TH9507 is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Updated 2025-10-03. Numbers and descriptions here follow the published literature rather than marketing material.
Practical handling centers on limiting moisture, oxygen, and temperature excursions. Lyophilized material is generally held at or below minus twenty degrees Celsius, protected from light and kept sealed until use. Once reconstituted, solutions are typically kept cold and used within a short window because hydrolysis and microbial growth both accelerate in liquid form. Repeated freeze-thaw cycles are avoided, since they promote aggregation. Vial contents should be inspected for particulates and clarity before analysis, and working aliquots are prepared to reduce the number of times the stock is opened.
Quantitation of the peptide relies mainly on reversed-phase high-performance liquid chromatography with ultraviolet detection, typically at 214 nanometers, where the peptide bond absorbs. Identity is confirmed by mass spectrometry, most often electrospray ionization coupled to liquid chromatography, and by peptide mapping after enzymatic digestion. Because related impurities differ only slightly in sequence or modification, method development emphasizes resolution rather than speed. Purity is usually reported as a percentage of the main peak area, with individual impurities listed separately when they exceed a defined reporting threshold.
Development work on the compound, originally designated TH9507, focused on conditions in which reduced growth hormone signaling is thought to contribute to altered body composition. The United States Food and Drug Administration approved it in 2010 for the treatment of excess visceral abdominal fat in adults with human immunodeficiency virus infection and lipodystrophy. Later research examined other populations, including adults with mild cognitive impairment, where a large trial did not meet its primary endpoints. This mixed record illustrates how a single mechanism can produce clear effects in one setting and inconclusive results in another.
Several related peptides act on the same receptor, including sermorelin, a shorter GHRH fragment, and modified analogs such as CJC-1295 and modified GRF(1-29) that are common in research settings rather than approved products. Tesamorelin differs from growth hormone itself in that it acts upstream, prompting the pituitary to release the hormone through physiological signaling rather than supplying it directly. Terminology in the literature distinguishes GHRH analogs, growth hormone secretagogues, and recombinant growth hormone, although popular discussion often blurs these categories together. Precise naming matters when comparing study results.
Tesamorelin is a synthetic peptide of 44 amino acids that reproduces the sequence of human growth hormone-releasing hormone (GHRH) and carries a trans-3-hexenoyl group on its N-terminal tyrosine. That small fatty-acid modification blocks cleavage by dipeptidyl peptidase-4, the enzyme that rapidly degrades native GHRH in plasma. The result is a molecule with a longer circulating half-life than the natural hormone while retaining the same receptor target. It is supplied as a lyophilized powder for reconstitution and belongs to the broader class of GHRH analogs studied for effects on pituitary growth hormone secretion.
| Property | Value | Notes |
|---|---|---|
| Routine purity assay | Reversed-phase HPLC | Ultraviolet detection near 214 nm |
| Identity confirmation | Liquid chromatography–mass spectrometry | Mass shift reveals modification or truncation |
| Typical purity specification | Greater than 95 percent | Reported as main-peak area percentage |
| Long-term storage | Minus 20 degrees Celsius or colder | Sealed, protected from light |
| Principal degradation routes | Oxidation, deamidation, aggregation | Monitored individually during stability studies |
特沙莫瑞林的检测通常依赖反相高效液相色谱和质谱联用。反相色谱可分离肽主峰与缺失序列、氧化产物等杂质，质谱则提供精确质量以确认身份。对于复杂基质中的定量，常采用液相色谱-串联质谱，并配合固相萃取或蛋白沉淀。生物样品中的肽易降解，因此采集和处理条件会影响结果。
稳定性研究通常考察温度、光照、湿度和 pH 对肽链的影响。冻干粉在低温避光条件下较为稳定，复溶后则需控制保存时间并避免反复冻融。肽类可能发生氧化、脱酰胺、水解和聚集，这些变化会改变色谱纯度。强制降解实验用于识别主要降解途径并验证分析方法的专属性。
The hexenoyl cap slows the enzyme step that trims the amino terminus of native GHRH, the same step that shortens its active lifetime in circulation. As a result, the modified peptide persists longer in plasma than the unmodified hormone in side-by-side comparison. Receptor activity stays broadly comparable, because the added group sits away from the residues that contact the binding site. This combination, preserved receptor activity with reduced degradation, explains why the analog was developed instead of the native sequence.
