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Semax is a synthetic heptapeptide composed of Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP), incorporating an ACTH(4–7)-derived sequence with a C-terminal Pro-Gly-Pro tripeptide.
Semax is a synthetic peptide containing seven amino acids that has been obtained from the sequence of adrenocorticotropic hormone (ACTH). It is made up of the ACTH(4–7) fragment, Met-Glu-His-Phe, bonded to a Pro-Gly-Pro (PGP) tripeptide at its C-terminus, giving the overall sequence Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP). According to PubChem, Semax has the molecular formula C₃₇H₅₁N₉O₁₀S, a molecular weight of approximately 813.9 g/mol, and the CAS number 80714-61-0.
Semax is commonly described as a synthetic ACTH-derived or melanocortin-related peptide. The C-terminal PGP sequence distinguishes it structurally from the native ACTH fragment and has been incorporated into the molecule in connection with peptide stability and resistance to enzymatic degradation.
Experimental research has investigated Semax in relation to neurotrophin-associated signaling, gene-expression regulation and peptide structure–activity relationships. Preclinical studies have reported changes in the transcription of genes encoding neurotrophins and their receptors, including BDNF, NGF and Trk-family receptors, although these observations are model- and condition-dependent and do not establish a single definitive molecular mechanism.
Transcriptomic and proteomic studies have additionally examined Semax-associated changes in immune response, inflammatory, neurotransmission and intracellular signaling pathways in experimental animal models. The molecular mechanisms responsible for these observations remain an active area of investigation.
Laboratory research material should be described on the basis of its specified seven-amino-acid sequence, molecular identity, chromatographic purity, chemical form and the batch-specific analytical records. The results of experiments must be given as research observations and not be interpreted as indicating therapeutic efficacy or as being suitable for use in humans.
Semax is a synthetic linear heptapeptide made up of seven amino acid residues and has the sequence Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP); it may also be expressed as H-Met-Glu-His-Phe-Pro-Gly-Pro-OH, which shows the presence of a free amino group at the N-terminus and a carboxylic acid group at the C-terminus. Both PubChem and the FDA substance database list the same defined sequence.
Semax is made up of the Met-Glu-His-Phe (ACTH 4–7) sequence linked to a Pro-Gly-Pro (PGP) tripeptide at the C-terminus. This structural feature sets it apart from the native ACTH(4–10) fragment and gives it a well-defined structure that is suitable for comparative studies of peptides and for research into their stability. Studies that have been published have looked into the role of the PGP region in the molecular stability of peptide analogs derived from ACTH.
The peptide has one methionine residue, and it is this residue that provides the sulfur atom found in its molecular formula. Since it contains no cysteine residues, it does not form disulfide bonds that are derived from cysteine. Also, the presence of histidine means that there is a side chain containing imidazole, which is capable of taking part in metal-ion coordination under the appropriate experimental conditions.
For the free peptide, PubChem reports a molecular formula of C₃₇H₅₁N₉O₁₀S, molecular weight of approximately 813.9 g/mol, and CAS number 80714-61-0.
Semax may also be encountered in different salt or counterion forms, which can alter the reported molecular composition. For laboratory characterization, the sequence, chemical form, molecular identity and purity should therefore be evaluated against the batch-specific Certificate of Analysis.
Semax is a synthetic heptapeptide whose amino acid sequence is Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP). Investigations into its molecular mechanism have been carried out in a number of experimental systems, especially with regard to neurotrophin-associated signaling, the regulation of gene expression and melanocortin-related pathways. The present evidence indicates that the molecular effects observed for Semax may be due to a number of interacting pathways rather than a single well-defined receptor mechanism.
Neurotrophin-Associated Signalling
Experimental studies have examined Semax in relation to brain-derived neurotrophic factor (BDNF) and nerve growth factor (NGF) signaling. In animal models, Semax exposure has been associated with changes in the expression of genes encoding BDNF, NGF and their receptors. These findings provide a basis for investigating how the peptide may influence neurotrophin-associated transcription and intracellular signaling under defined experimental conditions.
Gene-Expression Regulation
Transcriptomic research has identified Semax-associated changes across groups of genes involved in receptor activity, intracellular signaling, immune processes and neurotransmission. The direction and magnitude of these changes depend on the experimental model, tissue and sampling interval, so they are best interpreted as molecular responses requiring further mechanistic investigation rather than evidence of a single defined pathway.
Melanocortin-Related Research
Semax includes the Met-Glu-His-Phe sequence corresponding to ACTH(4–7), thus linking its structure to that of the melanocortin peptide family. This has led to studies into the molecular processes associated with melanocortins. Yet it cannot be assumed that Semax replicates the full receptor pharmacology of native ACTH merely because it has this four-amino-acid sequence.
PGP Fragment and Peptide Stability
The Pro-Gly-Pro (PGP) sequence at the C-terminus is what sets Semax apart from its parent fragment, which is derived from ACTH. Experimental research has examined the effect of this region on peptide degradation and on the formation of shorter peptide fragments, thus providing a basis for the study of structure–stability relationships and peptide metabolism.
Semax may best be regarded as a research peptide aimed at studying neurotrophin-associated signaling, transcriptional responses, the biology of ACTH-derived peptides and peptide structure–activity relationships. However, these proposed mechanisms are still the subject of experimental investigation and must not be seen as proof of therapeutic efficacy or as indicating that it is suitable for use in humans.
This summary reflects findings reported in published preclinical and in vitro research. The original studies supporting this information are listed in the references.
Semax has been investigated in experimental models examining brain-derived neurotrophic factor (BDNF) and nerve growth factor (NGF) systems. Preclinical studies have reported changes in the expression of BDNF, NGF and their associated receptors following experimental Semax exposure, providing a framework for studying peptide-associated regulation of neurotrophin signaling.
