Synonym |
β-Neoendorphin, Prodynorphin (175-183) (human, p product) |
Species |
Human |
Protein Accession |
P01210 |
Purity |
> 95% |
Endotoxin Level |
< 1.0 EU per μg |
Biological Activity |
N/A |
Expression System |
Chemical Synthesis |
Fusion Tag |
None |
Predicted Molecular Mass |
973.1 Da |
Formulation |
Supplied as a lyophilized powder |
Reconstitution |
Reconstitute in distilled water |
Storage & Stability |
Store at -20°C. For long-term storage, store at -80°C |
FAQ
What is β-Neoendorphin, Prodynorphin (175-183) (human, p), and how does it function in the
body?
β-Neoendorphin, Prodynorphin (175-183) (human, p), is a neuropeptide that belongs to the
class of endogenous opioid peptides. These peptides are naturally occurring substances in the human body
that have powerful effects on the central nervous system and are involved in modulating pain, reward,
and various other physiological processes. This particular peptide is derived from the larger precursor
protein, prodynorphin, which is present in several regions of the brain, including the hypothalamus and
the pituitary gland. Once synthesized, prodynorphin is cleaved into smaller active peptides like
β-Neoendorphin.
The primary function of β-Neoendorphin is to bind to opioid receptors in the
brain, particularly the kappa opioid receptors (KOR). These receptors are part of the opioid receptor
family, which also includes mu and delta opioid receptors. Each type of opioid receptor has distinct
functional roles and distribution patterns within the brain and peripheral tissues. Binding of
β-Neoendorphin to kappa receptors activates signaling pathways that can lead to various effects such as
analgesia, modulation of stress responses, and influence on mood.
Furthermore, the interaction
of β-Neoendorphin with the kappa receptors is associated with the modulation of the perception of pain,
making it potentially valuable in understanding mechanisms of pain relief and management. It is also
implicated in mood regulation and has been studied in the context of depression and anxiety disorders.
The peptide's role in the reward and addiction pathways has been of particular interest, as kappa
receptor activation is thought to counteract some of the rewarding effects mediated by mu opioid
receptors, thus providing insights into addiction mechanisms and potential therapeutic
interventions.
In addition to the central nervous system effects, β-Neoendorphin's influence is
broader, including potential effects on the neuroendocrine system. Studies suggest that it may regulate
hormonal release, impacting functions such as stress hormone (cortisol) secretion, and it may play a
role in reproductive biology due to its effect on the hypothalamic-pituitary-gonadal axis. Overall,
β-Neoendorphin represents a critical component of the body's neuropeptide network, and ongoing research
continues to uncover its diverse roles and therapeutic potential.
What are the potential
therapeutic applications of β-Neoendorphin, Prodynorphin (175-183) (human, p)?
The potential
therapeutic applications of β-Neoendorphin, Prodynorphin (175-183) (human, p) are indeed promising,
reflecting the broader therapeutic possibilities linked to the modulation of the opioid system. One of
the most well-studied applications is in the realm of pain management. The peptide’s ability to interact
with kappa opioid receptors presents a significant opportunity for developing pain relief medications.
This is of particular interest because traditional opioids that target mu receptors often come with
issues of addiction and tolerance. By targeting kappa receptors, β-Neoendorphin may offer an alternative
route to analgesia that potentially circumvents the addictive properties of conventional opioids.
Moreover, its interaction with kappa receptors opens avenues for its use in treating mood
disorders such as depression and anxiety. Kappa receptor agonists have been implicated in modulating
dysphoric and anxiety-related responses, and β-Neoendorphin's therapeutic benefit could arise from such
mechanisms. Recent studies have explored the role of kappa opioid receptor modulation as an
antidepressant strategy, especially for patients resistant to traditional antidepressants. The exact
pathways and cellular mechanisms remain an area of active research; however, the potential for new
classes of antidepressant drugs inspired by β-Neoendorphin's activity is a subject of great
interest.
Another exciting therapeutic avenue is in the treatment of addiction. Substance use
disorders often revolve around the reward system mediated by mu and delta opioid receptors.
