pe
pep-10917 v1 CC-BY-SA-4.0

Thymulin (FTS): immune system hormone that helps T cells grow up

A natural hormone made by the thymus gland that helps immune cells mature; requires zinc to work; experimental, not yet an approved drug.

statuscomputed targetIMMUNE length9 aa refs2
snapshot preclinical 0% confidence
Class
Thymic peptide — zinc-dependent immunomodulatory nonapeptide
Status
No approved therapeutic indication in any major regulatory jurisdiction
Best-supported effect
Endogenous role in T-cell differentiation and maturation (animal / in vitro; established immunology); zinc supplementation restoring endogenous thymulin activity in zinc-deficient populations (human RCT evidence — zinc intervention, not exogenous peptide administration)
Main caveat
Best-evidenced clinical action for supporting thymulin biology is correcting zinc deficiency, not injecting synthetic thymulin. Human evidence for exogenous synthetic thymulin is thin: decades-old investigational work in small immunodeficient cohorts; no completed controlled human efficacy trial
status 2 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.841
pTM0.879
avg pLDDT63.4
ranking score0.905
STRUCTURE · PEP-10917 × IMMUNE
ranking0.905
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence9 aa
159
EAKSQGGSN
in the news 11 articles
overview readme

Snapshot

Class: Thymic peptide — zinc-dependent immunomodulatory nonapeptide
Evidence tier: Animal-only evidence
Status: No approved therapeutic indication in any major regulatory jurisdiction
Best-supported effect: Endogenous role in T-cell differentiation and maturation (established immunology; animal and in vitro); zinc supplementation restores endogenous thymulin activity in zinc-deficient populations (human RCT evidence — zinc intervention, not exogenous peptide administration)
Main caveat: The best-evidenced clinical action for supporting thymulin biology is correcting zinc deficiency, not injecting synthetic thymulin. Human evidence for exogenous synthetic thymulin administration is thin: decades-old investigational work in small immunodeficient cohorts with no controlled efficacy trials. The endogenous biology is well-characterized; the exogenous therapeutic use is not


What this is

Thymulin is a nine-amino-acid (nonapeptide) hormone produced by thymic epithelial cells. It requires a tightly bound zinc ion to be biologically active — the peptide without zinc (apothymulin) is essentially inert as a receptor ligand. Thymulin plays a central role in T-cell differentiation and maturation, and its circulating levels decline as the thymus involutes with age.

Originally called Facteur Thymique Sérique (FTS), the peptide was isolated and characterized beginning in the 1970s by Jean-François Bach, Mireille Dardenne, and colleagues at the Necker Hospital and INSERM in Paris. Across the 1970s through 1990s, the Bach/Dardenne group established thymulin's role in CD4/CD8 T-cell lineage commitment, its zinc dependence, its circadian regulation by melatonin, and its bidirectional relationship with the hypothalamic-pituitary-thymic axis. The zinc-dependence observation also explained a longstanding clinical pattern: zinc deficiency produces immune phenotypes resembling thymic atrophy, and zinc repletion restores functional thymulin activity in deficient individuals.

Despite this scientific depth, thymulin has never been developed into an approved therapeutic. More recent preclinical research — using both the parent nonapeptide and thymulin-related analogs, particularly the peptide analogue of thymulin (PAT) — has explored analgesic, anti-inflammatory, and disease-model applications in animal systems. Human translational work has not followed.


