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Thymosin-beta-4-fragment

Ac-SDKP, Goralatide, Seraspenide

A tetrapeptide fragment of thymosin beta-4 that inhibits inflammation, reduces fibrosis, and regulates hematopoietic stem cell proliferation.

Quick Stats
Studies 83
Trials 3
Formula C20H33N5O9
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Utility 2
pubmed 2019

Neurodegenerative Disease-Related Proteins within the Epidermal Layer of the Human Skin.

Akerman. S Can SC; Hossain. Shireen S; Shobo. Adeola A; Zhong. Yifei Y; Jourdain. Roland R; Hancock....

Scientists found that proteins linked to Alzheimer’s and Parkinson’s, like alpha‑synuclein, tau and a fragment of beta‑amyloid, are present in the outer skin layer, and they also saw the inflammation‑related peptide thymosin‑beta‑4 there. The amount didn’t change much between young and old people, and seeing alpha‑synuclein inside skin cell nuclei is new. This shows skin could someday be used to check for brain disease markers, but it doesn’t change any current health hacks.

Utility 2
pubmed Mar 5, 1991

Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable.

Safer. D D; Elzinga. M M; Nachmias. V T VT

The study shows that a small protein called Fx, found in platelets, is actually the same thing as thymosin beta‑4, a peptide that binds to single actin units and stops them from forming filaments. This means thymosin beta‑4 is a natural regulator of the cell’s internal skeleton in many tissues.

Utility 2
pubmed 2002

Cloning expression in E.coli and biological activity of human thymosin beta(4).

Che. Yan-Ke YK; Yang. Hui H; Lu. Fan F; Pu. Qin Q; Li. Ren-De RD; Zhao. Zhong-Liang ZL

Scientists built a DNA copy of human thymosin‑beta‑4, put it into E.coli bacteria, and got the bacteria to make a lot of the peptide. They purified it to about 95% purity and showed it can make immune cells grow and change in lab tests.

Utility 2
pubmed Jun 13, 2007

Subcellular distribution of thymosin beta4.

Zoubek. Robert E RE; Hannappel. Ewald E

The study shows that thymosin beta‑4 and its pieces can move into the cell nucleus by simple diffusion, not needing special transport proteins, and this happens the same way whether the peptide is normal or has certain parts changed.

Utility 2
pubmed Aug 8, 2013

High-resolution HPLC-ESI-MS characterization of the contact sites of the actin-thymosin β(4) complex by chemical and enzymatic cross-linking.

Knop. Jana J; App. Christine C; Horn. Anselm H C AH; Iavarone. Federica F; Castagnola. Massimo M; Ha...

Scientists mapped exactly where a tiny piece of the protein thymosin‑beta‑4 (a fragment often talked about in biohacking circles) sticks to the cell's structural protein actin. They used chemical tricks to lock the two together and then identified the contact points with high‑resolution mass spectrometry. The results show that the fragment binds in several flexible spots rather than one rigid spot.

Utility 2
pubmed Oct 30, 2003

Thymosin beta 4 induces the synthesis of plasminogen activator inhibitor 1 in cultured endothelial cells and increases its extracellular expression.

Al-Nedawi. Khalid N I KN; Czyz. Malgorzata M; Bednarek. Radoslaw R; Szemraj. Janusz J; Swiatkowska....

The study found that the peptide thymosin beta‑4 (Tβ4) makes endothelial cells produce more PAI‑1, a protein that blocks the breakdown of blood clots. This effect was seen only in certain cell types and involved activation of a signaling pathway (MAPK) and a DNA‑binding factor (AP‑1). For people interested in using Tβ4 to boost health, the result suggests it could raise clot‑preventing proteins, which might increase cardiovascular risk.

Utility 2
pubmed 2001

beta-Thymosins, small acidic peptides with multiple functions.

Huff. T T; Müller. C S CS; Otto. A M AM; Netzker. R R; Hannappel. E E

Beta-thymosin peptides, especially thymosin beta‑4, are tiny proteins found in almost every cell where they hold onto single actin units, stopping them from forming fibers until the cell needs them. They also show up outside cells in blood and wound fluid and have been linked to things like new blood‑vessel growth, reduced inflammation, and possibly helping cancer cells move more easily, though we still don’t know exactly how they work outside the cell.

Utility 2
pubmed Jun 28, 2007

Thymosin fraction-5 possesses antiproliferative properties in HL-60 human promyelocytic leukemia cells: characterization of an active peptide.

Spangelo. Bryan L BL; Roach. Joseph D JD; Hadi. Freidun F; Damavandy. Ali A AA; Plieskatt. Jordan J;...

Researchers found that a protein mix from bovine thymus, called thymosin fraction‑5, contains a small piece (about 6 kDa) that can stop human leukemia cells (HL‑60) from growing and can trigger early signs of cell death. This was shown in lab dishes using several cell‑growth tests and flow‑cytometry.

Utility 2
pubmed Aug 18, 2009

Thymosin-beta4 attenuates ethanol-induced neurotoxicity in cultured cerebral cortical astrocytes by inhibiting apoptosis.

Yang. Hao H; Cui. Guang-Bin GB; Jiao. Xi-Ying XY; Wang. Jian J; Ju. Gong G; You. Si-Wei SW

In lab-grown brain support cells, adding the peptide thymosin‑beta‑4 before exposing them to high levels of alcohol helped the cells stay alive. It reduced cell death signals, lowered oxidative damage, and boosted protective proteins, suggesting the peptide can guard brain cells against alcohol‑related harm in a dish.

Utility 2
pubmed 1996

Correlations between biological activity and structural properties for two short homologous sequences in thymosin beta4 and gelsolin.

