Synonym |
BK(1-3) |
Species |
Human |
Protein Accession |
P01024 |
Purity |
Greater than 95% |
Endotoxin Level |
Less than 1 EU/µg |
Biological Activity |
Not specified |
Expression System |
Chemical synthesis |
Fusion Tag |
None |
Predicted Molecular Mass |
340.39 Da |
Formulation |
Lyophilized |
Reconstitution |
Reconstitute in H2O to a concentration of 0.1-1.0 mg/ml. |
Storage & Stability |
Store at -20°C. Stable for 12 months from the date of receipt. |
FAQ
What is Bradykinin (1-3) and how does it function within the human body?
Bradykinin (1-3) is a
truncated peptide fragment derived from bradykinin, a physiologically active peptide that is part of the
kinin-kallikrein system. Bradykinin (1-3) specifically consists of the first three amino acids of
bradykinin and is among several metabolites resulting from the breakdown of bradykinin in the body.
Understanding the function of Bradykinin (1-3) involves first recognizing the role of its
precursor, bradykinin. Bradykinin is a powerful vasodilator, meaning that it plays a critical role in
the regulation of blood pressure by causing blood vessels to expand. This peptide works by binding to
receptors on the surface of endothelial cells lining the blood vessels, stimulating the release of
endothelium-derived relaxing factors such as nitric oxide and prostacyclin. These factors, in turn, lead
to smooth muscle relaxation and an increase in blood flow. Bradykinin's influence on vessel dilation
explains its involvement in physiological responses such as inflammation and pain, since increased blood
flow and reduced vascular resistance facilitate the influx of immune cells to sites of injury or
infection.
Bradykinin (1-3), although a truncated fragment, still retains some activity
associated with its parent molecule. While it may not exhibit the full vasodilatory effects of
bradykinin because it lacks the complete structure to fully engage the bradykinin B2 receptors,
Bradykinin (1-3) can still be of physiological significance, possibly in modulating the effects of
bradykinin or interacting with other molecular pathways. For instance, it might play a role in
modulating inflammation and other cellular processes by interacting with enzymes or acting as a
competitive inhibitor for full-length bradykinin degradation, thus indirectly influencing bradykinin's
effects.
Understanding its more nuanced roles within the body requires further research,
particularly focusing on its interactions with receptors and enzymes, or its potential signaling roles,
which remain less characterized. Bradykinin (1-3) could have implications in pharmacological research,
especially for conditions related to high blood pressure, chronic inflammatory diseases, or pain
management. As such, its function continues to be a subject of scientific investigation, with potential
implications for developing therapeutic interventions leveraging its physiological pathways.
What
potential therapeutic applications might Bradykinin (1-3) have in medicine?
The potential
therapeutic applications of Bradykinin (1-3) in medicine are an area of active research and interest due
to its origin as a fragment of bradykinin, a peptide known for its role in modulating vascular tone and
inflammatory processes. The therapeutic possibilities hinge on understanding both its direct
interactions in the body and its indirect effects as part of the kinin-kallikrein system, which is
implicated in several pathological states such as cardiovascular diseases, inflammatory conditions, and
pain.
One of the potential applications for Bradykinin (1-3) lies in the realm of cardiovascular
health. Bradykinin is known to be a potent vasodilator, and while the fragment (1-3) may not replicate
this effect, its study could pave the way for the development of compounds that modulate vascular
responses in a controlled manner. Developing therapeutic agents that influence the kinin-kallikrein
system, of which Bradykinin (1-3) is a part, holds promise for managing blood pressure and improving
cardiac function, especially in cases of hypertension or heart failure.
In the context of
inflammatory diseases, Bradykinin (1-3) could offer new insights into managing conditions characterized
by chronic inflammation, such as arthritis or certain autoimmune diseases. The fragment may influence
the pathways associated with inflammation, potentially leading to the development of treatments that can
alleviate symptoms by reducing inflammatory cytokine production or modulating immune cell activity.
Further exploration of its interactions with enzymes and receptors involved in inflammation can also
identify targets for novel anti-inflammatory drugs.