Evidence map

Evidence layerGradeWhat it supports
HumanObservational / biomarkerMultiple human clinical trials and RCTs have characterized endogenous thymulin biology: zinc supplementation restores functional thymulin levels in zinc-deficient populations (elderly, IBD, pediatric malnutrition, AIDS patients); melatonin drives nocturnal thymulin elevation in humans; serum thymulin is measurably reduced in human zinc deficiency. These are endogenous biomarker studies and zinc intervention trials — not exogenous synthetic thymulin administration trials. Source describes historical small investigational studies in immunodeficient cohorts as the only human exposure evidence for the synthetic peptide; individual trial records are not extracted
AnimalModerateT-cell maturation and differentiation; anti-inflammatory effects in rodent models of inflammation and sepsis; analgesic effects in pain behavior models; protection in experimental MS (EAE), streptozotocin-induced type 1 diabetes, and allergic asthma models. Both parent nonapeptide and PAT analog studied across models
In vitroModerateZinc-binding site characterization; receptor binding on T-cell precursors; protein kinase C activation; intracellular calcium dynamics in thymocytes; cytokine modulation; antibody generation tools
ComputationalNone identifiedNo computational or structure-prediction data present in source
MechanismStrong (endogenous biology)Zinc-thymulin complex binds high-affinity surface receptors on T-cell precursors, activating PKC signaling; role in CD4/CD8 lineage commitment and cytokine regulation is well-established across decades of immunology. Translation of this mechanism to exogenous parenteral synthetic thymulin in adult humans has not been confirmed in controlled studies

Source-concentration and replication note: The foundational characterization of thymulin and much of the preclinical evidence originates from the Bach/Dardenne research group at INSERM Paris. Human data is from zinc supplementation intervention studies and observational biomarker work — not from controlled trials of exogenous synthetic thymulin. Animal evidence for pain and inflammation involves both the parent nonapeptide and PAT (a distinct analog molecule); evidence for the parent peptide specifically and evidence for the analog should not be conflated.


Claim check

ClaimVerdictEvidence layerConfidence
Zinc-thymulin complex is required for biological activity; zinc-free apothymulin is inactiveSupported (in vitro / biochemical)In vitroHigh — foundational biochemistry; established across zinc-binding and receptor assays
Zinc supplementation restores endogenous thymulin activity in zinc-deficient populationsSupported (human RCTs — zinc intervention)HumanHigh — multiple RCTs in elderly, IBD, AIDS, and pediatric malnutrition populations; this is evidence for zinc supplementation restoring endogenous thymulin, not for exogenous synthetic thymulin administration
Endogenous T-cell differentiation and maturation roleSupported (animal / in vitro)AnimalHigh — well-established immunology; animal models and in vitro systems
Anti-inflammatory and analgesic effects of exogenous thymulinSupported (preclinical)AnimalMedium — rodent models of inflammation, pain, sepsis; some evidence uses PAT analog rather than parent nonapeptide; no controlled human evidence for exogenous synthetic thymulin
Human efficacy for any indication via exogenous synthetic thymulin injectionNot establishedHumanHigh confidence in verdict — published literature explicitly states human evidence is thin, limited to decades-old small investigational studies in immunodeficient cohorts; no completed controlled human efficacy trial is extractable from source
Immune restoration in aging via injected synthetic thymulinNot establishedHumanHigh confidence in verdict — endogenous thymulin decline with aging is documented; published literature explicitly identifies "injecting thymulin restores a youthful immune system" as a myth; no controlled human efficacy trial present
Thymulin is biologically equivalent to Thymosin Alpha-1ContradictedAnimal / humanHigh — distinct peptides with different structures, mechanisms, and clinical histories; published literature explicitly names this as a myth

Experimental exposure

This section reports exposure used in animal experiments and historical investigational human context. It does not establish human dosing.

ContextSystemExperimental exposureDurationEndpointLimitation
Rodent pain, inflammation, MS, diabetes, and sepsis modelsRats / miceMicrogram-range doses by intraperitoneal or subcutaneous routes; per-study doses not individually extractedDays to weeks per studyPain behavior scores, inflammatory markers, cytokine levels, pathological markers in disease modelsRodent models; route and dose not validated in humans; some studies use PAT analog alongside parent peptide
Historical investigational human cohortsSmall immunodeficient patient populationsMicrogram-scale parenteral doses (historical); exact regimens not individually extracted in sourceShort windows; specific durations not extractedImmune parameter shiftsDecades-old; uncontrolled; selected populations; not applicable to current use contexts; no pharmacokinetic data from current research-chemical preparations
Human zinc supplementation trials (endogenous thymulin biomarker context)Elderly adults, IBD patients, pediatric malnutrition, AIDS patientsOral zinc supplementation; exact doses not individually extracted per trialVariable per trialSerum thymulin activity restoration; immune parametersThese are zinc intervention trials — they measure restoration of endogenous thymulin activity as a biomarker endpoint; they are not exogenous synthetic thymulin administration trials and do not establish dosing for synthetic peptide