Transcriptomic approaches have been used to examine changes in gene-expression profiles associated with Semax in experimental animal models. Reported transcriptional responses have involved genes associated with intracellular signaling, immune processes, vascular function and neurotransmission. These findings are model- and time-dependent and are best interpreted as areas for further mechanistic investigation.
Semax incorporates the Met-Glu-His-Phe sequence corresponding to ACTH(4–7), followed by Pro-Gly-Pro. This defined architecture makes Semax useful for comparative studies examining how modification of an ACTH-derived peptide sequence influences molecular behavior, stability and biological interactions.
The chromatographic and mass-spectrometric methods have been used to study the metabolism of Semax, and the research has shown the formation of shorter peptide fragments during degradation, enabling the investigators to look at the cleavage patterns and the role of the C-terminal Pro-Gly-Pro (PGP) region in peptide stability.
Semax has also been studied by means of more comprehensive transcriptomic and proteomic methods. These techniques enable scientists to detect groups of genes and proteins whose amounts change under specific experimental conditions, thus allowing them to formulate hypotheses regarding signaling networks that may be linked to the peptide. However, such associations do not in themselves prove that there are direct molecular targets or causal mechanisms.
Semax can be compared with ACTH-derived fragments, PGP-containing peptides and individual Semax fragments to investigate structure–activity relationships. These models can help determine how peptide length, sequence composition and the PGP region influence molecular properties and experimentally observed responses.
Semax's defined seven-residue structure also permits investigation using HPLC, LC-MS and tandem mass spectrometry. These approaches can be applied to molecular identity, chromatographic purity, degradation products and peptide fragmentation, providing analytical information complementary to biological experiments.
Overall, these areas are best presented as molecular, biochemical and preclinical experimental research. Findings from cellular or animal models should not be extrapolated into claims of clinical efficacy, therapeutic benefit or suitability for human use.
The analysis of Semax Peptide must verify that it has the specified MEHFPGP sequence, that it matches the correct molecular identity, that it has the required chromatographic purity, and that it possesses the composition specific to each batch. Reversed-phase high-performance liquid chromatography (RP-HPLC) may be employed to separate intact Semax from related substances and to determine its chromatographic purity. HPLC has likewise been used in research that has been published to keep an eye on degradation and the formation of shorter peptide fragments under experimental conditions.
By comparing the molecular ions that are observed with those that are expected on the basis of the Semax structure, mass spectrometry (MS) gives additional information regarding identity. Reference analytical data show a protonated molecular ion at about m/z 814, this being in agreement with the peptide's molecular mass of approximately 813.9 Da.
For supplied research material, analytical results should be assessed against the batch-specific Certificate of Analysis, with attention to peptide identity, HPLC purity, molecular mass, chemical form and related substances. The applicable COA should remain the primary reference for specifications assigned to an individual batch.
Store Semax at 2–8°C. Keep it sealed and protected from light, moisture, heat, and humidity. Avoid frequent temperature changes during storage.
For laboratory handling, let a refrigerated, sealed vial reach room temperature before opening. This helps prevent condensation from forming inside the container. Reseal the vial after handling and return it to the recommended storage conditions.
Semax is a synthetic heptapeptide and not one that occurs in nature; it is made by combining the ACTH(4–7) fragment with the C-terminal Pro-Gly-Pro (PGP) tripeptide, thus yielding Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP).
ACTH(4–7) refers to the four-amino-acid sequence Met-Glu-His-Phe derived from positions 4–7 of adrenocorticotropic hormone. PGP represents Pro-Gly-Pro, which is attached to this sequence to form the seven-residue Semax molecule.
The PGP region distinguishes Semax structurally from the native ACTH-derived fragment and has been investigated in relation to peptide stability and degradation behavior. Experimental studies show that Semax undergoes defined enzymatic cleavage pathways and exhibits different degradation characteristics from ACTH(4–10).
Preclinical research has reported Semax-associated changes in expression of BDNF (brain-derived neurotrophic factor) and NGF (nerve growth factor) genes. These observations have been demonstrated in rat brain models and provide a basis for investigating Semax in neurotrophin-associated molecular signaling and transcriptional research.
No. Research has identified associations with neurotrophin expression, transcriptional regulation and other molecular pathways, but a single definitive molecular mechanism has not been established. More recent RNA-Seq research continues to identify Semax-associated changes across multiple groups of genes, reinforcing the need to treat its mechanism as an ongoing area of investigation.
Semax degradation has been examined using experimental systems including rat blood, serum, neuronal and glial cell cultures, and brain plasma membranes. HPLC-based studies have identified shorter degradation products, including HFPGP and PGP, providing information about enzymatic cleavage and peptide stability.
By comparing the molecular mass and fragmentation patterns that have been observed with those that are expected on the basis of the defined MEHFPGP structure, mass spectrometry can be used to establish the identity of a peptide. When mass-based analysis is combined with chromatographic separation, it offers additional information that is useful for telling the intact peptide apart from related molecular species or degradation products.
Batch-specific verification provides analytical information about the particular Semax research material supplied, rather than relying solely on the general peptide name. The relevant Certificate of Analysis and supporting analytical documentation should therefore be reviewed when assessing stated identity, purity, molecular characteristics and chemical form.
Semax is for laboratory research and analytical use only. It is not intended for human or animal consumption or administration, or for the diagnosis, treatment, cure, or prevention of any disease or medical condition. It is not intended for clinical, therapeutic, or veterinary use.
All information provided on this page is for scientific and research purposes only and should not be interpreted as medical advice or a recommendation for human or animal use.
