What is ACTH (11-24) C75H106N20O19S 22006-64-0, and what are its primary applications?

ACTH (11-24) C75H106N20O19S is a synthetic peptide derived from the adrenocorticotropic hormone (ACTH), specifically focusing on the amino acid sequence from positions 11 to 24. This peptide sequence is known for its significant role in stimulating the adrenal cortex to produce and release glucocorticoids such as cortisol. The structure, consisting of 75 carbon (C), 106 hydrogen (H), 20 nitrogen (N), 19 oxygen (O), and 1 sulfur (S) atoms, ensures its functionality and interaction with cellular receptors. The chemical registry number 22006-64-0 identifies its unique composition across global scientific databases. One of the primary applications of ACTH (11-24) is in research settings, where it is used to explore adrenal function and endocrine system pathways. Scientists rely on this peptide to understand better the mechanisms of hormone action, receptor binding, and downstream effects in the body. Research into the peptide’s role expands across numerous therapeutic areas, including stress response mechanisms, immune function, and metabolic regulation. By studying ACTH (11-24), researchers aim to develop novel treatments for disorders like Addison's disease, Cushing’s syndrome, and other adrenal gland disorders.
In addition to its fundamental research applications, ACTH (11-24) serves as a tool for assaying the role of the adrenal axis in different physiological and pathological processes. For example, its ability to mimic the action of endogenous ACTH makes it an invaluable reagent in pharmaceutical research and the development of glucocorticoid-related therapies. Furthermore, the peptide acts as a critical reference in pharmacokinetic and pharmacodynamic studies, helping researchers understand how hormones affect human health. By examining its structural and functional properties, scientists aim to leverage ACTH (11-24) to create synthetic derivatives for use in targeted therapeutic interventions, reducing adverse effects associated with full-length ACTH treatment.

How does ACTH (11-24) interact with biological receptors in the body?

ACTH (11-24) interacts with biological receptors in the body through a highly specific binding process that involves the melanocortin receptor family, particularly the melanocortin 2 receptor (MC2R), also known as the ACTH receptor. This interaction is critical for the peptide’s ability to stimulate the production and release of glucocorticoids. Upon binding to MC2R on the surface of adrenal cortex cells, ACTH (11-24) triggers a cascade of intracellular events. The receptor is coupled with the G-protein, specifically the G-protein ADcyc, which stands for adenylyl cyclase-activating G-protein. When ACTH (11-24) binds to MC2R, it causes a conformational change that activates the associated G-protein. This activation, in turn, stimulates the enzyme adenylyl cyclase located on the inner membrane of the cell. Adenylyl cyclase catalyzes the conversion of ATP to cyclic adenosine monophosphate (cAMP), a secondary messenger essential for mediating ACTH's effects.
Increased levels of cAMP activate protein kinase A (PKA), which phosphorylates specific transcription factors and other proteins, leading to changes in gene expression. These changes ultimately result in the production of steroidogenic enzymes that facilitate the biosynthesis of glucocorticoids like cortisol. Consequently, ACTH (11-24) plays an integral role in maintaining homeostasis, particularly in the body's response to stress. Furthermore, through its interaction with receptors, ACTH (11-24) contributes to various physiological responses such as the immune response, energy homeostasis, and the regulation of inflammation. It is of particular interest in understanding how these responses can be modulated to therapeutic advantage in conditions where cortisol regulation is disrupted. The precise action of ACTH (11-24) at the receptor level is a subject of continuous study, as it may reveal new targets for drug development seeking to harness or modulate the peptide’s effects. These interactions provide a model for exploring receptor binding dynamics and are crucial for advancing therapeutic strategies aimed at receptor-mediated pathways.

What are the differences between ACTH (11-24) and full-length ACTH in terms of function and use?