Preclinical safety signals

SignalSystemNotes
Generally described as well-tolerated in short animal studiesRodentSource-bundle general statement; detailed per-study animal toxicology not individually extracted
Biological inactivity without zincAll systemsZinc-free apothymulin is inactive; zinc status of the recipient and zinc-loading state of the synthetic preparation are pharmacologically relevant variables; no controlled study has characterized this difference in humans
Research-chemical supply qualityNot a biological signalPurity, peptide identity, and endotoxin contamination vary substantially across unregulated suppliers; not independently characterized for end users
Long-term safety of chronic exogenous administrationNot establishedNo chronic human safety data present in source; long-term animal toxicology not individually extracted

Source-described theoretical cautions (no controlled safety program attached): Active autoimmune disease — thymulin's T-cell maturation role makes immune effects in autoimmune populations uncharted; organ transplantation requiring immunosuppression — interference with immunosuppression regimens is unstudied; pregnancy and breastfeeding — no reproductive safety data; pediatric populations — no studies of synthetic exogenous thymulin in children; known hypersensitivity to peptide therapeutics or excipients in research-chemical preparations of unverified composition; use of unverified research-chemical material in any clinical context — purity and endotoxin status are not assured outside regulated supply chains.

No human adverse event table is present in the attached source. Human safety data for exogenous synthetic thymulin administration in controlled conditions has not been individually extracted in this card.


Regulatory status

Region / bodyStatusNotes
US (FDA)Not approvedNo FDA-approved indication; no legitimate prescription pathway identified in source; synthetic thymulin in the research-chemical market is labeled "not for human consumption" and is not authorized for therapeutic use
EUNo marketing authorization (per available sources)Per available sources, no EU marketing authorization; not independently refreshed in this card
UKNo marketing authorization (per available sources)per available sources
CanadaNo marketing authorization (per available sources)per available sources
AustraliaNo marketing authorization (per available sources)per available sources
Eastern EuropeInvestigational / limited historical useSource notes a longer history of investigational and limited-use status for thymic peptides in some Eastern European countries; no current major-market approval identified
WADANot specifically named; likely falls under S0Per available sources, thymulin is not specifically named on the WADA Prohibited List; source notes it would fall under S0 (substances not approved by any governmental health authority for human therapeutic use) for athletes using exogenous synthetic thymulin; status is per available sources and not independently verified against the current WADA list

Zinc supplementation is an over-the-counter dietary supplement and is not WADA-prohibited.


Mechanism

Thymulin binds to high-affinity surface receptors on T-cell precursors in the thymus, promoting their differentiation into mature CD4+ and CD8+ T-cells. Biological activity is strictly dependent on the peptide carrying a bound zinc ion; without zinc, the apoprotein does not activate the receptor pathway. The zinc-thymulin complex activates protein kinase C (PKC) signaling and influences intracellular calcium dynamics in thymocytes. Downstream effects include modulation of cytokine production, enhancement of natural killer cell activity, and influence on the hypothalamic-pituitary-adrenal axis through the neuroendocrine-thymic axis.

Endogenous thymulin levels follow a circadian pattern with nocturnal peaks linked to melatonin signaling. This circadian regulation is established in both animal and human biomarker studies.

In preclinical pain and inflammation models, thymulin and related analogs — particularly the peptide analogue of thymulin (PAT) — have shown analgesic and anti-inflammatory effects attributed to modulation of spinal inflammatory signaling pathways and neuroinflammation attenuation. The relative contributions of the parent nonapeptide and PAT in these models have not been cleanly separated across studies.

Target confidence is verified for endogenous thymulin biology. Translation of the receptor-level mechanism to parenterally administered synthetic thymulin in adult humans has not been established in controlled studies.


