Interaction of thymic peptide thymosin alpha 1 with VIP receptors in rat intestinal epithelial cells: comparison with PHI and secretin.
Calvo. J R JR; Guerrero. J M JM; Goberna. R R
Key Findings
- Thymosinâalphaâ1 (10â»Âčâ°â10â»â·âŻM) modestly inhibits the binding of radiolabelled VIP.
- It is roughly 1,500âfold less potent than VIP at this inhibition.
- It produces only weak stimulation of cyclic AMP production in rat intestinal cells.
- Affinity ranking: VIP > PHI > secretin > thymosinâalphaâ1.
Practical Outcomes
- For biohackers, this means thymosinâalphaâ1 is unlikely to provide meaningful effects on gutârelated VIP pathways, such as metabolism or motility, at typical doses. It does not suggest any new dosing strategy or health benefit, so itâs not a useful addition to longevity or performance protocols.
Summary
The study shows that thymosinâalphaâ1 only barely interacts with the same gut receptors that the hormone VIP uses. It is far weakerâabout 1,500 times less potentâat blocking VIP binding and only slightly raises cellular signaling (cAMP). In short, thymosinâalphaâ1 isnât a strong activator of these VIP receptors.
Abstract
1. Thymic peptide thymosin alpha 1 (10(-10)-10(-7) M) is shown to inhibit the specific binding of 125I-labelled VIP. 2. Thymosin alpha 1 was 1500 times less potent than VIP at inhibiting 125I-labelled VIP binding. 3. Thymosin alpha 1 (10(-10)-10(-7) M) was weak in stimulating cyclic AMP production. 4. Interaction of thymosin alpha 1 with VIP receptors is compared with PHI and secretin. 5. The order of affinity of different peptides is VIP greater than PHI greater than secretin greater than thymosin alpha 1.
Study Information
pubmed
1989
10.1016/0306-3623(89)90203-6
10
15