Taiy Chemical
β-Endorphin (6-31) (human)
Synonym Leu-enkephalin
Species Human
Protein Accession P01210
Purity Greater than 98%
Endotoxin Level Less than 1 EU/ug
Biological Activity Not specified
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass 3497.8 Da
Formulation Lyophilized from a 0.2 μm filtered solution of 20% acetonitrile and 0.1% TFA
Reconstitution It is recommended to reconstitute the lyophilized β-Endorphin (6-31) (human) in sterile 18 MΩ-cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.
Storage & Stability Lyophilized β-Endorphin (6-31) (human) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution, the peptide should be stored at 4°C between 2-7 days and for future use below -18°C.
FAQ
What is β-Endorphin (6-31) (human) and how does it work in the body?

β-Endorphin (6-31) (human) is a modified peptide fragment originating from the larger endogenous peptide, β-endorphin. The full β-endorphin is a well-studied opioid peptide, produced primarily in the pituitary gland, and is known for its significant role in pain modulation and producing feelings of euphoria. The importance of these peptides in the endogenous opioid system underscores their utility in neurophysiological processes, which prominently include pain modulation, mood regulation, and stress response.

β-Endorphin (6-31) specifically is a fragment meaning it does not exhibit all the characteristics of the full-length peptide. Nonetheless, fragments can maintain some biological activities or exhibit new properties altogether. In the case of β-Endorphin (6-31), it retains some analgesic properties, though possibly to a lesser extent compared to the whole molecule, due to its truncated nature which affects receptor binding and function. This peptide operates through binding to and activating opioid receptors, primarily the mu-opioid receptor, which is critical in modulating the perception of pain and stress.

The human body’s use of β-endorphin represents a natural mechanism to cope with pain and stress. By understanding the specific activities of short fragments like β-Endorphin (6-31), researchers aim to delineate the pathways and mechanisms in which these peptides can be therapeutically utilized while potentially minimizing addictive side effects that are often associated with stronger full-length endorphins or exogenous opioids. The utility of β-Endorphin (6-31) lies in its potential as an auxiliary peptide, paving the way for alternative strategies in managing pain and mood disorders. Fragment-based approaches are often a pursuit in therapeutics due to the hypothesis of reduced side effects while preserving beneficial properties.

What are the potential applications of β-Endorphin (6-31) (human) in modern medicine?

The potential applications of β-Endorphin (6-31) in medicine are rooted in its relationship to the body’s natural pain-relief and mood-regulating opioid system. The principal areas of exploration include pain management, treatment of mood disorders, and perhaps even as adjunctive therapy in broader stress-response systems. As with full-length β-endorphin, its fragment may play a role in providing analgesia, which is relief from pain. This avenue is particularly attractive given the worldwide need for better pain management strategies that do not rely heavily on traditional opioid therapies, which can be highly addictive and prone to abuse.

Further exploring β-Endorphin (6-31) opens up its potential utility in treating mood disorders, such as depression and anxiety, which are often linked to dysregulation in β-endorphin levels and other neurotransmitter systems. Since endorphins contribute to feelings of happiness and well-being, understanding and leveraging these systems could unlock new treatments that are less reliant on conventional medications and their associated side effects. Additionally, β-Endorphin (6-31) might intersect with conditions involving dysregulation of stress responses, possibly offering benefits in chronic stress management.

The hope is that understanding and application of such peptides could extend beyond symptomatic pain and mood relief, potentially influencing the physiological and psychological aspects of diseases, considering the interconnected nature of stress, mood, and pain pathways in pathological conditions. Experimentation with β-Endorphin (6-31) peptides may yield new insights into holistic treatment approaches that target multiple layers of pathophysiology. The continued study into human β-Endorphin (6-31) molecules aims to help craft targeted solutions in clinical settings that maximize therapeutic benefits while minimizing usual vulnerabilities associated with stronger opioid applications.

What distinguishes β-Endorphin (6-31) (human) from its full-length counterpart?

What distinguishes β-Endorphin (6-31) from its full-length counterpart primarily lies in its composition and specific functional characteristics. β-Endorphin itself is a 31-amino-acid peptide, part of the endogenous opioid family, whose full structural program interacts robustly with opioid receptors like the mu, delta, and kappa receptors, eliciting potent analgesic and euphoric responses. Full-length β-endorphin's actions are extensive, covering modulation of pain perception, immune responses, and even hormonal releases, heavily influencing how the body reacts to stress and pain.

By contrast, β-Endorphin (6-31) is a fragment derived from the full peptide, encompassing a specific shorter chain that may or may not include all the active sites needed to fully engage each receptor identically. For instance, while it retains ability to bind opioid receptors, the truncated nature potentially alters its binding dynamics. This could mean different efficacy and functional outcomes, typically suggesting β-Endorphin (6-31) might provide limited or finely tuned engagement when compared to the full peptide, allowing for more specific applications or reduced affinity which could translate into fewer side effects in certain therapeutic contexts.

The interest in these sorts of peptide fragments is grounded in their ability to achieve desired outcomes without overstimulating receptors, which often lead to tolerance and addiction in opioid usage. β-Endorphin (6-31) may hold the potential to act favorably in systems where complete receptor activation by the full peptide is unnecessary or even detrimental. Essentially, engineering or isolating such fragments reflects a precision-based approach in drug development—one where the goal is to curve the benefits of the opioid system towards non-addictive, well-tolerated methodologies for managing stress, pain, emotional balance, and beyond.

