4 ms·
https://www.nature.com/articles/s41586-025-08683-y https://www.nature.com/articles/s41586-025-08683-y This seems to be the paper, but its behind a paywall. An
by anotherpaul 2y ago
https://www.nature.com/articles/s41586-025-08683-y https://www.nature.com/articles/s41586-025-08683-y
This seems to be the paper, but its behind a paywall.
Anyone with access can tell me if they publish the 12mer amino acid sequence? Is there more to it (post translational modifications)
Or is it just the peptide?
- archimedes237 2y agoNote, I have access but this is not my field. I just asked ChatGPT your question after have it read the paper. This is what the response was: Yes, the paper provides the 12-mer amino acid sequence of BRP: THRILRRLFNLC . Regarding post-translational modifications, the BRP peptide was synthesized with a C-terminal amidation, which was critical for its bioactivity. The non-amidated version of BRP was inactive in vitro . Additionally, the paper mentions that the C-terminal cysteine (C12) was synthesized as a free thiol . So, BRP is not just a simple peptide—it has a key post-translational modification (C-terminal amidation) that influences its function.
- anotherpaul 2y agoVery nice, thank you. This indeed answers my question.