β-Neoendorphin's inhibitory role on reward pathways via kappa receptor activation provides a potential
mechanism to reduce cravings and withdrawal symptoms, offering a novel strategy for addiction therapy.
Beyond these central nervous system implications, β-Neoendorphin may confer benefits in stress
management and neuroendocrine disorders. It may help regulate cortisol levels and influence the brain's
stress response, offering a therapeutic edge in stress-related conditions.
Additionally, there
are potential implications in reproductive health, given its regulatory effect on hormone release from
the pituitary gland. This opens possibilities for addressing certain types of hormonal imbalances or
dysfunctions. The versatility of β-Neoendorphin in interacting with various physiological systems makes
it a candidate for diverse therapeutic strategies. However, translating these potentials into clinical
applications will require more extensive research and clinical trials to fully understand its
mechanisms, efficacy, and safety in humans.
How is β-Neoendorphin, Prodynorphin (175-183) (human,
p) synthesized, and is this process scalable for research purposes?
β-Neoendorphin, Prodynorphin
(175-183) (human, p) is synthesized through a process that involves peptide bond formation, which
requires a solid understanding of organic chemistry and peptide synthesis techniques. In laboratories,
β-Neoendorphin is typically synthesized using solid-phase peptide synthesis (SPPS), a widely employed
method for peptide production due to its efficiency and ability to produce longer peptides accurately.
SPPS operates by anchoring the C-terminal of the first amino acid to an insoluble resin, allowing for
the stepwise addition of protected amino acids to build the peptide chain.
Each amino acid
addition is carefully controlled to ensure specificity and accuracy, often using automated synthesizers
that facilitate the coupling reactions and deprotection steps. Following the assembly of the peptide
chain, the product undergoes cleavage from the resin, along with the removal of protecting groups from
the side chains, resulting in a crude peptide that is further purified using high-performance liquid
chromatography (HPLC). This method ensures the final product is of high purity, a necessity for any
biological research application, to avoid confounding results or unintended biological responses.
The synthesis process, while intricate, is relatively scalable, making it appropriate for
producing the quantities needed for research studies. The key to scalability lies in the optimization of
the synthesis conditions and the efficiency of the purification process. Advances in peptide
synthesizers have made it possible to increase yield and purity, allowing researchers to obtain
sufficient quantities of β-Neoendorphin for in vitro and in vivo studies. Additionally, factors like
cost and time efficiency are vital, especially in the context of academic and pharmaceutical research
where resource availability can be limited.
On an industrial scale, peptide production can be
adjusted to meet higher demand by altering reactor sizes and adapting purification techniques to handle
larger volumes. This scalability makes β-Neoendorphin, Prodynorphin (175-183) not only accessible but
also feasible for widespread research exploration. However, successful synthesis, especially when
scaling up, requires maintaining strict quality controls to adhere to regulatory standards if the
peptide is intended for therapeutic research and potential clinical applications. As research advances,
continuous improvements in peptide synthesis and purification methodologies bode well for the broader
application of β-Neoendorphin in scientific and medical endeavors.
What challenges exist in the
research and application of β-Neoendorphin, Prodynorphin (175-183) (human, p)?
Research and
application in the domain of β-Neoendorphin, Prodynorphin (175-183) (human, p) face a myriad of
challenges inherent to the exploration of complex biological peptides. One of the primary challenges is
the difficulty associated with elucidating the precise mechanisms of action of β-Neoendorphin within the
human body. While we know that it binds to kappa opioid receptors, the downstream effects of this
binding, including specific signaling pathways engaged and cellular responses elicited, require further
clarification. Understanding these interactions at a granular level is crucial because opioid systems
are highly complex and multifaceted, often involving a network of compensation pathways and interactions
with other neurotransmitter systems, such as dopamine and serotonin.