The differences between ACTH (11-24) and full-length adrenocorticotropic hormone (ACTH) in terms of function and use are grounded in their molecular structure, receptor binding affinity, and resulting biological effects. Full-length ACTH is a polypeptide made up of 39 amino acids and is the primary stimulus for adrenal gland activities in the production of cortisol and other corticosteroids. The entire hormone is synthesized from proopiomelanocortin (POMC) and plays a crucial role in the body's response to stress. On the other hand, ACTH (11-24) represents a truncated version of this hormone, comprising a smaller sequence of amino acids from the 11th to the 24th position. Although shorter, this segment retains the essential functional domains necessary for binding to the melanocortin 2 receptor (MC2R) and activating the cascade that leads to glucocorticoid production.
One significant difference in their function relates to biological activity. The full-length ACTH has been shown to engage multiple receptors and elicit a broader range of physiological responses than ACTH (11-24). This wider receptor affinity allows for diverse roles, including influencing skin pigmentation and appetite control, which are related to different members of the melanocortin receptor family. Conversely, ACTH (11-24), due to its truncated structure, may have a more limited interaction profile, predominantly targeting MC2R to modulate adrenal activity. This specificity can be advantageous in research settings where selective action is desired to study adrenal function without the confounding effects from other receptor pathways typically activated by the full-length hormone. In terms of use, full-length ACTH is utilized clinically to assess adrenal gland function through tests like the ACTH stimulation test. In contrast, ACTH (11-24) is more commonly confined to research applications where a focused analysis of the MC2R-mediated pathway is sought. Furthermore, ACTH (11-24) serves as a valuable tool in experimental setups that investigate MC2R activation due to its constrained receptor interaction compared to the full-length counterpart. These functional and application distinctions underline the utility of each form, allowing tailored approaches in both clinical and scientific research domains. Understanding these differences enhances the development of therapeutic strategies that leverage specific pathways in hormone-related diseases.

Are there any known side effects or risks associated with ACTH (11-24) in research studies?

While ACTH (11-24) itself is primarily utilized in preclinical and scientific research rather than clinical applications, understanding potential side effects or risks is crucial for safe laboratory practice. As a synthetic peptide harnessed to study adrenal gland function and related biochemical pathways, ACTH (11-24) generally presents a lower risk profile compared to full-length ACTH when used under controlled laboratory conditions. However, several factors can contribute to potential risks associated with its use. Firstly, the mode of administration and the concentration of peptide solutions can impact experimental outcomes and safety. High concentrations or improper handling might lead to unintended biological responses or artifacts in experimental settings. For accurate and safe results, researchers must diligently adhere to standardized protocols and dosing guidelines tailored to their particular model systems. Secondly, while ACTH (11-24) may not directly induce adverse effects, improper usage in laboratory animals or cellular models can result in misleading data that misconstrues the peptide’s effects. These inaccuracies could potentially skew the understanding of its role, especially concerning receptor interactions and subsequent hormonal pathways. It underscores the importance of robust study designs and cross-validation of results with complementary methods. Furthermore, peptides like ACTH (11-24) have the potential to degrade or form aggregates if not stored or prepared correctly, which may lead to reduced activity or unpredicted biological interactions. To mitigate such risks, researchers must ensure proper storage conditions, including temperature control and protection from light and moisture, preserving the peptide’s integrity throughout its usage period. Although direct adverse effects in the context of ACTH (11-24) research are minimal, laboratories must maintain rigorous safety standards and ethical guidelines when implementing this peptide in animal studies. Considerations must also be given to animal welfare and the minimization of discomfort or distress. Modern research frameworks often include institutional review boards or ethics committees that evaluate and approve study protocols, ensuring that ACTH (11-24) usage aligns with ethical scientific conduct. Such oversight helps safeguard the responsible use of peptides in research, fostering advancements in biological understanding while minimizing risks associated with scientific exploration.

Can ACTH (11-24) be used for therapeutic purposes, and if so, what is its potential?

