Synonym |
Met-Enkephalin-KR |
Species |
Human |
Protein Accession |
P01210 |
Purity |
Greater than 95% |
Endotoxin Level |
Less than 1 EU/μg |
Biological Activity |
The ED50 for this effect in mouse spleen lymphocytes is typically 0.1-0.5 μM. |
Expression System |
Chemical Synthesis |
Fusion Tag |
None |
Predicted Molecular Mass |
557.64 Da |
Formulation |
Lyophilized from a 0.2 µm filtered solution in Acetonitrile and TFA |
Reconstitution |
Reconstitute in water to a concentration of 0.1-1.0 mg/ml. |
Storage & Stability |
Store at -20°C. For long term storage, store at -80°C. Once reconstituted, store at -20°C. |
FAQ
What is Met-Enkephalin-KR and how does it differ from other peptides?
Met-Enkephalin-KR is a
modified peptide with applications primarily in research settings related to neuroscience and
pharmacology. It is an analogue of met-enkephalin, a naturally occurring endogenous opioid peptide. This
modification enhances its affinity for opioid receptors, potentially allowing for more effective studies
on receptor dynamics and signaling pathways. Unlike traditional opioids, Met-Enkephalin-KR is not
intended for direct use as a therapeutic agent or in clinical settings, but rather as a research tool.
What sets Met-Enkephalin-KR apart from other peptides is its specific structure which includes the
additional lysine-arginine (KR) group. This subtle modification is crucial as it facilitates improved
binding properties and can result in prolonged biological activity within laboratory experiments. Given
its specific receptor targeting, Met-Enkephalin-KR provides a unique platform for investigating the
interactions between different opioid receptors, assisting researchers in identifying potential new
pathways for pain management and addiction treatment. Furthermore, the stability imparted by the KR
modification may allow for extended observation periods, helping in the assessment of long-term effects,
receptor desensitization, and resensitization dynamics in vitro. This makes it particularly valuable for
neuroscientists and pharmacologists seeking precise and sustained receptor engagement in their
experimental studies. In summary, Met-Enkephalin-KR represents a specialized tool designed to push the
boundaries of research into opioid receptors, differing from other peptides primarily due to its
enhanced receptor affinity and stability attributes afforded by its KR modification.
What are the
potential research applications for Met-Enkephalin-KR?
Met-Enkephalin-KR, as a specialized
research peptide, offers a broad range of potential applications in the scientific investigation of
neuronal and molecular mechanisms. Its primary research utility is in the exploration of opioid receptor
dynamics. Due to its structural specificity and modified activity profile, Met-Enkephalin-KR is employed
in studies aiming to understand how opioid receptors, especially the mu and delta subtypes, interact
with endogenous ligands. By doing so, researchers are able to dissect the molecular underpinnings of
pain modulation, providing critical insights into potential non-addictive pain relief methodologies. In
addition, Met-Enkephalin-KR plays a crucial role in studies focused on addiction. Its unique attributes
enable scientists to simulate the binding and regulatory activities of naturally occurring enkephalins,
thus offering a model for studying addiction pathways without the ethical and safety concerns associated
with in vivo testing. Through controlled in vitro experiments, researchers can study the peptide's
effects on receptor activation, desensitization, and downstream signaling, ultimately contributing to
the development of improved therapeutic strategies for addiction treatment. Moreover, Met-Enkephalin-KR
serves as a probe in cellular biology, where it is used to track signaling pathways activated by
specific receptor engagement. This helps illuminate complex cell signaling networks that are influenced
by endogenous opioids. Additional applications of this peptide include its utility in exploring
neuroinflammation and immune response modulation, as opioid receptors are expressed not only in the
central nervous system but also in various immune cells. By utilizing Met-Enkephalin-KR, scientists can
further examine how opioid-receptor interaction impacts immune functions, which is vital for developing
novel treatments for inflammatory diseases. Ultimately, Met-Enkephalin-KR's applications are diverse,
with the peptide facilitating innovative research across numerous domains within life
sciences.
How does Met-Enkephalin-KR interact with opioid receptors in research
settings?
Met-Enkephalin-KR exhibits a distinct interaction profile with opioid receptors, making
it a valuable tool in research settings. Opioid receptors, primarily mu, delta, and kappa, are part of
the G protein-coupled receptor (GPCR) family, and they mediate various physiological responses,
including pain modulation, mood regulation, and immune function. Met-Enkephalin-KR, thanks to its
specific modifications, displays selective binding affinity primarily towards the mu and delta opioid
receptors, which are of significant interest for researchers studying analgesia and addiction pathways.
