Good news! Cancer is history (soon)!
"MYC is the shapeless protein responsible for making the majority of human cancer cases worse. ...
"Normally, MYC's activity is strictly controlled. In cancer cells, it becomes hyper active, and is not regulated properly," ...
"Normally, MYC's activity is strictly controlled. In cancer cells, it becomes hyper active, and is not regulated properly," ...
In the paper, the team describes a new peptide that binds directly to MYC with what is called sub-micro-molar affinity, which is getting closer to the strength of an antibody. In other words, it is a very strong and specific interaction. ..."
"... “We improved the binding performance of this peptide over previous versions by two orders of magnitude,” ... “This makes it closer to our drug development goals.” ..."
From the abstract:
"Here, we present the second generation of our bicyclic peptide library (NTB), featuring a stereodiversified structure and a simplified construction strategy. We utilized a tandem ring-opening metathesis and ring-closing metathesis reaction (ROM-RCM) to cyclize the linear peptide library in a single step, representing the first reported instance of this reaction being applied to the preparation of macrocyclic peptides. Moreover, the resulting bicyclic peptide can be easily linearized for MS/MS sequencing with a one-step deallylation process. We employed this library to screen against the E363-R378 epitope of MYC and identified several MYC-targeting bicyclic peptides. Subsequent in vitro cell studies demonstrated that one candidate, NT-B2R, effectively suppressed MYC transcription activities and cell proliferation."
The MYC proteins (grey ribbons) bind to DNA and promote cancer progression. UCR researchers developed a molecule (orange pretzel-like shape) that binds to MYC, inhibiting its cancer-promoting function
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