Pain management is another area where
Bradykinin (1-3) could be of therapeutic relevance. Bradykinin itself is involved in the sensation of
pain by interacting with sensory neurons and promoting pain signal transmission. An understanding of how
its metabolites, including Bradykinin (1-3), impact these pathways may uncover new analgesic targets,
potentially leading to treatments that alleviate pain by altering bradykinin metabolism or receptor
activity.
Furthermore, this peptide may find application in regenerative medicine. The interplay
of the kinin system in tissue repair processes is being evaluated, and manipulating its components like
Bradykinin (1-3) might accelerate healing or improve outcomes in wounds or post-operative
recovery.
Although promising, the therapeutic development of Bradykinin (1-3) requires extensive
clinical research to determine its efficacy, safety profile, and mechanism of action within human
physiology. Understanding how it interacts with other biological pathways and what effects it exerts at
different concentrations will be paramount in harnessing its full potential in therapeutic
settings.
How does Bradykinin (1-3) compare to other segments of the bradykinin peptide in terms
of activity?
Bradykinin (1-3) represents a specific fragment of the broader bradykinin peptide,
consisting only of the first three amino acids. The complete bradykinin peptide is a nonapeptide,
meaning it comprises nine amino acids, each contributing to its overall activity, and influence on blood
vessels, inflammation, and pain pathways. To understand how Bradykinin (1-3) compares in terms of
activity to other segments, one must consider the structural and functional contributions of different
peptide portions.
The full sequence of bradykinin is responsible for its strong vasodilatory and
inflammatory effects. It primarily acts through interaction with the bradykinin B2 receptor, leading to
downstream cellular events that cause relaxation of vascular smooth muscle and increased permeability of
blood vessels, pivotal in inflammatory responses. Other fragments of bradykinin, resulting from
enzymatic cleavage, also exhibit distinct activities but are usually seen as less potent individually
compared to the intact peptide.
Bradykinin (1-3), as a truncated segment, does not possess the
necessary structure to effectively engage bradykinin receptors to the same extent as bradykinin itself.
However, this does not imply it is inactive. The activity of Bradykinin (1-3) may lie in subtler
biochemical interactions rather than the direct receptor-mediated actions associated with the full
peptide. For example, it might have a regulatory role, modulating enzyme activity that influences the
turnover or action of bradykinin or other kinins. This type of activity can prevent or enhance the
formation of active peptides, thereby altering physiological responses indirectly.
Comparatively,
other bradykinin fragments might retain different functions, such as antagonistic effects to mitigate
overactivity of the kinin system or serving as substrates for enzymes that degrade active peptides. Each
fragment has been subject to varying degrees of research, with some fragments showing potential for
specific modulation of inflammatory pathways or offering analgesic potentials.
In terms of
therapeutic development, the unique biochemical environment and condition-specific response profiles of
these fragments, including Bradykinin (1-3), reveal a domain ripe for targeted drug design. There is
considerable interest in understanding these distinctions because they could herald the development of
new drugs that specifically leverage the nuanced modulatory roles of bradykinin fragments. Clinical
research into these differences is critical for elucidating the full potential of kinin system
modulation as a therapeutic strategy.
What research is being conducted on Bradykinin (1-3) and
its implications for future therapies?
Research on Bradykinin (1-3) is part of a broader
investigation into the kinin-kallikrein system's extensive biological activities and its potential
therapeutic implications. The kinin system's complexity, with its multiple peptides and interacting
enzymes, remains an intriguing area for medical research due to its role in cardiovascular function,
inflammation, pain, and possibly tissue regeneration. Bradykinin (1-3), as a fragment resulting from the
breakdown of bradykinin, is under study for its biological activity and potential influence on these
systems.
Ongoing research efforts are particularly focused on understanding the peptide's
physiological and pathophysiological roles. Scientists are delving into characterizing the receptors and
signaling pathways that Bradykinin (1-3) may modulate or interact with. Such studies are essential for
identifying its mechanistic roles, which could lead the way towards novel therapeutic strategies for
diseases where dysregulation of the kinin system is evident. By delineating how this fragment affects
cellular processes, researchers aim to not only develop therapies that leverage its direct actions but
also those that control the overall kinin pathway's activity in states of disease.
