before doing biological methods. Screening methods included wound healing assay and transwell invasion assays.
Results: Two out of the five designed peptides showed anti-migratory and anti-invasive properties against the triple-negative and highly metastatic MDA-MB-231 breast cancer cell lines. It can also inhibit metastasis hallmarks (e.g., migration and invasion) in breast cancer cells.
Conclusions: We provide the first report of inhibitory molecules derived from the MIEN protein sequence. It can go a long way to inhibit cancer cell progression. Acknowledgments: The work was supported by local funds.
Recommended Citation
Tripathi, Amit Kumar; Desai, Priyanka Prakash; and Vishawanatha, Jamboor K., "First Report of the Peptide Inhibitors of Cancer Cell Migration From MIEN1 Protein Sequence" (2023). Research Symposium. 116.
https://scholarworks.utrgv.edu/somrs/theme1/posters/116
First Report of the Peptide Inhibitors of Cancer Cell Migration From MIEN1 Protein Sequence
Background: MIEN1 is a tumor-specific protein that regulates migration and invasion of cancers. It is overexpressed in human breast, prostate, colorectal, ovarian cancers, making this protein a potential therapeutic target for these cancers. Our goal is to identify small inhibitory peptides (iPeps) derived from the MIEN1 protein.
Methods: CASTp server was used to identify the pockets or empty concavities on the MIEN1 protein surface into which potential inhibitory molecules can gain access. The peptides were able to form hydrogen bonding with MIEN1 in chimera which is an indication of their MIEN1 binding. AntiCp server also indicated their anticancer activity. The peptides were synthesized and correct molecular mass was ascertained before doing biological methods. Screening methods included wound healing assay and transwell invasion assays.
Results: Two out of the five designed peptides showed anti-migratory and anti-invasive properties against the triple-negative and highly metastatic MDA-MB-231 breast cancer cell lines. It can also inhibit metastasis hallmarks (e.g., migration and invasion) in breast cancer cells.
Conclusions: We provide the first report of inhibitory molecules derived from the MIEN protein sequence. It can go a long way to inhibit cancer cell progression. Acknowledgments: The work was supported by local funds.