How is research currently approaching the study of β-Endorphin (6-31) in human health care?

Research into β-Endorphin (6-31) is multifaceted, intertwining fields such as neurobiology, pharmacology, and clinical medicine. The studies focus on understanding how this peptide fragment interacts with opioid receptors, with special attention to its binding specificity, efficacy in inducing analgesic effects, and its overall pharmacokinetics within the human body. Given its potential role in analgesia without the potent addictive risks of full opioids, one approach is highlighting its performance in controlled experimental settings, identifying how it can mitigate pain under various conditions, from acute scenarios to chronic pain models. This basic understanding forms the bedrock for informed application and dosage frameworks which are critical in medical interventions.

Additionally, researchers aim to elucidate the neurological pathways that β-Endorphin (6-31) impacts. By employing advanced imaging and molecular techniques, scientists can observe changes at the receptor and neural circuitry levels when the fragment is administered. This helps in understanding not only its immediate biological effects but also long-term implications, such as changes in receptor sensitivity or neural plasticity.

Furthermore, clinical research is concerned with safety profiling and therapeutic potential, often established by thorough preclinical assessments in animal studies before transitioning to human trials. These clinical studies focus on differentiating its effects compared to traditional treatments, evaluating outcomes such as efficacy in pain relief, mood stabilization, and stress management, and carefully monitoring any potential side effects in human populations.

The accumulating data offers promising implications not only in designing better therapeutic regimens but also in crafting more refined questions about endogenous peptide fragments within larger physiological systems. By understanding β-Endorphin (6-31) interactions at molecular and systemic levels, researchers contribute to a paradigm shift in how we view peptide applications as potent, but potentially safer alternatives or adjuncts to classical synthetic pharmaceuticals.

Is β-Endorphin (6-31) (human) safe for therapeutic use in humans?

The safety of using β-Endorphin (6-31) in humans as a therapeutic agent is yet to be firmly established through extensive clinical trials, which remain essential to understanding its profile comprehensively. Initial studies must ensure that the peptide fragment does not exhibit unexpected toxicity or adverse reactions when administered within therapeutic boundary conditions. Safety profiling generally constitutes a significant aspect of both early and progressive phases of drug trials.

Initial preclinical findings typically involve animal studies, helping scientists predict the peptide's safety in humans by assessing pharmacokinetics, pharmacodynamics, and any toxicological concerns. These models aim to simulate human physiological conditions, including potential interactions with other medications and cross-reactivity with biomolecules within the human body. However, scientific understanding derived from animal models always requires validation through rigorously monitored human trials.

These human trials usually start with phase I clinical trials, focusing on safety aspects in small groups of healthy volunteers, progressively advancing to phase II and III trials that assess efficacy in broader patient populations with the condition the peptide aims to treat. Researchers vigilantly monitor side effects, dosing intervals, and therapeutic ceilings to ensure the utmost effectiveness while minimizing risks.

The dynamic between safety and efficacy often dictates the viability of a peptide like β-Endorphin (6-31) for widespread use in therapeutic regimens. Even with a potentially favorable safety profile from preliminary investigations, ongoing research will focus on long-term safety outcomes, the development of tolerance, or the antigenic potential that could limit its use. As clinical data matures, β-Endorphin (6-31) may emerge as a commendably safe, non-addictive alternative for various conditions, but until comprehensive phase III data are available, recommending it conclusively would be premature.

What are the challenges researchers face in developing β-Endorphin (6-31) as a treatment option?

Developing β-Endorphin (6-31) as a viable treatment option entails multiple challenges spanning scientific, regulatory, and logistical dimensions. The primary scientific challenge is understanding the intricacies of its interaction with opioid receptors and its resultant pharmacological effects. The marked variation in receptor dynamics or unexpected pseudo side effects require extensive research to decode. The challenge is not merely synthesizing the peptide but appreciating its place within broader neurochemical and systemic frameworks which dictate human health and disease progression.

Furthermore, establishing clear mechanisms of action that justify its suitability over existing treatments necessitates rigorous experimental validation. The treatment’s selective targeting without fully occupying or downregulating opioid receptors is a formidable challenge, demanding a precise balance in achieving desired therapeutic outcomes without undermining receptor functionality or instigating dependency.

From a regulatory perspective, peptide fragments must undergo comprehensive safety and efficacy evaluations not only to meet but also to exceed standards applied to traditional small-molecule drugs. Regulatory bodies such as the FDA or EMA require exhaustive datasets for approval, ensuring new treatments do not inherit or propagate adverse patterns known in larger opioid peptides.

Logistically, one significant hurdle concerns manufacturing and formulation – specifically, developing stable and reliable production methods that guarantee purity, consistency, and scalability. Additionally, the creation of stable formulations that ensure the peptide remains efficacious and non-degrading across various conditions presents further obstacles.

Clinical trials themselves pose considerable challenges; recruiting suitable patient groups, adhering to ethical guidelines, maintaining blinding and randomization in trials, and securing funding often present substantial barriers to advancing development. Finally, once a treatment enters the market, the incorporation into healthcare practices involves educational efforts to inform practitioners on the integration of such novel therapies along with patient acceptance and compliance, which cannot be underestimated in assessing a new drug’s impact and integration potential.
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