Taiy Chemical
Bradykinin (1-3)
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.
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