The potential use of ACTH (11-24) for therapeutic purposes is an area of interest, although it predominantly remains within the realm of research rather than established clinical treatments. Being a truncated version of the full-length adrenocorticotropic hormone, ACTH (11-24) retains a core functionality related to adrenal cortex stimulation, primarily via its interaction with the melanocortin 2 receptor (MC2R). This specificity presents opportunities to explore ACTH (11-24) in therapeutic contexts, especially for conditions related to adrenal insufficiency or dysfunction. One potential therapeutic application could be in the management of conditions such as Addison's disease, characterized by insufficient production of glucocorticoids like cortisol. ACTH (11-24) might offer a more targeted approach to stimulating cortisol production without some side effects associated with broader receptor activation by the full-length hormone. Its precise receptor interaction could limit unwanted physiological responses, presenting a potentially favorable safety profile. Moreover, the peptide’s selectivity poses advantages in therapeutic design by potentially minimizing interactions with other melanocortin receptors that the full-length hormone might affect. This selectivity could allow for the development of more focused therapies that minimize side effects associated with broader receptor engagement, critical for patients requiring chronic management of adrenal-related disorders. In addition, ACTH (11-24)’s role in modulating the hypothalamic-pituitary-adrenal (HPA) axis presents another therapeutic angle, potentially offering novel ways to modulate immune responses and inflammation, given the glucocorticoid’s role in these pathways. However, transitioning ACTH (11-24) from research to clinical use involves comprehensive pharmacological studies, including pharmacokinetics and pharmacodynamics profiling to determine therapeutic indexes and dosing regimens. More importantly, clinical trials are necessary to rigorously evaluate safety, efficacy, and potential side effects in human populations, wherein the full implications of the peptide's interaction with human physiology would be thoroughly assessed. Despite these promising aspects, it's critical to recognize that research is ongoing and that any therapeutic uses of ACTH (11-24) remain experimental as of now. The peptide serves as a model in understanding hormonal pathways and precursor for designing derivatives that, after rigorous testing, might advance into therapeutic options that enhance patient outcomes in adrenal-related conditions. The development pathway for such therapies would be expected to follow robust regulatory assessments to ensure that any potential product is safe, effective, and applicable for human use.

What are the storage and handling requirements for ACTH (11-24) to ensure its stability and functionality?

Proper storage and handling of ACTH (11-24) are critical to preserving its stability and functionality in research applications. As with many peptides, maintaining an appropriate environment is essential to prevent degradation, preserve activity, and ensure accurate experimental outcomes. The primary concern regarding storage is temperature control. ACTH (11-24) should be stored at a low temperature, ideally at −20°C or lower, to assure stability over time. Freezing the peptide helps maintain its structural integrity by slowing down molecular motion and reactivity, significantly reducing the potential for degradation via hydrolysis or oxidation. It’s important to avoid repeated freeze-thaw cycles, which can lead to peptide degradation and aggregation, ultimately affecting biological activity. To circumvent this, researchers often aliquot the peptide into smaller, single-use volumes before freezing. This approach minimizes the need to thaw and refreeze the entire batch while preserving the peptide’s efficacy. After thawing, the peptide should be kept at low refrigerator temperatures (approximately 4°C) for short-term use and handled promptly to minimize exposure to room temperature, which could accelerate degradation processes. Lyophilization is another key method for enhancing peptide stability, removing moisture that might otherwise facilitate hydrolytic degradation. If the peptide comes in lyophilized form, it should reconstituted with appropriate solvents—typically sterile, buffered solutions—to restore it to an active state for experimental use. The solvent choice and its pH can significantly impact the peptide’s solubility and activity; thus, empirical determination of these solvent parameters is often a necessary step during protocol development. Beyond storage and reconstitution concerns, light exposure is another factor to manage, as some peptides are prone to photodegradation. Thus, ACTH (11-24) should be stored in light-proof containers when not in use, reducing potential photolytic reactions. Furthermore, researchers should employ good laboratory practices, ensuring all handling of the peptide is done with clean, non-reactive equipment, preferably in conditions that limit air exposure, particularly humid environments. To assist with these demands, using inert or atmosphere-controlled gloveboxes could be beneficial, especially in higher-sensitivity applications. Proper labeling, including concentration, preparation date, and expiration, is vital for maintaining an effective inventory system. Compliance with these handling protocols is necessary for achieving reproducibility and maintaining the peptide integrity throughout its intended experimental lifecycle, facilitating reliable and informative research data.