Several compounds share the GHRH framework, including sermorelin, the shorter 1-29 fragment, and other analogs built on the full 1-44 chain. Naming follows a common convention: a stem that identifies the peptide plus a suffix marking analog status. Reports may describe tesamorelin by its sequence fragment, as a GHRH(1-44) analog, or by its amino-terminal modification. Indexing the compound therefore requires searching all of these forms, since some older literature predates the current international nonproprietary name.
Tesamorelin is a synthetic peptide built from 44 amino acids and classified with the growth hormone–releasing hormone family. Its sequence corresponds to the human GHRH(1-44) backbone, carrying one structural change at the amino terminus. That change is a trans-3-hexenoyl group placed where the natural peptide would have an unmodified end. The modification is the feature that separates the compound from the endogenous hormone in name, in stability, and in how it is handled in the laboratory.
The peptide is supplied as a lyophilized powder in single-use vials and is normally kept refrigerated between two and eight degrees Celsius, protected from light. Once dissolved, the solution is handled carefully because peptide bonds and the acyl modification can degrade under warm or alkaline conditions. Vials are inspected for cracks, and the powder is checked for color and uniformity before handling. Temperature excursions during shipping are a frequent reason for quality questions.
Identity and purity are assessed with reversed-phase high-performance liquid chromatography, which separates the peptide from truncated or oxidized forms. Mass spectrometry confirms the expected molecular weight, and peptide mapping after enzymatic digestion verifies the amino acid sequence. Water content is measured because residual moisture affects stability, and tests for aggregates or particulates are standard for injectable peptides. Circular dichroism can indicate whether the molecule has adopted an unexpected secondary structure in solution.
Research supply is often accompanied by a certificate of analysis listing chromatographic purity, mass confirmation, and storage conditions. Laboratories compare that document with an independent test when material is intended for bench work, since certificates describe a batch rather than an individual vial. Published studies usually state the source and purity of the peptide because small differences in purity can shift measured activity. Full analytical validation is rarely reported, which leaves batch-to-batch comparability an open question.
ICV injection of α-Interferon has been used for the treatment of intracranial malignancies in the clinic. α-Interferon has antiviral, antibacterial, and immunostimulatory properties. However, severe central nervous system symptoms occur after injection for ICV, intravenous, and intramuscular routes of administration. Additionally, only .09-.18% of the total Interferon dose was seen to pass through the blood-brain barrier when injected intramuscularly. In one study, intraperitoneal injection of α-Interferon was done on mice and there was no impact on monoamine levels. Another study conducted a similar experiment using the ICV injection method. This study showed reduced monoamine levels in the frontal cortex, in a dose-dependent manner. This indicates that ICV injection increases the percentage of the dose that reaches the mouse brain.
=== Degradation of DNA during bisulfite treatment === A major challenge in bisulfite sequencing is the degradation of DNA that takes place concurrently with the conversion. The conditions necessary for complete conversion, such as long incubation times, elevated temperature, and high bisulfite concentration, can lead to the degradation of about 90% of the incubated DNA. Given that the starting amount of DNA is often limited, such extensive degradation can be problematic. The degradation occurs as depurinations resulting in random strand breaks. Therefore, the longer the desired PCR amplicon, the more limited the number of intact template molecules will likely be. This could lead to the failure of the PCR amplification, or the loss of quantitatively accurate information on methylation levels resulting from the limited sampling of template molecules. Thus, it is important to assess the amount of DNA degradation resulting from the reaction conditions employed, and consider how this will affect the desired amplicon. Techniques can also be used to minimize DNA degradation, such as cycling the incubation temperature. In 2020, New England Biolabs developed NEBNext Enzymatic Methyl-seq, an alternative enzymatic approach to minimize DNA damage. Instead of bisulfite, APOBEC is used to convert C into U. Distinction between C, 5mC, and 5hmC is granted by the further modifications that "protect" the modified bases from APOBEC.
=== Powder === Powder is either the pure drug by itself (talcum powder), or is made of the drug mixed in a carrier such as corn starch or corn cob powder (Zeosorb AF – miconazole powder). Can be used as an inhaled topical (cocaine powder used in nasal surgery).
