What is ACTH (1-14) C75H106N20O19S 22006-64-0, and what does it do?

ACTH (1-14), scientifically designated as C75H106N20O19S with a compound number of 22006-64-0, is a synthetic analog of a segment from the adrenocorticotropic hormone (ACTH). This particular peptide consists of the first 14 amino acids of the ACTH sequence, removing the remaining sequence that is present in the full ACTH. The principal function of ACTH in its complete form is to stimulate the adrenal glands to produce glucocorticoids such as cortisol, which play a vital role in metabolism regulation, immune response modulation, and stress adaptation. ACTH (1-14) specifically refers to the truncated version of the hormone, meaning it incorporates only the initiating part of the sequence, which was synthesized to study the effects of specific segments of ACTH independently of the full hormone.

The particular interest in ACTH (1-14) among researchers is its potential utility in understanding the biological activity of the ACTH hormone in a more nuanced way. By isolating part of the sequence, scientists can investigate how different segments of the hormone contribute differently to its overall function and physiological roles. This approach helps in understanding the differentiation in receptor activation and downstream effects that might not be apparent when observing the entire ACTH molecule. Furthermore, due to the focus on the first 14 peptides, research may delve into aspects such as receptor binding affinity, efficacy, and the potential neuropeptide influence independently, which has interesting implications for neurological research, given ACTH’s role in neural activity modulation.

The modified peptide segment offers a glimpse into peptide therapeutic potential—what smaller, more defined ACTH fragments may be capable of when it comes to receptor targeting, side effect potential, and range of action. This, over the full hormone, presents further pathways for pharmaceutical innovation endeavors as well. It can be used as a prototype for creating new drugs that might mimic or alter the effects of endogenous hormones, reflecting a growing trend in medicine focusing on peptide-based solutions. The precise implications and capabilities of ACTH (1-14) are subjects of ongoing investigation, with aims to better discern its selective activation of receptors or modulation of certain physiological pathways without the broader activity scale of full-length ACTH, offering insights that could lead to novel, more targeted therapeutic strategies.

How is ACTH (1-14) C75H106N20O19S 22006-64-0 different from full-length ACTH?

ACTH (1-14) differs significantly from its full-length counterpart, full-length ACTH (typically composed of 39 amino acids), as it comprises only the first 14 amino acids of the ACTH molecule. This truncated form is primarily used in research to understand the peptide’s functional dynamics without influence from the remainder of the hormone sequence. The complete ACTH hormone is known for inducing specific effects on the adrenal cortex, triggering different cellular responses that culminate in the production of cortisol and other glucocorticoids. However, by focusing on ACTH (1-14), researchers can pinpoint how the initial sequence contributes to these responses and whether such effects can be isolated or altered.

In terms of functional activity, full-length ACTH and ACTH (1-14) may exhibit different profiles in their ability to bind to receptors and stimulate certain biological processes. Full-length ACTH has a well-characterized role in informing the adrenal glands to synthesize and secrete glucocorticoids. The truncated peptide, on the other hand, provides a framework for dissecting the binding specificity of the amino acids that it comprises. At the level of pharmaceutical interest, understanding this specific part of ACTH opens new avenues, particularly related to receptor activation, specificity, and desensitization phenomena, which all have dramatic implications for therapeutic management.

Structurally, the two versions of ACTH exist on a continuum of function where ACTH (1-14) is the starting sequence. Structure-function studies emphasize that these shortened sequences can still retain some signaling capacity, indicating that parts of the sequences have inherent value in docking or initiating receptor interaction, although not necessarily leading to full hormonal response. Furthermore, the lack of additional residues in ACTH (1-14) simplifies the molecular makeup, thereby aiding in the potential reduction of unintended side effects or unpredictable actions that are sometimes observed with the complete sequence.

In essence, ACTH (1-14) represents a smaller, more controlled investigation piece that provides utility in foundational research. Evaluating its own distinct properties compared to full ACTH can enhance understanding of sequence segment contributions to hormone function, growth, and expansion into therapeutic lines of inquiry, enhancing the evidence-based assessment of peptide therapy and furthering developments of targeted treatment approaches.

What is the significance of the chemical composition C75H106N20O19S for ACTH (1-14)?

The chemical composition C75H106N20O19S embodies the elemental make-up of the peptide ACTH (1-14), marking crucial scientific insight into its structure and function. Each aspect of this composition plays a role in the peptide's formation, characteristics, and potential biological activity, which collectively describe the peptide's functionality in various physiological or investigative frameworks. The elements in this formula denote the specific count of each atom present in the peptide, contributing to intricate folding, the formation of active sites, and receptor interactions that define peptides and proteins.

Carbon (C), making up 75 atoms in this compound, forms the backbone of the peptide structure. It allows for the varied array of molecular interactions because of its significant versatility within organic chemistry, extending the structural complexity necessary for biological activity. Hydrogen (H) atoms, totaling 106, are pivotal for maintaining the three-dimensional structural integrity of the peptide, through bonds that create specific folding patterns stabilized by secondary structures like alpha-helices and beta-sheets.

Nitrogen (N), included with 20 atoms, is crucial for peptide bond formation, linking amino acids into the peptide chain. This bonding establishes the primary sequence of the peptide, defining the biological function through the sequence of joint residues. Oxygen (O), 19 atoms present, partakes in forming carbonyl and other groups crucial for structural stabilization, intramolecular bonding, and are essential for facilitating interactions with receptors and other proteins in biological systems.

