pe
pep-04429 v1 CC-BY-SA-4.0

Thymalfasin (Zadaxin): immune-boosting peptide for hepatitis B and C

A lab-made copy of a natural thymus hormone that strengthens the immune system; approved in over 35 countries to treat long-term hepatitis B and C, but not approved in the United States.

statusbioassayed targetANTIMICROBIAL length28 aa refs3
fda-approved
status 5 / 5 · 2 contributors
prediction metrics boltz-2 2.2.1
ipTM0.000
pTM0.497
avg pLDDT82.5
ranking score0.759
STRUCTURE · PEP-04429 × ANTIMICROBIAL
ranking0.759
?
RECEPTOR UNKNOWN
peptide conformation only · no target structure
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
sequence28 aa
151015202528
SDAAVDTSSEITTK DLKEKKEVVEEAEN
in the news 7 articles
overview readme

What this is

Thymalfasin (also called Thymosin Alpha-1 or Tα1, sold as Zadaxin) is a 28-amino-acid peptide that the thymus gland produces naturally to regulate immune function. It has been approved in more than 35 countries — including Italy, China, and much of Asia and Latin America — for the treatment of chronic hepatitis B and C and as a vaccine adjuvant in immunocompromised patients. It is not FDA-approved in the United States. Thymalfasin should not be confused with Thymosin Beta-4 (TB-500): despite sharing a family name, they are distinct peptides with different sequences, mechanisms, and indications.

History

Thymosin Alpha-1 was isolated in the 1970s by Goldstein and colleagues at the Albert Einstein College of Medicine, working from a thymus extract preparation called thymosin fraction 5 (Goldstein and colleagues, PNAS 1977). The 28-residue sequence — corresponding to the N-terminal segment of prothymosin alpha — was characterized as the principal immunologically active component of that fraction and shortly after produced synthetically. Goldstein subsequently co-founded SciClone Pharmaceuticals, which commercialized the synthetic peptide as Zadaxin (thymalfasin) for hepatitis B, hepatitis C adjunct therapy, and immune reconstitution. Regulatory approvals in more than 30 countries followed over the subsequent decades. In the United States, Thymosin Alpha-1 was never approved by the FDA despite multiple attempted indications; it remained accessible through compounding pharmacies until 2023, when the FDA removed it from the 503A compounding bulk substances list based on its size-and-complexity risk criteria — not on any specific harm signal.

What it does

Thymalfasin acts on the immune system rather than on a single receptor or tissue. It promotes the maturation and activation of T-cells — the immune system's primary adaptive fighters — and enhances the killing activity of natural killer (NK) cells. At the same time it modulates cytokine production to favor a coordinated Th1-type immune response without simply amplifying inflammation. The practical effect in clinical use is meaningful in specific immunocompromised or dysregulated-immunity contexts: improving the immune response to viral infections like hepatitis B and C, enhancing vaccine responsiveness in elderly or immunocompromised patients, and helping to restore immune homeostasis in conditions like severe sepsis and acute pancreatitis. It is more accurately described as an immune modulator than a generic immune booster — its strongest evidence is in states of immune dysfunction rather than in healthy people with vague complaints.

Mechanism

Thymalfasin acts on toll-like receptors TLR2 and TLR9 on dendritic cells, promoting their maturation and antigen-presentation capacity. This upstream effect drives T-cell differentiation and enhances both NK cell activity and cytotoxic T-lymphocyte function. Thymalfasin also upregulates MHC class I molecule expression, improving immune surveillance. The combined effect is a shift toward Th1-type cytokine profiles while modulating excessive inflammatory responses — the mechanistic rationale for its use in both infectious disease (hepatitis, sepsis) and as a vaccine adjuvant. The structural biology of the peptide has been characterized: NMR and molecular dynamics studies show Tα1 is intrinsically disordered in solution, adopting transient helical elements rather than a fixed fold (Elizondo-Riojas and colleagues, Biochemistry 2011).

