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- W1591369916 abstract "Specific protein–protein interactions (PPIs) constitute a key underlying mechanism for the presence of a multitude of intracellular signaling pathways, which are essential for the survival of normal and cancer cells. Specific molecular blockers for a crucial PPI would therefore be invaluable tools for an enhanced functional interrogation of the signaling pathway harboring this particular PPI. On the other hand, if a particular PPI is essential for the survival of cancer cells but is absent in or dispensable for the survival of normal cells, its specific molecular blockers could potentially be developed into effective anticancer therapeutics. Due to the flat and extended PPI interface, it would be conceivably difficult for small molecules to achieve an effective blockade, a problem which could be potentially circumvented with peptides or proteins. However, the well-documented proteolytic instability and cellular impermeability of peptides and proteins in general would make their developing into effective intracellular PPI blockers quite a challenge. With the advent of the peptide ‘stapling’ technology which was demonstrated to be able to stabilize the α-helical conformation of a peptide via bridging two neighboring amino-acid side chains with a ‘molecular staple’, a linear parent peptide could be transformed into a stronger PPI blocker with enhanced proteolytic stability and cellular permeability. This review will furnish an account on the peptide ‘stapling’ technology and its exploitation in efforts to achieve an enhanced functional interrogation or manipulation of intracellular signaling pathways especially those that are cancer relevant." @default.
- W1591369916 created "2016-06-24" @default.
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- W1591369916 creator A5039451118 @default.
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- W1591369916 date "2015-03-23" @default.
- W1591369916 modified "2023-09-26" @default.
- W1591369916 title "An enhanced functional interrogation/manipulation of intracellular signaling pathways with the peptide ‘stapling’ technology" @default.
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- W1591369916 doi "https://doi.org/10.1038/onc.2015.37" @default.
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