Another significant
challenge lies in the potential side effects that may arise from modulating the kappa opioid receptors,
which are known to cause dysphoria and hallucinations in some contexts. This necessitates a careful
balance in any therapeutic application to mitigate adverse effects while capitalizing on beneficial
outcomes like pain relief or antidepressant effects. Developing compounds or modifying β-Neoendorphin to
enhance therapeutic effects while minimizing side effects requires innovative approaches and thorough
pharmacological studies.
Ethical considerations and regulatory hurdles represent additional
layers of complexity, particularly when transitioning from benchtop research to clinical trials.
Rigorous safety and efficacy evaluations are mandated, often requiring comprehensive preclinical studies
in relevant animal models before human trials can be contemplated. These stringent requirements are
necessary to ensure patient safety but can significantly delay the development and application
processes.
Moreover, β-Neoendorphin research contends with technical challenges linked to peptide
stability and bioavailability. Peptides are often susceptible to rapid degradation in the
gastrointestinal tract and bloodstream, posing a challenge for oral administration. Research into
protective formulations and alternative delivery methods, such as intranasal or transdermal systems, is
ongoing but requires substantial development to overcome these barriers effectively.
Intellectual
property issues and competitive research landscapes can also pose challenges. Secure patents and
collaborations can be essential to advance research but may introduce complications in terms of research
freedom and cost considerations. Nevertheless, continued interdisciplinary collaboration, encompassing
chemistry, pharmacology, and clinical medicine, holds the key to addressing these challenges. Despite
these hurdles, the scientific and therapeutic potential of β-Neoendorphin propels ongoing research
efforts, as overcoming these challenges could pave the way for innovative treatments in pain, mood
disorders, and addiction.
How does β-Neoendorphin, Prodynorphin (175-183) (human, p) differ from
other opioids, and why is it important?
β-Neoendorphin, Prodynorphin (175-183) (human, p),
distinctively stands out from traditional opioids due to its unique interaction with the kappa opioid
receptors, as opposed to the mu receptors typically targeted by most opioid drugs like morphine and
oxycodone. The importance of this difference lies in the potential for developing therapeutic
interventions that not only offer pain relief but also minimize the risks associated with opioid
consumption, such as addiction and tolerance. Traditional opioids are highly effective at reducing pain
due to their action on the mu receptors but are notorious for their ability to cause euphoria, leading
to a risk of misuse and the development of dependence and addiction.
In contrast,
β-Neoendorphin’s selective affinity for kappa receptors positions it differently within the realm of
opioid peptides. Kappa receptor agonists traditionally induce fewer euphoria-related effects, which
might limit their abuse potential. However, activation of kappa receptors can sometimes result in
dysphoria or anxiety, side effects that are not typically observed with mu receptor activation.
Therefore, understanding and moderating these effects are essential in leveraging β-Neoendorphin’s
potential clinical benefits.
The differentiation extends beyond analgesia to encompass
psychological and emotional outcomes. Kappa opioid receptors play a substantial role in stress response
and emotional regulation, suggesting that β-Neoendorphin can impact mood disorders differently from
other opioids. It offers an intrigue in addressing conditions like depression and anxiety, especially
since mu opioids, often worsen such disorders over time. This peptide's mechanism provides researchers
with insights into distinct pathways of mood regulation alternatives to the usually explored mu
receptor-mediated pathways. Furthermore, β-Neoendorphin's role in the regulation of stress hormones like
cortisol diversifies its impact beyond central nervous system effects to include potential influences on
the neuroendocrine system, differing starkly in action compared to mu-selective
agents.
Understanding β-Neoendorphin's differentiated interaction is crucial for developing a
nuanced approach to a host of conditions. As the opioid crisis continues to claim lives globally,
research into alternatives like β-Neoendorphin gains urgency. If strategies can be developed to utilize
its benefits while mitigating adverse effects, β-Neoendorphin could offer a new therapeutic avenue that
leverages opioid system modulation without succumbing to the pitfalls typical of traditional opioids.
Enhanced knowledge of β-Neoendorphin and its unique receptor interactions continues to be pivotal for
innovation across pain management, mental health treatment, and neuroendocrine disorders.