Evidence

  • Human: Strong. Multiple randomized controlled trials and meta-analyses support efficacy in chronic hepatitis B (as an adjunct to entecavir or interferon-based regimens), chronic hepatitis C (adjunct to peginterferon/ribavirin in non-responders), severe sepsis, and acute pancreatitis. A large randomized trial in metastatic melanoma found no survival benefit when combined with interferon alfa and dacarbazine. RCT-level evidence also exists for vaccine adjuvant effects in elderly patients receiving influenza vaccination. For COVID-19, multiple observational reports and meta-analyses have been published but no large definitive randomized trial has produced a conclusive result. Garaci and colleagues (Annals of the New York Academy of Sciences, 2007) reviewed the full bench-to-bedside clinical trajectory.
  • Animal: Well-characterized immunology in preclinical models underpins the human trial program.
  • In vitro: Receptor-level mechanism (TLR2/TLR9 activation, dendritic cell maturation, MHC class I upregulation) established in cell-based studies.

Known effects

  • Hepatitis B immune response enhancement — Strong (multiple RCTs and meta-analyses; basis for international approval as Zadaxin)
  • Hepatitis C adjunct response — Moderate (RCTs in non-responders to interferon/ribavirin; adjuvant role, not monotherapy)
  • Severe sepsis immune restoration — Moderate (multicenter RCT evidence, ulinastatin combination protocols)
  • Acute pancreatitis immune support — Moderate (double-blind RCT evidence; reduced infection rates in severe acute pancreatitis)
  • Vaccine adjuvant in elderly/immunocompromised — Moderate (RCT evidence for influenza vaccination response enhancement)
  • COPD exacerbation reduction — Emerging (meta-analysis evidence)
  • Long COVID / post-viral immune restoration — Emerging (observational data showing restored T-cell homeostasis; no large RCT)
  • Cancer (metastatic melanoma) — Preclinical rationale not confirmed in large RCT; no benefit found in combination with interferon alfa + dacarbazine

Safety signals

Thymalfasin has a favorable safety profile in published trials. Injection site reactions are the most commonly reported adverse effect and are typically mild. The peptide has been well tolerated in trials lasting up to 6–12 months, including in elderly populations and patients with advanced liver disease. No withdrawal or rebound syndrome has been described. Formal drug-interaction studies are limited; available data derive from co-administration with antivirals and immunomodulators in hepatitis and sepsis trials, where no clinically significant pharmacokinetic interference was reported.

Regulatory status

  • US: Not FDA-approved for any indication. Removed from the 503A compounding bulk substances list in 2023 (risk-based size-and-complexity criteria, not a safety signal). 503B outsourcing facilities may compound under more restrictive conditions.
  • International: Approved in more than 35 countries as Zadaxin or thymalfasin for chronic hepatitis B, hepatitis C adjunct therapy, immune reconstitution in immunocompromised patients, and vaccine adjuvant use. Approved markets include Italy, China, the broader ASEAN region, parts of Latin America, and the Middle East. EU status is mixed — available in some member states under national authorizations, without centralized EMA approval.
  • WADA: Not listed by name on the WADA Prohibited List. Thymalfasin is an immune modulator rather than a performance or recovery enhancer in the WADA framework. Athletes subject to WADA code should be aware that WADA's S0 category can capture substances not approved for human therapeutic use in the athlete's jurisdiction.

Myths and misconceptions

  • "Thymalfasin is FDA-approved" — It is not FDA-approved for any indication. Approval in more than 35 other countries is a meaningful clinical track record, but approved-elsewhere is not equivalent to FDA-approved, and since 2023 the US compounding pathway has also narrowed.
  • "The 2023 FDA compounding decision means it was found to be unsafe" — The decision removed Thymalfasin from the 503A bulk substances list based on size-and-complexity risk criteria for compounded peptides, not on any specific harm signal. Its international safety record is favorable.
  • "Tα1 is a general immune booster for anyone with a weak immune system" — Its strongest evidence is in specific dysregulated-immunity contexts (chronic hepatitis, severe sepsis, vaccine response in the immunocompromised). Evidence for general "wellness" use in healthy individuals is substantially thinner.
  • "Thymosin Alpha-1 and Thymosin Beta-4 (TB-500) do similar things because they share a name" — They share only a family designation. Tα1 is a 28-residue immune modulator; Thymosin Beta-4 is a 43-residue actin-sequestering peptide primarily associated with tissue repair. They have distinct sequences, mechanisms, and regulatory histories.
  • "Tα1 was shown to cure COVID-19 based on Italian and Chinese data" — Early-pandemic observational reports suggested possible benefit in severe COVID-19, but no large randomized trial produced a definitive positive result, and no regulatory body authorized Tα1 for COVID-19.