Chemistry

FieldValue
Common nameThymulin
Other namesFacteur Thymique Sérique (FTS), FTS, Zinc-Thymulin, Serum Thymic Factor
SequencepGlu-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn (9 residues; N-terminal pyroglutamate)
Length9 amino acids (nonapeptide)
TopologyLinear
Key featureRequires zinc cofactor for biological activity; zinc-free apothymulin is biologically inactive
Molecular weight~857 Da (apoprotein; approximate; does not include bound zinc)
FormulaNot individually extracted from source
CASNot individually extracted from source
Sequence confidenceNeeds review — sequence is from established thymulin literature; available literature does not provide a machine-readable sequence string; needs independent verification against primary chemistry source

The zinc-binding requirement is a pharmacologically defining property. The zinc status of the recipient and the zinc-loading state of any synthetic preparation are both relevant variables for any exogenous administration context — and this has not been characterized in controlled human studies.


Open questions

  • Central translational gap: Whether adding exogenous synthetic thymulin to a zinc-replete patient produces any clinical benefit beyond what zinc supplementation alone achieves has never been tested in a controlled human study. This is the foundational unanswered question for any therapeutic use of the synthetic peptide.
  • Human pharmacokinetics of current research-chemical preparations: Absorption, distribution, half-life, and tissue uptake have not been characterized in humans for synthetic thymulin as currently sold. Dosing rationale is entirely speculative in the absence of PK data.
  • Zinc-status interaction in exogenous administration: Injecting synthetic thymulin into zinc-deficient and zinc-replete patients would be expected to produce different pharmacological outcomes; no controlled study has characterized this difference.
  • Parent nonapeptide vs PAT contributions: Preclinical evidence for analgesic and anti-inflammatory effects involves both the parent thymulin nonapeptide and PAT, a distinct synthetic analog. The extent to which observations in animal models are attributable to each molecule separately is not clearly resolved across published research literature.
  • Long-term safety of chronic exogenous administration: No chronic human safety data is present in this card. The immune consequences of sustained exogenous thymulin in adults are unknown.
  • Research-chemical supply quality: Purity, peptide identity, and endotoxin contamination vary substantially across research-chemical thymulin suppliers and have not been independently characterized for end users.
  • Human translation of preclinical disease-model findings: Promising animal results in MS, asthma, and type 1 diabetes models have not been followed by published human controlled trials. Translation potential is unknown.
Hypotheses4 directions▾ collapse

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.

openupdated 2026-06-05

Does zinc make thymulin active by forcing it into a specific shape that a zinc-free but pre-shaped version might also achieve?

The zinc requirement makes thymulin unstable and hard to develop as a drug. If a rigidified version could work without zinc, it could be manufactured reliably, stored more easily, and potentially given orally, making it a realistic medicine for immune deficiency and aging.

The hypothesis
Thymulin's zinc-dependent activity operates through a zinc-induced conformational switch in the EAKSQGGSN backbone that creates a negatively charged face (E1, the Glu carboxylate) opposing a positive-polar face (K2, A3 backbone) required for receptor engagement, and apothymulin's inactivity is caused by loss of this constrained presentation rather than loss of a zinc-contact needed by the receptor.
Why it’s plausible
EAKSQGGSN contains Glu at position 1 and Lys at position 2, creating a local electrostatic dipole. The remaining residues (A, S, Q, G, G, S, N) are small, polar, or flexible. Free Glu-1 carboxylate and free Lys-2 amine in apothymulin would electrostatically repel each other in solution, preventing the peptide from adopting the constrained turn needed for receptor contact. Zinc coordination by E1 and by another donor in the peptide (S3 or S7 hydroxyl, or the N-terminal amine) would neutralize E1's charge and bridge the backbone into a loop, enabling receptor engagement. This predicts that a cyclic analog locking the same conformation would be active even without zinc.
Why it matters
A zinc-independent conformationally constrained thymulin analog would overcome the instability of the zinc-peptide complex in vivo and enable development of stable exogenous thymulin therapeutics that do not require co-administration of zinc.
Plausibility.60
Novelty.50
Impact.65
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceEAKSQGGSN: E1 carboxylate and K2 amine are adjacent; zinc coordination would neutralize the E1 side chain and bridge the backbone; S3 and S7 provide additional coordination candidates
[2]
paper
Thymulin receptors exist on T cell lines with defined affinities; the zinc-peptide complex but not apothymulin binds these receptors, implying that zinc creates the active conformation rather than directly contacting the receptor
doi: 10.1517/14728220903512991
[3]
noteZinc is required for biological activity; apothymulin is essentially inert; the Bach/Dardenne group established this across decades of biophysical and immunological work
openupdated 2026-06-05

Could chemists make a circular version of thymulin that stays in the active shape on its own, bypassing the need for zinc entirely?