Moreover,
research is being conducted on its potential cardiovascular implications, given the kinin system's known
effects on blood pressure regulation and vascular health. Bradykinin (1-3) is being explored for any
indirect roles it may play in modulating blood pressure or contributing to protective cardiovascular
mechanisms under pathological conditions such as hypertension or heart failure. These studies are often
preclinical, involving animal models and in vitro experiments to assess the peptide's influence on
vascular cells or hemodynamic parameters.
The fragment is also being investigated in cellular and
molecular contexts of inflammation, seeking to unravel if it can modulate cytokine release or interact
with immune cell signaling pathways. By understanding these interactions, there is potential to discover
new anti-inflammatory therapies that could be more precisely targeted, thereby reducing side effects
associated with broader spectrum anti-inflammatory drugs.
Another fascinating aspect of research
is the hypothesis that Bradykinin (1-3) may possess unknown regenerative properties or influence tissue
repair. This is fueling studies into whether this fragment, possibly in conjunction with other system
components, could play roles in wound healing or in restoring function post-injury.
As research
continues, including advanced studies such as clinical trials, the therapeutic landscape for Bradykinin
(1-3) is anticipated to expand. These explorations will help determine its safety, efficacy, and
potential applications, setting the stage for its inclusion in future treatment paradigms for a variety
of conditions. Each discovery paves the way for potentially innovative medical interventions that could
redefine current strategies for managing complex diseases involving inflammation, vascular integrity,
and beyond.
Why is the study of Bradykinin (1-3) important for understanding the kinin-kallikrein
system?
The study of Bradykinin (1-3) holds significant importance in the broader context of
understanding the kinin-kallikrein system due to its role as a metabolite of bradykinin, a key peptide
within this system. The kinin-kallikrein system involves a cascade of enzymatic reactions that produce
kinins, which are peptides responsible for various physiological functions such as vasodilation,
modulation of blood pressure, pain sensation, and inflammation. Research into Bradykinin (1-3),
therefore, offers insights into the complex regulation and modulation of this essential biochemical
pathway.
Understanding Bradykinin (1-3) enriches our knowledge of how the kinin-kallikrein system
functions at a fine-tuned level. Bradykinin, the parent molecule, exerts its effects by binding to
specific receptors, triggering processes that lead to vascular and inflammatory responses. When
bradykinin is cleaved into fragments like Bradykinin (1-3), these smaller peptides can potentially
interact with biological systems in nuanced ways, either by modulating enzyme activity that affects
kinin balance, acting as ligands with other receptor systems, or influencing cellular processes
indirectly.
Studying Bradykinin (1-3) can reveal the dynamics of kinin degradation and clearance
in the body—a crucial aspect of maintaining homeostasis and preventing overactivity of the kinin system
that could lead to pathological conditions such as chronic inflammation or hypertension. The way these
fragments are processed and what effects they exert can illuminate feedback mechanisms that maintain
equilibrium within the system.
The importance also extends to pharmacological perspectives. By
dissecting the roles and actions of Bradykinin (1-3), researchers can better understand how to
manipulate the kinin system with drugs, particularly in diseases where the system's regulation is
disrupted. Targeting specific fragments or understanding their interactions can lead to more precise
therapeutic interventions that offer better efficacy with reduced side effects compared to current
treatments that broadly affect the pathway.
Additionally, Bradykinin (1-3) studies contribute to
the foundational science necessary for exploring potential physiological roles beyond what is
classically understood. Innovating in the context of network systems biology, researchers can start
mapping out the complex interactions of kinins with other pathways, opening the door to discovering
unforeseen connections and applications in medical research. The significance of studying this fragment
is thus tied to unraveling the full spectrum of kinin activity and modulation, enabling the development
of targeted therapies that could significantly impact patient care in the future.