Taiy Chemical
((Cys31,Nva34)-Neuropeptide Y (27-36))2
Synonym Cys31,Nva34-Neuropeptide Y (27-36)2
Species Human
Protein Accession P01303
Purity > 95%
Endotoxin Level < 1 EU/ug
Biological Activity Stimulates food intake in rats
Expression System Chemical Synthesis
Fusion Tag None
Predicted Molecular Mass 1109.3 Da
Formulation Lyophilized
Reconstitution Centrifuge vial before opening. Reconstitute in distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml.
Storage & Stability Store at -20°C. For long-term storage, store at -80°C. After reconstitution, store at -20°C. Avoid repeated freeze-thaw cycles.
FAQ
What is ((Cys31,Nva34)-Neuropeptide Y (27-36))2, and what are its potential benefits?

((Cys31,Nva34)-Neuropeptide Y (27-36))2 is a synthetic peptide derived from Neuropeptide Y (NPY), a 36-amino acid peptide neurotransmitter involved in various physiological processes. This modified peptide, focusing on the specific segment 27-36 of the NPY sequence, has undergone alterations at positions 31 and 34, replaced respectively with cysteine (Cys) and norvaline (Nva). The modifications are designed to enhance the peptide's stability, receptor affinity, or functional activity. Neuropeptide Y itself plays a crucial role in regulating various physiological functions, including energy balance, appetite control, circadian rhythms, and stress response. By focusing on the specific region of NPY, scientists seek to study or modulate precise aspects of these physiological processes.

Research suggests that this modified peptide could offer several potential advantages, such as influencing appetite-related pathways, which could be pivotal in managing conditions like obesity or metabolic syndrome. Due to its role in stress-related pathways, there is also interest in exploring how it might affect anxiety or stress-resilience mechanisms.

Furthermore, because NPY and its derivatives are involved in cardiovascular function regulation, this modified peptide might offer insights into managing hypertension or heart disease. Researchers might explore options where such peptides can be utilized to influence blood flow or vascular resistance.

Moreover, neuropeptides, by their nature, interact with central nervous system pathways. There is an avenue for researching how this peptide modification might affect neurological functions or disorders, possibly offering a therapeutic angle in neurodegenerative diseases or cognitive disorders. The modifications in the peptide could enhance blood-brain barrier permeability, increasing therapeutic potential in central nervous system-targeted treatments.

While the potential benefits are promising, it's imperative to underscore that much of the research might currently be at a preclinical stage. Efficacy and safety need rigorous evaluation through clinical trials before potential therapeutic applications become realities. Nonetheless, the modifications in ((Cys31,Nva34)-Neuropeptide Y (27-36))2 promise an exciting area for future research to unlock novel therapeutics by targeting biological pathways more precisely.

How does ((Cys31,Nva34)-Neuropeptide Y (27-36))2 compare to natural Neuropeptide Y in terms of structural and functional attributes?

The structural differentiation between ((Cys31,Nva34)-Neuropeptide Y (27-36))2 and the natural Neuropeptide Y (NPY) is primarily due to the intentional modifications incorporated into the synthetic peptide. NPY is a native ligand consisting of 36 amino acids, instrumental in various central and peripheral nervous system roles. The modified peptide, on the other hand, is a focus on the 27-36 segment of the sequence, with strategic residue replacements — cysteine for the original amino acid at position 31, and norvaline at position 34. These substitutions are crafted to achieve specific objectives, such as enhanced resistance to enzymatic degradation or improved receptor interaction.

The physiological function of native NPY is multifaceted, involving complex interactions with various receptor subtypes across the body. It's responsible for modulating appetite, energy homeostasis, stress response, and is implicated in influencing blood pressure and heart rate. In contrast, ((Cys31,Nva34)-Neuropeptide Y (27-36))2 seeks to harness or modulate these functions more specifically by binding effectively to certain receptor types, possibly offering heightened specificity or prolonged interaction, ultimately yielding more controlled physiological effects.

From a functional perspective, the modified peptide might provide advantages in research and potential therapeutic contexts. By changing specific amino acids, the overall peptide stability can be improved, which is crucial when considering the peptide for potential therapeutic use, as it would need to maintain integrity until reaching its target site. Also, these modifications might prevent rapid degradation, a common limitation of peptide-based treatments in the bloodstream, resulting in increased bioavailability and clinical efficacy.

The alterations might also influence the mode and capacity of intracellular signaling pathway activation, potentially leading to differentiated or more desirable physiological outcomes compared to native NPY. Such an approach aids researchers not just in understanding the general mechanism of NPY itself, but also in delineating the role specific segments or receptor interactions play in broader physiological contexts.

While the focus on structural and functional attributes for this and other synthetic peptides presents clear advantages, definitive applications remain heavily dependent on ongoing research and trials to concretely understand the impact of these modifications both in vitro and in vivo.

Are there any specific research studies or clinical trials focused on ((Cys31,Nva34)-Neuropeptide Y (27-36))2?

As of the current understanding and existing literature, specific, widely-documented research studies or clinical trials specifically focusing on ((Cys31,Nva34)-Neuropeptide Y (27-36))2 might be at varying stages of research. The scientific exploration of modified peptides is a vibrant and ongoing field, but given the nature of niche or highly specialized peptides, individual studies may not be extensively published or publicly available.

The peptide modification ((Cys31,Nva34)-Neuropeptide Y (27-36))2 itself might feature as a component of broader research exploring neuropeptide Y derivatives or other related peptides interested in assessing their physiologic or pathological relevance. This subset of peptide research often focuses on detailed mechanistic studies which seek to understand how modifications influence receptor binding, efficacy, selectivity, or biological response in various model organisms or cell lines.