The zinc requirement makes thymulin fragile and difficult to deliver as a drug. A self-stable ring version would be far easier to manufacture and store, could survive longer in the bloodstream, and might even work as a pill, transforming an interesting research compound into a real medicine for immune deficiency.

The hypothesis
A Zn2+-chelating cyclic analog of thymulin, in which E1 and S8 are bridged by a synthetic zinc-coordinating motif, would be constitutively active (zinc-independent) and substantially more protease-resistant than linear EAKSQGGSN, enabling parenteral or potentially oral delivery without the pharmacokinetic limitations of the native zinc-peptide complex.
Why it’s plausible
EAKSQGGSN contains E (carboxylate), K (amine), and multiple S/N (hydroxyl/amide) residues suitable for metal coordination. The native zinc complex likely forms a pseudo-cyclic structure through coordination-induced backbone constraints. Engineering a covalent macrocyclic lactam or thioether bridge between positions 1 and 9 (or 1 and 8, E-N or E-S) would lock the zinc-bound conformation permanently. Linear peptides with multiple Ser and Gly residues are rapidly degraded by serum proteases; cyclization dramatically increases half-life. The Gly-Gly motif at positions 6-7 is a known flexible linker that accommodates the turn required for cyclic closure.
Why it matters
A zinc-independent constitutively active thymulin mimic would be the first developable thymulin therapeutic with defined pharmacokinetics, overcoming the major obstacle that has stalled thymulin drug development for decades.
Plausibility.60
Novelty.50
Impact.65
Basis · grounding2 papers · 1 computed/note
[1]
sequenceEAKSQGGSN: E1 and N9 are 8 residues apart (feasible macrolactam ring size 10-11 atoms); G6G7 provides conformational flexibility for cyclization; S3/S7/S8 hydroxyl groups provide additional potential coordination sites
[2]
paper
Cyclic peptides can be completely resistant to proteolytic degradation; cyclization is a validated strategy for converting protease-labile linear peptides into stable drug candidates
doi: 10.1021/acs.joc.5b01878
[3]
paper
Amino acid substitutions for proteolytic resistance; cyclization and backbone modification provide complementary approaches to metabolic stability
doi: 10.3389/fmicb.2020.563030
openupdated 2026-06-05

Since thymulin needs zinc to work, is getting more zinc into thymic cells a more efficient way to boost thymulin activity than injecting synthetic thymulin?

Zinc supplements are safe, cheap, and widely available. If simply ensuring adequate zinc restores the body's own thymulin activity in older adults, it would be an immediate, low-cost public health intervention to reduce infection risk and potentially improve vaccine responses in the elderly.

The hypothesis
Systemic zinc repletion to the upper-normal range in zinc-insufficient elderly individuals is a more effective strategy for restoring thymulin-mediated immune function than exogenous synthetic thymulin injection, because the rate-limiting step is zinc availability to thymic epithelial cells rather than thymulin peptide availability.
Why it’s plausible
The readme explicitly states that zinc supplementation restores endogenous thymulin activity in zinc-deficient populations with human RCT evidence, whereas exogenous synthetic thymulin has only thin evidence from small uncontrolled studies. If zinc availability to thymic epithelial cells is rate-limiting, exogenous apothymulin administered without zinc would be inactive, and exogenous zinc-thymulin complex administration would need to compete with plasma metal-binding proteins. By contrast, zinc supplementation increases intracellular zinc in thymic epithelial cells, enabling biosynthesis of the full zinc-thymulin complex endogenously where it is most needed.
Why it matters
This would justify zinc supplementation as first-line intervention for thymulin-related immune decline in the elderly before committing to complex exogenous peptide drug development, with immediate clinical translability.
Plausibility.70
Novelty.30
Impact.70
Basis · grounding2 papers · 1 computed/note
[1]
noteHuman RCT evidence exists for zinc supplementation restoring thymulin activity in deficient populations; exogenous thymulin evidence is from decades-old small uncontrolled trials
[2]
paper
Synthetic thymulin used in over 250 subjects including RA and immunodeficiency patients; reported effects but no controlled efficacy trials, consistent with the hypothesis that zinc-repletion achieves similar or superior outcomes
doi: 10.1007/bf02985220
[3]
paper
Zinc is required for thymulin biological activity; thymic epithelial cell zinc availability is the gate through which zinc deficiency reduces thymulin-mediated T-cell maturation
doi: 10.1517/14728220903512991
openupdated 2026-06-05

