A Constrained Helical Peptide Against S100A4 Inhibits Cell Motility in Tumor Cells
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
A Constrained Helical Peptide Against S100A4 Inhibits
Cell Motility in Tumor Cells
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| Creator |
Naiya, Gitashri
Kaypee, Stephanie Kundu, Tapas K Roy, Siddhartha |
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| Subject |
Structural Biology & Bioinformatics
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| Description |
S100A4, a member of a calcium-regulated protein family,
is involved in various cellular signaling pathways.
From many studies over the last decade or so, it has
become clear that it is involved in tumor metastasis,
probably playing a determinative role. However, except
the phenothiazine group of drugs, no significant inhibitor
of S100A4 has been reported. Even the phenothiazines
are very weak inhibitors of S100A4 action. In this
study, we report design and development of a conformationally constrained helical peptide modeled on the
non-muscle myosin peptide that binds to S100A4. This
conformationally constrained peptide binds to S100A4
with a dissociation constant in the nanomolar range. We
also synthesized a peptide for experimental control that
bears several alanine mutations in the peptide–protein
interface. We demonstrate that the former peptide specifically inhibits motility of H1299 and MCF-7 cells in a
wound-healing assay. Structures of several S100A4–
ligand complexes suggest that it may be possible to
develop a smaller peptide–small molecule conjugate
having high affinity for S100A4. Peptide–drug conjugates
of this kind may play an important role in developing
drug leads against this antimetastasis target
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| Date |
2015
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/2344/1/CHEMICAL_BIOLOGY_%26_DRUG_DESIGN__V__86___(_4_)_945%2D950;2015.pdf
Naiya, Gitashri and Kaypee, Stephanie and Kundu, Tapas K and Roy, Siddhartha (2015) A Constrained Helical Peptide Against S100A4 Inhibits Cell Motility in Tumor Cells. Chemical Biology & Drug Design , 86 (4). pp. 945-950. |
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| Relation |
http://www.eprints.iicb.res.in/2344/
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