Amylin fragment (8-37): lab research tool
A lab-only piece of amylin, a hormone the pancreas releases with insulin, used by scientists to study how amylin signals work in the body. Experimental, not an approved drug.
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.
A chemistry service or a researcher ordered the sequence, it was manufactured, and mass spectrometry confirmed the right molecule was produced.
A binding or activity measurement confirmed that it actually does what the computer predicted — or didn't.
What this is
Amylin (8-37) is a 30-amino-acid fragment of human amylin — the pancreatic hormone co-secreted with insulin by β-cells. The full hormone is 37 residues long; this peptide drops the first seven, removing the Cys2–Cys7 disulfide loop that the intact hormone uses to engage its receptor. It is a research-tool peptide used in laboratory studies of the amylin receptor system, not a therapeutic. The stored sequence ATQRLANFLVHSSNNFGAILSSTNVGSNTY is the N-terminally truncated backbone; the full-length amylin from which it derives normally carries a C-terminal amide and the disulfide ring at its N-terminus, neither of which is present in this 8-37 form.
What it does
Amylin's receptors are not stand-alone proteins. They are heterodimers built from the calcitonin receptor (CTR, gene CALCR) and one of three receptor activity-modifying proteins (RAMPs), giving three distinct amylin receptor subtypes — AMY1, AMY2, and AMY3 — alongside the related CGRP and adrenomedullin receptors of the same family (Hay 2018). Truncated amylin fragments that lack the N-terminal disulfide loop, including the 8-37 form, are studied as ligands at these CTR/RAMP complexes, where the missing N-terminus changes how the peptide engages the receptor relative to the intact hormone (Lee 2016).
Mechanism
The calcitonin receptor is a class B (secretin family) G-protein-coupled receptor. Peptide ligands of class B GPCRs use a two-domain binding model: the C-terminal portion of the peptide docks into the receptor's extracellular domain, and the N-terminal portion then activates the transmembrane core. Amylin (8-37) retains the C-terminal recognition region of amylin but loses the N-terminal segment required for full receptor activation, which is the structural basis for its use as a probe of amylin receptor pharmacology (Lee 2016). The extracellular domain of CTR is itself sensitive to post-translational modification — N-glycosylation at Asn130 of the human CTR extracellular domain significantly increases peptide hormone affinity (Lee 2017), and assembly with RAMPs allosterically reshapes the receptor's ligand preferences across the calcitonin/CGRP/amylin/adrenomedullin family (Advances in Pharmacology 2020; Hay 2018).
Evidence
- Human: No human clinical trials. This peptide is a research reagent, not a drug candidate with registered trials on ClinicalTrials.gov.
- Animal: The broader CTR/amylin receptor system has been characterized in mouse genetics: global and osteoclast-specific deletion of the calcitonin receptor causes increased bone formation, and calcitonin signaling through CTR negatively regulates osteoclast expression of
Spns2(Keller 2014). CTR-null mice also show susceptibility to hypercalcemia, establishing a physiological role for the receptor in calcium handling (Davey 2008). These studies use the receptor, not amylin (8-37) itself, as the experimental handle. - In vitro: Receptor-pharmacology work on the calcitonin/amylin receptor family — including binding and signaling studies of truncated peptide ligands at CTR alone and CTR/RAMP heterodimers — underpins what is known about how fragments like amylin (8-37) interact with this receptor system (Lee 2016; Lee 2017; Hay 2018).
Regulatory status
- US / EU: Not a marketed drug; no FDA or EMA approvals. Research-grade peptide only.
- WADA: Not individually listed. The full-length amylin agonist pramlintide is a marketed drug in a different class; amylin (8-37) is a distinct research fragment and is not the same molecule.
Related peptides
- Full-length amylin and the pharmacological amylin analog pramlintide — the agonist counterparts of this fragment at the AMY receptor family.
- Calcitonin — endogenous ligand of the calcitonin receptor (CTR), the shared GPCR backbone of the AMY receptors (Hay 2018).
- CGRP and adrenomedullin — sister peptides in the same calcitonin/CGRP family, signaling through CTR-like receptor (CLR) plus RAMP combinations (Hay 2018; Advances in Pharmacology 2020).
Open questions
- How the absence of the Cys2–Cys7 disulfide loop quantitatively reshapes binding kinetics at AMY1, AMY2, and AMY3 versus calcitonin receptor alone is not resolved in the sources collected for this card.
- Whether glycosylation state of CTR (Lee 2017) differentially affects affinity of truncated amylin fragments relative to the intact hormone is not directly addressed by the available references.
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.
Is the front part of the amylin fragment too floppy to trigger the receptor, even though the back part still docks correctly?
If confirmed, it would suggest that adding a simple molecular clamp to stiffen the loose end could convert this research tool into a functioning amylin mimic, potentially useful for treating type 2 diabetes or obesity.
Is the polar, asparagine-rich segment in the middle of this peptide a main part that locks onto the amylin receptors regardless of subtype?
If true, this central segment could define a minimal core for amylin-based compounds. Note: the segment is bounded by a phenylalanine on one side and a glycine on the other, not by two phenylalanines as sometimes stated.
▸full evidence table2 metrics
| metric | value | tool |
|---|---|---|
| ipTM | 0.8026445508003235 | boltz-2 |
| ranking score | 0.6297109127044678 | boltz-2 |
▸3-letter notation
▸recipeboltz-2 2.2.1
| parameter | value |
|---|---|
| model | boltz-2 2.2.1 |
| weights | — |
| hardware | vast_v100_32gb |
| mlx version | — |
| python | — |
| random seed | 1 |
| msa strategy | colabfold_local |
| runtime | — |
| predicted by | — |
| predicted at | 2026-05-22 |
▸citationbibtex
@peptide{pep10499,
sequence = {ATQRLANFLVHSSNNFGAILSSTNVGSNTY},
target = {calcr},
author = {peptidemodel},
year = {2026},
status = {synthesized}
}