Does thymulin boost immunity indirectly by first signaling through the pituitary gland rather than acting directly on immune cells?

If thymulin works through the brain-hormone system, it would open entirely new ways to deliver it, including nasal sprays that reach the brain. It would also connect immune decline in aging to the broader hormonal changes of aging, suggesting that treating one might treat the other.

The hypothesis
Thymulin acts on a receptor in the neuropeptide/neuroimmune axis rather than a conventional immune-cell surface receptor, given that the best-characterized downstream effects involve hypothalamic-pituitary modulation of thymic epithelial cell function rather than direct T-cell activation.
Why it’s plausible
The literature snippet from 10.1517/14728220903512991 notes that thymulin receptors were demonstrated on anterior pituitary cells, not only T cells. Gonadotropin and ACTH axis perturbations (gonadectomy, adrenalectomy) alter serum thymulin levels, and thymulin secretion is modulated by growth hormone and prolactin. This neuroendocrine reciprocal regulation suggests thymulin may signal both peripherally (on T cells) and centrally (on pituitary and hypothalamic cells), raising the possibility that its primary immunomodulatory action is indirect, mediated through hypothalamic-pituitary-immune axis modulation rather than direct T-cell receptor engagement.
Why it matters
If thymulin's primary receptor is neuroendocrine, the therapeutic target for immunosenescence reversal would shift from immune compartment to brain/pituitary, with implications for intranasal or CNS-targeted delivery strategies and for understanding why thymic involution is linked to age-related hormonal changes.
Plausibility.60
Novelty.45
Impact.65
Basis · grounding2 papers · 1 computed/note
[1]
paper
Thymulin receptors demonstrated on anterior pituitary cells; Brown et al. used pituitary cells to show thymulin binding, establishing a neuroendocrine receptor beyond T-cell lines
doi: 10.1517/14728220903512991
[2]
paper
Gonadectomy and adrenalectomy alter thymulin levels; gonadotropins and ACTH axis interacts with thymulin secretion; establishes bidirectional hypothalamic-pituitary-thymus communication
doi: 10.1016/j.peptides.2003.11.002
[3]
structureopenfold3 ipTM=0.841 against 'immune' annotated target; moderate-high confidence but 'immune' is a broad category that includes neuroimmune targets
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.8413631916046143 openfold3-mlx
ranking score 0.9048908352851868 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.426global PDE — lower = better
disorder0.112fraction disordered
chain pair ipTM (A, B)0.841interface quality
3-letter notation
Glu-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn
recipeopenfold3-mlx 0.3.1
parametervalue
modelopenfold3-mlx 0.3.1
weights
hardware
mlx version
python
random seed
msa strategy
diffusion samples1
runtime80s
predicted bymlx@peptide
predicted at2026-05-03
citationbibtex
peptidemodel (2026). Thymulin (FTS): immune system hormone that helps T cells grow up (pep-10917, v1). PeptideModel. https://peptidemodel.com/card/pep-10917
@peptide{pep10917,
  sequence = {EAKSQGGSN},
  target   = {immune},
  author   = {peptidemodel},
  year     = {2026},
  status   = {computed}
}
clinical trials 1 on ct.gov · 1 on EUCTR · checked 2026-05-09
ct.gov trials 1
EUCTR 1
PubMed RCT 2
by phase
1no phase
by status
1completed
references 2 papers
[2] supporting
discussion no comments
sign in to comment
peptidemodel.com CC-BY-SA-4.0 research only · not for human use