Related peptides

  • LL-37 — a human cathelicidin antimicrobial peptide with innate immune and TLR-modulating activity; related through the innate immunity interface but distinct in origin and primary function.
  • Thymosin Beta-4 (TB-500) — the other prominent thymosin-family peptide in clinical and biohacker discussion; different sequence, different mechanism (actin sequestration and tissue repair rather than immune modulation), frequently confused with Tα1 due to the shared name.
Hypotheses5 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 2026-06-11

Could thymalfasin help sepsis survivors whose immune systems shut down and leave them vulnerable to new infections?

After surviving sepsis, many patients face weeks of dangerous immune weakness with no approved treatment. If thymalfasin could safely restart their immune response, it might prevent the secondary infections that kill many ICU patients after the initial crisis has passed.

The hypothesis
Thymalfasin could be effective as an adjunctive therapy in sepsis-induced immunoparalysis, where it might restore monocyte HLA-DR expression and T-cell responsiveness through the same immune reconstitution mechanism that underlies its hepatitis efficacy.
Why it’s plausible
Sepsis-induced immunoparalysis is characterized by a state of profound immune suppression in survivors that closely parallels the immunocompromised state thymalfasin was designed to correct. Mechanistically, both conditions involve reduced antigen presentation, T-cell anergy, and elevated regulatory T-cell activity. Thymalfasin is already approved for immune reconstitution in immunocompromised patients, suggesting its biological activity is state-dependent (it boosts suppressed immunity without causing autoimmunity in normal hosts), which is exactly the safety profile needed for sepsis adjunctive therapy.
Why it matters
Sepsis survivors face prolonged immune suppression and high rates of secondary infection with no approved immunostimulatory therapy. If thymalfasin reverses immunoparalysis, it could reduce ICU mortality and long-term morbidity in a large patient population with no current pharmacological options.
Plausibility.60
Novelty.50
Impact.80
Basis · grounding2 computed/notes
[1]
noteThymalfasin approved in 35+ countries for immune reconstitution in immunocompromised patients and as vaccine adjuvant, demonstrating a clinically validated ability to restore immune function from a suppressed state.
[2]
sequenceThe peptide's net acidic charge and thymus-derived origin are consistent with an endogenous homeostatic signal that corrects immune deficits rather than uniformly amplifying immunity, matching the conditional activity needed for sepsis-immunoparalysis treatment.
openupdated 2026-06-11

Could thymalfasin restart an immune response in patients whose cancer has become resistant to immunotherapy?

Checkpoint inhibitors help many cancer patients but stop working over time. If thymalfasin reactivates immune cells through a different pathway, it could give those patients a second chance at immune-driven remission.