Many initial studies of this nature tend to be situated within academic research settings or private sector biotech companies where proprietary information limits public disclosure until patent filings or broader public interest studies are initiated. However, the appeal of peptide-based treatments and interventions due to their specificity and physiological roles means there could be ongoing or upcoming trails exploring various synthetic derivatives. These could aim to unveil insights pertinent to metabolic processes like appetite or energy control, cardiovascular function, or stress-related pathways, all of which are areas of interest given the foundational role NPY plays.

In addition to preclinical research, any progression to clinical trials would depend heavily on initial safety, efficacy evaluations, and subsequent regulatory reviews. Clinical trials if undertaken, focus on evaluating these parameters further across multiple phases to assess impacts in humans, including potential therapeutic dividends and identifying side effects. These trials, when registered, are often made available via clinical trial registries or publications in peer-reviewed journals, providing a resource for understanding current research scopes or results related to this peptide.

Ultimately, while direct references to current trials might not be abundantly available, the trajectory of research on peptides of neuropeptide Y origin remains an active space, with continuous development often prefacing significant announcements regarding clinical advancements or therapeutic potentials. Checking resources like clinicaltrials.gov or academic journals could yield insights into emerging studies or breakthroughs as research in this field progresses.

What are the safety profiles or potential side effects associated with ((Cys31,Nva34)-Neuropeptide Y (27-36))2?

Understanding the safety profile or potential side effects of ((Cys31,Nva34)-Neuropeptide Y (27-36))2 is integral to evaluating its suitability for any potential therapeutic applications. Like many novel peptide-based compounds under investigation, the safety or toxicity of this synthetic peptide must be firmly established prior to it transitioning from exploratory research to more direct therapeutic considerations.

((Cys31,Nva34)-Neuropeptide Y (27-36))2, given its derivation from the naturally occurring Neuropeptide Y (NPY), is suggested to possess an intrinsic biological compatibility. Yet, modifications such as those present in this peptide could lead to unpredicted interactions within biological systems. This necessitates a comprehensive examination of its pharmacokinetic and pharmacodynamic properties in preclinical models. The initial focus typically involves assessing its stability, metabolism, and distribution, helping delineate how long the compound remains active and at what concentrations it circulates through different physiological systems.

Early safety trials often involve in vitro and in vivo studies, potentially employing animal models to predict responses in biological systems akin to humans. These studies typically look for acute toxicity and any chronic or cumulative toxicology if the peptide were to be administered over extended periods or repeatedly. Moreover, testing tends to emphasize detecting potential pro-inflammatory responses, allergic reactions, or any unintended cross-reactivity with biological proteins beyond its targeted receptor pathways.

This peptide's potential side effects, if documented, would be openly reported in scientific studies or clinical trials, aiming to identify any adverse reactions or safety concerns. Common considerations often assessed in peptide-based interventions include impacts on blood pressure, heart rate, appetite variations, or central nervous system-related effects, aligned with NPY's known physiological influence.

Despite safety assessments revealing favorable profiles, understanding risk associated biases, population-specific responses, or the presence of intercurring pathologies remains pivotal, augmenting the perspective on the peptide's clinical applicability. Engaging rigorous scientific and ethical standards during trial phases ensures any potential therapeutic peptides such as ((Cys31,Nva34)-Neuropeptide Y (27-36))2 meet safety validations consonant with regulatory and patient care protocols. As ongoing research advances, these profiles might evolve, pointing toward refined applications and confidence in safety, potentially enlightening newer paths in peptide-related therapeutic applications.

How does ((Cys31,Nva34)-Neuropeptide Y (27-36))2 potentially impact metabolic processes such as appetite and energy balance?

The potential impact of ((Cys31,Nva34)-Neuropeptide Y (27-36))2 on metabolic processes like appetite and energy balance is particularly noteworthy given the essential role its parent peptide, Neuropeptide Y (NPY), plays within these domains. NPY is one of the most potent appetite-stimulating factors, predominantly influencing the hypothalamus, a region of the brain critical in regulating energy homeostasis and hunger signals.

By being a derivative focusing on the crucial 27-36 segment of NPY, the modified peptide ((Cys31,Nva34)-Neuropeptide Y (27-36))2 may differently interact with specific receptor subtypes such as Y1 and Y5 receptors, known to be implicated in appetite modulation and feeding behavior. Enhanced receptor selective activation or inhibition by this peptide can provide insights into controlling appetite signals, possibly attenuating or stimulating intake as found necessary in varying clinical scenarios like obesity or cachexia.

Moreover, modifications involving cysteine and norvaline might intentionally increase binding affinities or elongate signal durations intracellularly, influencing metabolic pathways. Such effects can alter homeostatic states and hormone release involved in feeding rhythms or energy exertion levels, playing a role in better managing energy stores within the body. Shifts in how energy balance is maintained due to modified neuropeptide interaction could lead to profound implications for body weight regulation or metabolic syndrome interventions when thoroughly explored.

Further exploration in metabolic modeling using this peptide could elucidate not just how it impacts central appetite control directly, but also its potential peripheral effects, as NPY receptors are present in other metabolic pathways, including insulin sensitivity and lipid metabolism. Such insights would be pivotal in crafting comprehensive therapeutic strategies aimed not just at limiting caloric intake but improving overall metabolic efficiency, glucose uptake, and lipid storage diversification.

Analyzing dosing, delivery methods, and peptide stability remains a frontier to ensuring metabolic influence remains beneficial without undermining other simultaneously functioning regulatory processes. The potential this peptide holds in understanding and influencing metabolic conditions highlights an intricate balance, leveraging modified mechanisms to influence broad-reaching physiological benefits, paving the way for tailored metabolic interventions.
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