=== Scientific journal articles === Holick, MF (2007). "Vitamin D deficiency". N Engl J Med. 357 (3): 266–81. doi:10.1056/NEJMra070553. PMID 17634462. S2CID 18566028. Holick, MF (2006). "Resurrection of vitamin D deficiency and rickets". J Clin Invest. 116 (8): 2062–72. doi:10.1172/JCI29449. PMC 1523417. PMID 16886050. Pietras, SM; Obayan, BK; Chai, MH; Holick, MF (2010). "Vitamin D2 treatment for vitamin D deficiency and insufficiency for up to 6 years". Arch Intern Med. 169 (19): 1806–8. doi:10.1001/archinternmed.2009.361. PMID 19858440. Biancuzzo, RM; Young, A; Bibuld, D; Cai, MH; Winter, RM; Klein, EK; Ameri, A; Reitz, R; Salameh, W; Chen, TC; Holick, MF (2010). "Fortification of orange juice with vitamin D(2) or vitamin D(3) is as effective as an oral supplement in maintaining vitamin D status in adults". Am J Clin Nutr. 91 (6): 1621–6. doi:10.3945/ajcn.2009.27972. PMC 2869510. PMID 20427729. Holick, MF; Binkley, NC; Bischoff-Ferrari, HA; Gordon, CM; Hanley, DA; Heaney, RP; Murad, MH; Weaver, CM; et al. (2011). "Evaluation, treatment, and prevention of vitamin D deficiency: an Endocrine Society clinical practice guideline". J Clin Endocrinol Metab. 96 (7): 1911–30. doi:10.1210/jc.2011-0385. PMID 21646368.
Sources: en.wikipedia.org
== Human proteins containing this domain == BMP binding endothelial regulator (BMPER) Cysteine-rich motor neuron 1 protein (CRIM1) Extracellular matrix protein 2 (ECM2) Fraser extracellular matrix complex subunit 1 (FRAS1) Neural EGFL like 1 (NELL1) Neural EGFL like 2 (NELL2) Peroxidasin like (PXDNL) Von Willebrand factor C and EGF domain-containing protein (VWCE) Von Willebrand factor (VWF)
=== Collagen-like characteristics === Spongin and collagen exhibit comparable filament structure, both displaying a hierarchical organization of nanofibrils, microfibrils, and fibers, as well as a triple-helical based structure. Spongin microfibrilis measure approximately 10 nm in diameter and exhibit a periodic banding pattern every 60 nm, comparing to collagen's 67 nm periodicity. Despite the structural similarities, amino acid analysis reveals that spongin contains significantly higher levels of tyrosine residues, approximately 90% of which are mono- or di-brominated derivatives. This abundance of tyrosine is related to the oxidation of phenylalanine residues, which are prevalent in collagen but nearly absent in spongin. The brominated tyrosine derivatives are hypothesized to play a crucial role in stabilizing spongin's triple-helical structure through cross-linking.
The articular cartilage function is dependent on the molecular composition of the extracellular matrix (ECM). The ECM consists mainly of proteoglycan and collagens. The main proteoglycan in cartilage is aggrecan, which, as its name suggests, forms large aggregates with hyaluronan and with itself. These aggregates are negatively charged and hold water in the tissue. The collagen, mostly collagen type II, constrains the proteoglycans. The ECM responds to tensile and compressive forces that are experienced by the cartilage. Cartilage growth thus refers to the matrix deposition, but can also refer to both the growth and remodeling of the extracellular matrix. Due to the great stress on the patellofemoral joint during resisted knee extension, the articular cartilage of the patella is among the thickest in the human body. The ECM of articular cartilage is classified into three regions: the pericellular matrix, the territorial matrix, and the interterritorial matrix.
Sources: en.wikipedia.org
Reversed-phase high-performance liquid chromatography with ultraviolet detection is the standard technique for purity and content. Mass spectrometry provides orthogonal confirmation of identity. The two are normally used together rather than in isolation.
Removing water slows hydrolysis and limits the mobility that drives aggregation. A dry powder is also less hospitable to microbial growth. These factors make cold storage of the solid form more forgiving than storage of a reconstituted solution.
Methionine oxidation, asparagine and glutamine deamidation, and non-covalent or covalent aggregation are the main routes reported for peptides of this class. Each is tracked as a separate impurity. Their relative abundance depends on formulation and storage history.
It is a synthetic peptide built from 44 amino acids arranged in the same order as human growth hormone-releasing hormone. A short fatty-acid chain, described as a trans-3-hexenoyl group, is attached to the first amino acid. The finished molecule is formulated as a sterile powder that is dissolved before use.