[Interaction of the synthetic immunomodulatory dipeptide bestim with murine macrophages and thymocytes].
Kolobov. A A AA; Kolodkin. N I NI; Zolotarev. Iu A IuA; Tathill. C C; Navolotskaia. E V EV
Key Findings
- Thymogen binds very tightly to mouse macrophages (Kd ~2 nM) and thymocytes (Kd ~3 nM)
- Unlabeled thymogen competes for the same binding sites (Ki ~1 nM)
- Binding is lost after trypsin treatment, indicating a protein receptor
- At concentrations from 10⁻¹⁰ to 10⁻⁶ M, thymogen reduces adenylate cyclase activity in these cells
Practical Outcomes
- The findings suggest a possible immunomodulatory action of thymogen, but without human studies or dosing info, there’s no actionable protocol for longevity or performance. More research is needed before recommending it for self‑experimentation.
Summary
This mouse study shows that the synthetic peptide thymogen (bestim) tightly binds to immune cells and can lower an enzyme called adenylate cyclase, but it only tested cells in a dish and gave no human data or dosing guidance, so it isn’t ready for practical use by biohackers.
Abstract
The tritium-labeled dipeptide bestim (gamma-D-Glu-L-Trp) with a specific activity of 45 Ci/mmol was obtained by high-temperature solid-state catalytic isotope exchange. It was found that [3H]bestim binds with a high affinity to murine peritoneal macrophages (Kd 2.1 +/- 0.1 nM) and thymocytes (Kd 3.1 +/- 0.2 nM), as well as with plasma membranes isolated from these cells (Kd 18.6 +/- 0.2 and 16.7 +/- 0.3 nM, respectively). The specific binding of [3H]bestim to macrophages and thymocytes was inhibited by the unlabeled dipeptide thymogen (L-Glu-L-Trp) (Ki 0.9 +/- 0.1 and 1.1 +/- 0.1 nM, respectively). After treatment with trypsin, macrophages and thymocytes lost the ability to bind [3H]bestim. Bestim in the concentration range of 10(-10) to 10(-6) M reduced the adenylate cyclase activity in the membranes of murine macrophages and thymocytes.
Study Information
pubmed
2008
10.1134/s1068162008010044