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.