Feinberg. J J; Mery. J J; Heitz. F F; Benyamin. Y Y; Roustan. C C

Researchers found that tiny pieces of the proteins thymosin‑beta‑4 and gelsolin, especially a short sequence with the pattern (I, V)EKFD, can stop actin from forming long fibers. The way these tiny pieces fold (their secondary structure) matters a lot for this activity.

Utility 2
pubmed Oct 5, 2004

Nuclear localisation of the G-actin sequestering peptide thymosin beta4.

Huff. Thomas T; Rosorius. Olaf O; Otto. Angela M AM; Müller. Christian S G CS; Ballweber. Edda...

Scientists found that the small protein thymosin‑beta‑4 can move from the cell’s fluid into the nucleus using an active transport system, and that only its front half (the N‑terminal part) goes into the nucleus while the back half stays in the cytoplasm. This suggests the peptide might also bind actin inside the nucleus, hinting at unknown nuclear functions.

Utility 2
pubmed 1993

Actin-sequestering ability of thymosin beta 4, thymosin beta 4 fragments, and thymosin beta 4-like peptides as assessed by the DNase I inhibition assay.

Hannappel. E E; Wartenberg. F F

The study shows that the whole thymosin‑beta‑4 protein can bind to single actin molecules and stop them from forming fibers, but short pieces of the protein that miss the first 12 amino acids cannot do this. Changing the methionine at position 6 to its oxidized form doesn’t stop the protein from working.

Utility 2
pubmed Mar 6, 2006

Thymosin beta4 and AcSDKP inhibit the proliferation of HL-60 cells and induce their differentiation and apoptosis.

Huang. Wei Qi WQ; Wang. Bao He BH; Wang. Qi Ru QR

In lab experiments, two small proteins that naturally come from bone marrow—thymosin‑beta‑4 and its fragment AcSDKP—were shown to slow down the growth of a leukemia cell line (HL‑60) and push those cancer cells to change shape, become more like normal cells, and eventually die. The effect got stronger at higher concentrations and seemed to involve raising calcium inside the cells.

Utility 2
pubmed 2004

Thymosin beta 4 and its N-terminal tetrapeptide, AcSDKP, inhibit proliferation, and induce dysplastic, non-apoptotic nuclei and degranulation of mast cells.

Leeanansaksiri. Wilairat W; DeSimone. Shirley K SK; Huff. Thomas T; Hannappel. Ewald E; Huff. Thomas...

The study shows that the protein thymosin beta‑4 and its short piece AcSDKP can stop mast cells from multiplying and push them into a growth‑stop state at extremely low concentrations, but higher doses make the cells release their stored chemicals. Only the whole peptide and the four‑amino‑acid piece work; broken‑down fragments do not.

Utility 2
pubmed 1995

The interaction of (1-4)-fragment of thymosin beta 4 with calmodulin-sensitive cAMP phosphodiesterase from hypothalamus.

Voelter. W W; Kapuzniotu. A A; Mihelic. M M; Gurvits. B B; Abrahamian. G G; Galoyan. A A

A tiny piece of the protein thymosin beta‑4 (four amino acids long) can bind to an enzyme in the brain that breaks down the signaling molecule cAMP. It makes the enzyme less active, especially when the enzyme normally needs a helper protein called calmodulin. This could change how cells in the immune and nervous systems communicate, but the study was done in isolated tissue and does not give any dosing or safety advice for people.

Utility 2
pubmed Apr 1, 2005

Identification of the positive and negative cis-elements involved in modulating the constitutive expression of mouse thymosin beta4 gene.

Hsiao. Hung-Liang HL; Su. Yeu Y

Scientists mapped the DNA region that controls how much mouse thymosin‑beta‑4 protein a cell makes. They found a short piece of DNA that drives very strong production of the protein, even stronger than a common lab promoter, and it works in human cells too. This knowledge is mainly useful for making the peptide in the lab, not for direct health‑boosting tips.

Utility 1
pubmed Oct 1, 1983

Thymosin beta arg10, a major variant of thymosin beta 10 in rabbit tissues.

Ruggieri. S S; Erickson-Viitanen. S S; Horecker. B L BL

This study just describes that rabbits have slightly different forms of two small proteins called thymosin beta‑4 and beta‑10, with the rabbit version of beta‑10 having an extra arginine and being present in similar amounts to the beta‑4 variant, unlike other animals where beta‑10 is much less abundant. It’s a basic biology finding, not a guide for using these peptides in humans.

Utility 1
pubmed 1983

In vitro synthesis of thymosin beta 4 encoded by rat spleen mRNA.

Filipowicz. A W AW; Horecker. B L BL

Scientists showed they can make the 43‑amino‑acid peptide thymosin‑beta‑4 in test‑tube systems using rat spleen RNA, confirming its exact structure but not revealing any new health effects or dosing tips.

Utility 1
pubmed Feb 16, 2018

Molecular Motions and Interactions in Aqueous Solutions of Thymosin-&#x3b2;<sub>4</sub> , Stabilin C-Terminal Domain (CTD) and Their 1:1 Complex Studied by <sup>1</sup> H&#x2005;NMR Spectroscopy.

Bokor. M&#xf3;nika M; Tantos. &#xc1;gnes &#xc1;; M&#xe9;sz&#xe1;ros. Attila A; Jenei. Bence B; Hamin...

The study used NMR to look at how the small peptide thymosin‑beta‑4 fragment and a piece of the stabilin protein behave in water and how they bind together. It found that the complex they form is quite flexible and has a lot of disordered parts, with about 40% of the peptide’s binding sites involved in the interaction.