CRSP1 opioid receptor signaling peptide
A brain-made chemical messenger designed to act on opioid receptors, the same body system that controls pain and mood; experimental, not an approved medicine.
A researcher, an agent, or an algorithm wrote down the sequence and picked a target to hit.
An AI model like OpenFold3 or AlphaFold built a 3D structure and scored how well it fits the binding site.
A second contributor repeated the computation on their own hardware and the scores matched.
Literature-extracted sequence peptide — synthesized for bioassay as documented in linked reference(s)
Fork this card to add platform evidence →
Activity measured in linked reference(s) — IC50/MIC/cytotoxicity data
Fork this card to add platform evidence →
Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.
What if a peptide long catalogued as an opioid-like compound actually works through a completely different system in the body?
If the receptor identity is corrected, researchers studying bone density, energy regulation, or heart function could gain a new lead compound, while pain researchers would stop chasing a dead end. Getting the target right is the first step before any drug work can begin.
Could a natural peptide quiet pain signals the way calcitonin does, without any risk of opioid dependence?
If this hypothesis holds, CRSP1 might point toward a class of pain drugs that do not carry addiction risk, which would matter enormously for patients needing long-term relief. Drugs targeting the related CGRP pathway already work for migraines; a central-acting cousin could open similar doors for other pain conditions.
Could replacing one vulnerable spot in the peptide's chain prevent it from breaking down before it ever reaches a patient?
Peptide drugs often degrade during storage or inside the body before they can do their job. If this substitution works, it could make CRSP1 viable as an actual medicine and would also make it easier to study in the lab, removing a practical barrier that often kills otherwise promising compounds.
Does a specific shape in the peptide, formed by two linked building blocks at its tip, determine whether it can activate its target receptor?
If this loop is confirmed as the active part of the molecule, drug designers could build smaller, more precise compounds based on it rather than using the whole peptide. That kind of insight tends to speed up development and can improve how selectively a drug acts, reducing unwanted side effects.
▸full evidence table2 metrics
| metric | value | tool |
|---|---|---|
| ipTM | 0.4931243062019348 | boltz-2 |
| ranking score | 0.6980369687080383 | boltz-2 |
▸structural qualityopenfold3
| metric | value | note |
|---|---|---|
| gpde | 1.143 | global PDE — lower = better |
| disorder | NaN | fraction disordered |
▸3-letter notation
▸recipeboltz-2 1.0
| parameter | value |
|---|---|
| model | boltz-2 1.0 |
| weights | — |
| hardware | nvidia_nim_api |
| mlx version | — |
| python | — |
| random seed | — |
| msa strategy | none |
| diffusion samples | 1 |
| runtime | — |
| predicted by | mlx@peptide |
| predicted at | 2026-04-24 |
▸citationbibtex
@peptide{pep05449,
sequence = {ACNTATCMTHRLAGWLSRSGSMVRSNLLPTKMGFKIFNGPRRNSWF},
target = {oprm1},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}