Sulfur (S) with a single atom in the peptide composition may participate in the formation of disulfide linkages when present in residues like cysteine that occur in longer forms of the peptide, though in ACTH (1-14) it could have limited involvement in more complex disulfide bonding networks. However, it still plays a role in potential interactions with other protein interfaces, giving specificity to the peptide configuration and function.

Overall, the notation C75H106N20O19S underscores the precision involved in understanding peptide chemistry and is significant to how researchers frame experimental approaches to investigate its implications in biological systems. Each number and element denotes a careful balance that comprehensively determines peptide behavior, influencing how ACTH (1-14) interacts with biological environments, offering a glimpse into its specific potential applications in medicine and therapeutics research. Appreciating the complex interaction of these atoms provides insights into how similar peptides might be utilized or modified for enhanced biological function or therapeutic purpose.

How is ACTH (1-14) C75H106N20O19S 22006-64-0 used in research?

ACTH (1-14), identified by its specific molecular formulation C75H106N20O19S and CAS number 22006-64-0, is primarily leveraged in academic and biopharmaceutical research owing to its ability to spotlight specific mechanisms of hormonal activity. Its primary usage is to unravel the particular roles of peptide segments in broader protein function, focusing on its role in receptor interactions. By isolating this segment of the ACTH hormone, researchers can delve into investigations regarding receptor specificity, signal transduction processes, and secondary cellular responses attributable to precise amino acid sequences.

A significant area of study with ACTH (1-14) is its neuropeptide activity, where researchers inspect how truncated peptides can affect neurological processes and receptor activities. Since ACTH influences neurological functions along with its endocrine roles, ACTH (1-14) can be a model to comprehend how peptides affect synaptic transmission, neuroplasticity, and modulation of neurotransmitter release. These insights have implications for neurological research, including potential therapeutic avenues for neurodegenerative diseases, mood disorders, and cognitive function inquiries.

In endocrinological contexts, studies involving ACTH (1-14) often aim to discern specific pathways of adrenal stimulation outside of traditional cortisol production roles. This reflects on delineating peptide hormone actions beyond the full hormonal extent, examining the signalling triggered from only the initial part of the peptide sequence. By undertaking this focused examination, scientists can understand fragment-dependent activity, which might correlate to receptor profile nuances, possibly leading to innovative endocrinological interventions with minimized adverse effects.

Biochemically, the properties of ACTH (1-14) are investigated for its potential roles in protein folding, stability, receptor binding, and its efforts to discern multiple receptor modulation. Structural biology studies aim to construct models to understand how the peptide interacts at the atomic level with corticosteroid receptors and mimetic pathways. Through physical and computational simulations, the peptide can serve as a probe to decipher receptor kinetics, structural interaction potential, and perhaps alternative peptide design for improved therapeutic profiles.

Researchers might also use ACTH (1-14) within assays to establish higher efficacy treatments or inform diagnosis strategies regarding adrenal and pituitary disorders. Understanding ACTH (1-14) facilitates a more profound comprehension of adrenal response modulation, which is crucial for conditions like Addison's disease or pituitary-adrenal pathologies. By examining first-hand the peptide-mediated cellular communications, ACTH (1-14) could spotlight specific receptor targeting methods that enable heightened control and diagnostic precision in handling these challenging disorders.

What are the potential therapeutic applications of ACTH (1-14) C75H106N20O19S 22006-64-0?

While ACTH (1-14) C75H106N20O19S in its primary usage serves as a research tool, there are broader investigative inquiries into its potential therapeutic applications that result from its particular action as a truncated peptide sequence of ACTH. Therapeutic potential can be especially noted in conditions wherein control over glucocorticoid production or receptor site modulation is essential. As it functions as a segment of the more extensive ACTH hormone, ACTH (1-14) might carry distinct properties that offer unique benefits in clinical applications when dissected from the full hormone structure.

One therapeutic avenue pertains to its use in conditions associated with the central nervous system. Given ACTH's known effects on cognitive and emotional states due to its action on neural tissue, ACTH (1-14) may help in modulating these states, offering a nuanced approach to managing stress-related disorders or neurodegenerative conditions. The task is in delineating the signalling cascades attributable to the peptide’s shortened form, facilitating more targeted interventions that isolate compensatory or regulatory pathways that existing treatments don't currently address.

Endocrine disorders offer another potential area where ACTH (1-14) could play a role in modulating adrenal production of glucocorticoids. By providing selectivity towards specific receptor subtypes, it might be feasible to regulate adrenal overproduction or suppression with fewer side effects than using synthetic glucocorticoid treatments or the full hormone itself. The quest here is in refining application methods that may allow for differential patterning of hormone synthesis, aligning therapy more closely with patient symptomatology and pathophysiology.

Anti-inflammatory properties often link with glucocorticoid-modulating agents, suggesting that ACTH (1-14) might be tailored for interventions in inflammatory or immunological settings. By modulating these pathways through downstream effects related to this peptide fragment, one could explore areas such as autoimmune disease management, where tuning immune activity without broad-spectrum hormone impact is desirable.

Additionally, in dermatological research, ACTH (1-14) might provide a foundation for treatments concerning skin health and healing. Through modulation of glucocorticoid pathways, it could have applications in treating pathologies related to skin, such as chronic inflammatory diseases, certain proliferative disorders, or accelerated wound healing. A fractionated peptide's role could allow recalibration of cellular growth cycles and immunity balance, fostering healthier tissue outcomes in affected individuals.