The hypothesis
Thymalfasin could restore anti-tumor immunity in patients with PD-1/PD-L1 checkpoint inhibitor resistance by rescuing exhausted CD8+ T-cell populations through a mechanism independent of the PD-1 axis.
Why it’s plausible
A major unmet need in oncology is re-sensitizing tumors that are primary or acquired resistant to checkpoint blockade. Thymalfasin's known activity includes promoting T-cell maturation and function in immunocompromised states, which functionally overlaps with reversing exhaustion. Because thymalfasin was isolated from thymic tissue as a T-cell maturation factor, its mechanism likely involves transcriptional reprogramming of T-cell fate rather than blocking a single inhibitory ligand interaction, suggesting it could act orthogonally to PD-1/PD-L1.
Why it matters
If thymalfasin rescues T-cell exhaustion through a non-PD-1 pathway, it represents a combinable agent for the large and growing population of checkpoint-refractory cancer patients, potentially converting cold tumors to immunologically active ones.
Plausibility.50
Novelty.60
Impact.80
Basis · grounding2 computed/notes
[1]
noteThymalfasin approved for immune reconstitution in immunocompromised patients and as vaccine adjuvant, establishing its ability to restore functional T-cell responses from a suppressed baseline analogous to exhaustion.
[2]
sequenceAt 28 aa with no known receptor tyrosine kinase motif, thymalfasin is unlikely to directly block PD-1/PD-L1 interaction surfaces, implying any anti-exhaustion effect must proceed via a separate signaling axis.
openupdated 2026-06-11

Does thymalfasin only activate the immune cells that fight viruses without triggering the ones that cause inflammatory storms?

If thymalfasin is selective for the right immune cell type, it could be developed into a safer adjuvant for vaccines and immune therapies, particularly for elderly or immunocompromised patients who need a strong response without inflammation risk.

The hypothesis
Thymalfasin selectively activates innate immune responses in myeloid dendritic cells rather than plasmacytoid dendritic cells, and this cell-type selectivity is determined by the peptide's N-terminal SDAAVD segment.
Why it’s plausible
The two major dendritic cell subsets drive qualitatively different immune responses: myeloid DCs favor IL-12-driven Th1 and cytotoxic responses while plasmacytoid DCs drive interferon-alpha responses. Thymalfasin's clinical profile (benefit in chronic viral hepatitis requiring Th1 immunity, not interferonopathies) suggests myeloid DC bias. The N-terminal SDAAVD motif contains the beta-sheet-prone AAVD sequence that could mediate selective binding to surface lectins or scavenger receptors preferentially expressed on myeloid DCs.
Why it matters
Establishing DC-subset selectivity would explain why thymalfasin's adjuvant effect is well-tolerated (no interferon storm) and would guide engineering of analogs with tunable myeloid vs. plasmacytoid bias for different disease contexts.
Plausibility.45
Novelty.70
Impact.60
Basis · grounding3 computed/notes
[1]
sequenceN-terminal residues 3-7 (AAVDT) form a beta-strand-prone motif with high pLDDT=82.5 in monomer prediction, suggesting a structured surface-exposed epitope capable of selective receptor engagement.
[2]
structureboltz-2 monomer pLDDT=82.5 indicates a moderately well-folded peptide with a defined 3D shape, supporting the idea that the N-terminal segment presents a consistent binding surface rather than remaining disordered.
[3]
noteThymalfasin approved for hepatitis B and C, conditions requiring Th1 cellular immunity, consistent with myeloid DC rather than plasmacytoid DC activation.
openupdated 2026-06-11

Could a much shorter version of thymalfasin be just as effective as the full peptide?

If the active region is small, scientists could make a shorter, cheaper version that behaves the same way, making treatments more affordable and easier to deliver for patients in lower-income countries where thymalfasin is already widely used.

The hypothesis
The central alpha-helical segment of thymalfasin (approximately residues 14-22, DLKEKKEVV) constitutes the bioactive core responsible for receptor engagement, while the flanking disordered acidic tails serve primarily as solubility and stability enhancers with negligible independent activity.
Why it’s plausible
The sequence DLKEKKEVV (residues 14-22) contains the only amphipathic helical potential in the peptide: alternating hydrophobic (L14, V21, V22) and charged (K17, K18, K19, E20) residues consistent with a class A amphipathic helix. This is the type of motif commonly found in receptor-binding domains of immunomodulatory peptides. The flanking segments (SDAAVDTSSEIT and EEAEN) are rich in small polar residues that reduce aggregation but lack obvious receptor-contact geometry. If the central helix is removed or scrambled, activity should be lost; if only flanking tails are truncated, activity should be preserved.
Why it matters
Identifying a minimal bioactive core would enable design of shorter, cheaper, and potentially more potent thymalfasin analogs, reducing synthesis cost and improving pharmacokinetics for clinical applications.
Plausibility.50
Novelty.50
Impact.60
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceResidues 14-22 (DLKEKKEVV): L14 and V21/V22 provide hydrophobic face; K17, K18, K19 and E20 provide charged face, consistent with a receptor-binding amphipathic helix motif absent from the flanking regions.
[2]
structurepLDDT=82.5 for the full monomer suggests structured regions exist; the central segment is the most likely contributor given its amphipathic character, while terminal acidic residues are typically disordered in thymosin-family peptides.
[3]
paper
Original isolation from thymosin fraction 5 identified this 28-residue sequence as the immunologically active component, but subregion activity mapping was not reported.
doi: 10.1073/pnas.74.2.725
openupdated 2026-06-11