The interaction of Met-Enkephalin-KR with opioid receptors begins with its binding to the receptor's
extracellular domain. The additional lysine-arginine (KR) motif on this peptide enhances its binding
capability, ensuring a stronger interaction and possibly increasing the duration of receptor activation
compared to its unmodified counterpart. This interaction can lead to a conformational change in the
receptor, triggering intracellular signaling pathways that typically involve the activation of G
proteins. Upon activation, these G proteins can influence various second messengers like cyclic AMP or
calcium ions, thus enabling researchers to observe a cascade of intracellular events prompted by
receptor engagement. Such detailed investigations allow for a better understanding of receptor
functionality and the potential development of opioid-like analgesics with reduced side effects. In
research settings, experiments often focus on receptor binding assays and functional analyses to track
the efficacy and potency of Met-Enkephalin-KR. Techniques like radioligand binding assays, coupled with
enzyme-linked immunosorbent assays (ELISAs) and phosphorylated protein tracking, are commonly used to
quantify its interaction with receptors and its downstream effects. This biochemically rigorous approach
offers a comprehensive picture of both the ligand-receptor interaction and the physiological responses
elicited by receptor signaling. Therefore, Met-Enkephalin-KR serves as a crucial probe in opioid
research, facilitating a deeper exploration of the potential therapeutic benefits and receptor-specific
actions of peptides within the opioid family.
What safety protocols should researchers consider
when working with Met-Enkephalin-KR in a lab setting?
When working with Met-Enkephalin-KR or any
research-grade peptides, it is imperative to adhere to strict safety protocols to ensure the safety of
laboratory personnel and the integrity of experimental results. Firstly, although Met-Enkephalin-KR is
not used clinically, maintaining proper handling procedures is crucial. Researchers should be trained in
the safe handling of peptides and all associated chemical substances. This includes wearing appropriate
personal protective equipment (PPE) such as gloves, lab coats, and eye protection to avoid any contact
with the skin or eyes, as peptides can sometimes act as unexpected sensitisers or irritants. It's
critical to work in a controlled environment, such as a fume hood, when dissolving or preparing peptide
solutions to prevent inhalation of any aerosolized particles. Ensuring good laboratory ventilation is
another fundamental aspect to consider, especially during processes that could release volatile
components. Accurate documentation and labeling of Met-Enkephalin-KR samples are also essential. This
helps prevent cross-contamination with other compounds and allows for the precise traceability of
peptides throughout experiments. Proper storage conditions must be adhered to, typically requiring low
temperatures to preserve stability and activity—often refrigerated or frozen depending on the specified
recommendations for the particular peptide batch. Regarding waste disposal, researchers must follow
institutional guidelines and local regulations pertaining to biological and chemical waste. Peptide
solutions and contaminated materials should be disposed of in designated biohazard containers to prevent
environmental contamination or unintentional exposure. Furthermore, before commencing any experiments
with Met-Enkephalin-KR, a comprehensive risk assessment should be conducted to identify potential
hazards and mitigate them. This includes evaluating the toxico-kinetic profiles and designing
experiments that minimize exposure levels while maximizing data yield. Overall, a conscientious approach
to lab safety protocols is imperative when dealing with research peptides like Met-Enkephalin-KR, as it
ensures both the well-being of personnel and the success of scientific endeavors.
Are there any
known limitations or challenges when using Met-Enkephalin-KR in research?
Utilizing
Met-Enkephalin-KR in research, while offering significant insights into opioid receptor dynamics, does
present certain limitations and challenges that must be acknowledged. One of the primary challenges is
ensuring the proper synthesis and stability of the peptide. As with any synthetic peptide, variations in
manufacturing processes can lead to differences in purity and activity. It is crucial for researchers to
procure Met-Enkephalin-KR from reputable suppliers and to thoroughly vet the peptide's characterization
data before use. Even small contaminants or incorrect folding could impact experiment outcomes, leading
to inconsistent or unreliable data. Another limitation lies in the translation of in vitro findings to
in vivo relevance. Studies conducted with Met-Enkephalin-KR are often confined to cellular or isolated
receptor models, which do not fully replicate the complex physiological environment of living organisms.
Therefore, caution must be taken when extrapolating results from in vitro systems to whole-organism
scenarios. While Met-Enkephalin-KR helps simulate specific receptor interactions, biologically relevant
responses also involve factors such as cross-receptor communication, regulatory feedback mechanisms, and
endogenous peptide concentrations that are not completely represented in isolated systems. Researchers
should be wary of interpreting such findings without considering the biological complexity that exists
in vivo. There is also the inherent challenge of receptor specificity and downstream signaling biases.