Could thymalfasin's real target be a human immune sensor rather than a bacterial membrane?

If true, drug developers could design sharper versions that tune the immune system more precisely, potentially helping patients with infections, cancer, or immune deficiencies without the risk of direct antimicrobial resistance pressure.

The hypothesis
Thymalfasin's annotated 'antimicrobial' target classification is a mislabeling, and its primary molecular target is a thymic epithelial receptor or toll-like receptor pathway component rather than a direct pathogen membrane.
Why it’s plausible
The annotated target 'antimicrobial' implies direct pathogen killing, yet thymalfasin's clinical approvals are for immune modulation in hepatitis and vaccine adjuvancy, not direct antimicrobial activity. The sequence SDAAVDTSSEITTKDLKEKKEVVEEAEN is highly acidic and amphipathic but lacks the cationic charge density (only 4 basic residues vs 6 acidic) that characterizes known membrane-disrupting antimicrobial peptides. This mismatch suggests the true binding partners are host immune receptors rather than microbial targets.
Why it matters
Correctly identifying the molecular target of thymalfasin would unlock rational engineering of analogs with improved receptor selectivity, explain why it modulates immunity without direct killing, and open new indications in autoimmune and checkpoint-related contexts.
Plausibility.70
Novelty.20
Impact.50
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceSDAAVDTSSEITTKDLKEKKEVVEEAEN has net negative charge at physiological pH (D2, D7, E18, E22, E23, E26 vs K15, K17, K19, K20), inconsistent with canonical cationic antimicrobial peptide behavior.
[2]
noteClinical approvals are for chronic hepatitis B, hepatitis C adjunct, and vaccine adjuvancy in immunocompromised patients, all immune-modulatory indications with no documented direct antimicrobial mechanism.
[3]
paper
Original isolation characterized the peptide as the immunologically active component of thymosin fraction 5, framing its activity as immunological, not microbicidal.
doi: 10.1073/pnas.74.2.725
details expand to inspect
full evidence table1 metrics
metricvaluetool
ranking score 0.7594963908195496 boltz-2
3-letter notation
Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn
recipeboltz-2 2.2.1
parametervalue
modelboltz-2 2.2.1
weights
hardwarevast_v100_32gb
mlx version
python
random seed1
msa strategynone_monomer
runtime
predicted by
predicted at2026-05-23
citationbibtex
peptidemodel (2026). Thymalfasin (Zadaxin): immune-boosting peptide for hepatitis B and C (pep-04429, v1). PeptideModel. https://peptidemodel.com/card/pep-04429
@peptide{pep04429,
  sequence = {SDAAVDTSSEITTKDLKEKKEVVEEAEN},
  target   = {antimicrobial},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
clinical trials 63 on ct.gov · 2 on EUCTR · checked 2026-05-22
ct.gov trials 63
with results 2
EUCTR 2
PubMed RCT 5
by phase
1phase 14phase 22phase 31phase 42no phase
by status
4completed2recruiting1not yet recruiting1withdrawn2unknown
references 3 papers
[2] computational (NMR + MD)
[3]
Thymosin alpha 1: from bench to bedside
Garaci, E. et al. Annals of the New York Academy of Sciences 2007
bioassay
discussion no comments
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