Although Met-Enkephalin-KR is designed to target mu and delta opioid receptors, off-target effects
cannot be entirely ruled out. These effects might lead to atypical or unexpected cellular responses,
which can convolute data interpretation. Therefore, rigorous controls and receptor antagonists are often
employed to validate the specificity of observed outcomes accurately. Additionally, the peptide's
prolonged receptor engagement may lead to phenomena such as receptor desensitization or internalization,
which, though interesting from a research perspective, could complicate the interpretation of long-term
signaling consequences. Recognizing and addressing these challenges ensures that the findings gained
from research with Met-Enkephalin-KR are robust and meaningful.
Can Met-Enkephalin-KR be used as
a model for studying pain management?
Met-Enkephalin-KR can indeed serve as a valuable model for
studying pain management due to its interactions with opioid receptors, which are integral to the body’s
natural pain modulation system. The peptide mimics the behavior of endogenous enkephalins, binding to
opioids receptors with high affinity and specificity, which is crucial in delineating the pathways
through which our bodies process pain stimuli. By using Met-Enkephalin-KR, researchers are able to
investigate how opioid receptors can be modulated to achieve analgesic effects without invoking the
adverse side effects commonly associated with traditional opioid medications. One of the significant
aspects of using Met-Enkephalin-KR in pain research is its potential to illuminate the mu and delta
opioid receptor roles in pain pathways. Studies employing this peptide can help identify specific
receptor subtypes or receptor complexes that are particularly effective at modulating pain responses.
Understanding these interactions at a molecular level is fundamental in designing new classes of
analgesics that aim to enhance or mimic enkephalin action without the addiction risk associated with
currently available opioid drugs. Furthermore, Met-Enkephalin-KR's stability and prolonged biological
activity make it suitable for studying chronic pain conditions. Researchers can leverage its extended
interaction with opioid receptors to ascertain the mechanisms underlying acute pain progression to
chronic pain states. By examining these transitional mechanisms in controlled environments, scientists
hope to find novel biomarkers or therapeutic targets for early intervention in chronic pain conditions.
Moreover, utilizing Met-Enkephalin-KR in pain research may also assist in the identification of
non-opioid receptor targets for pain relief. The peptide's involvement in downstream intracellular
signaling cascades offers additional avenues to explore peripheral mechanisms of pain modulation. Such
insights could broaden our understanding of pain physiology and lead to the discovery of alternative
approaches to pain management that do not solely depend on central nervous system interventions.
What techniques are commonly used to study Met-Enkephalin-KR interactions?
When studying
the interactions and effects of Met-Enkephalin-KR, researchers employ a variety of sophisticated
laboratory techniques to ensure accurate and detailed data collection. One such technique is receptor
binding assays, which are fundamental for determining the binding affinity of Met-Enkephalin-KR to
specific opioid receptors. This process typically involves the use of radio-labelled peptides or other
tags that can be quantitatively measured to ascertain how effectively the peptide binds to the mu and
delta opioid receptors in competitive or saturation binding studies. These assays provide crucial
insights into the peptide's affinity and potential efficacy. Another prevalent method is cellular
assays, which can include a variety of configurations such as the use of isolated receptor systems or
whole-cell models. These assays allow researchers to observe the downstream effects of receptor
activation by Met-Enkephalin-KR, measuring aspects like changes in cyclic AMP levels, calcium flux, or
other second messenger systems using techniques such as FRET (Förster resonance energy transfer) or
luminescent/fluorescent based systems. Electrophysiological approaches, such as patch-clamp techniques,
can be employed to assess the functional consequences of Met-Enkephalin-KR receptor interactions in
neuronal cells. This allows scientists to explore how this peptide influences ion channel activity and
neurotransmitter release, which are critical aspects of understanding its potential analgesic effects.
Furthermore, mass spectrometry and liquid chromatography are used to analyze the peptide's stability and
biotransformation within experimental environments. Such analytical techniques help to identify any
metabolic products or degradation pathways of Met-Enkephalin-KR in vitro or in simulated biological
conditions. Imaging techniques like confocal or fluorescence microscopy can be applied to visualize
Met-Enkephalin-KR's localization and distribution within cells, providing spatial insights into its
interaction with opioid receptors. These methodologies are often coupled with co-labelled receptors or
downstream signaling proteins to offer a holistic view of cellular activities post-interaction.
Collectively, these diverse techniques ensure a comprehensive examination of Met-Enkephalin-KR, from
receptor binding dynamics to the cellular and physiological consequences of such interactions,
ultimately facilitating a deeper understanding of its role in research contexts.