Pinealon Peptide Overview
Pinealon is a valuable research agent utilized to explore the sophisticated interplay between central brain signaling, cognitive biology, and the mechanisms of metabolic regulation within cells. Its applications include detailed studies on how regulatory neuropeptides affect neuronal communication, synaptic plasticity, and various measures of overall cognitive performance. By targeting systems linked to oxidative stress and cellular energy management, Pinealon acts as a robust model for understanding the biological underpinnings of cellular stability and resilience during adverse conditions.
Research protocols meticulously investigate Pinealon’s specific molecular interactions, with emphasis on its capacity to modulate key neurobiological signaling cascades, such as those governing neurotrophic factors, ensuring mitochondrial integrity, and maintaining cellular energy balance. Published studies suggest that Pinealon may help safeguard neuronal function by shielding cells from metabolic disturbances, actively reducing oxidative damage, and contributing to intracellular repair mechanisms in research models.
In controlled settings, Pinealon is also used to assess the role of peptide-mediated responses in cellular adaptation to various experimental challenges, including environmental, chemical, and oxidative stressors. This research is essential for clarifying how peptide-regulated systems successfully maintain homeostasis, potentially enhance cognitive endurance, and preserve metabolic efficiency, especially in the brain and other energy-intensive tissues.
Pinealon Peptide Structure
Pinealon is a synthetic tripeptide characterized by the amino acid sequence: Glutamic acid - Aspartic acid - Arginine (Glu-Asp-Arg).
Pinealon Peptide Research
Pinealon Research and Neuronal Protection
In studies utilizing prenatal rat models, Pinealon has been shown to exert strong neuroprotective effects by defending developing neurons against oxidative stress, which in turn supports the development of normal cognitive function and motor coordination. Experimental data highlighted significant reductions in the accumulation of reactive oxygen species (ROS) and a decreased number of necrotic brain cells in treated subjects. In essence, these results indicate that Pinealon helps prevent neuronal cell death within these models.
Subsequent investigations have confirmed and elaborated on these initial observations. Further research validated that Pinealon's defense strategy against cell death involves not only reducing oxidative damage and necrosis but also influencing the cellular cell cycle. This finding provided early evidence suggesting that Pinealon's mechanism of action may be exerted at the DNA level. Furthermore, Pinealon has been observed to regulate cell cycle progression through the activation of proliferation pathways. In the context of oxidative stress, this action serves primarily to counteract cellular damage by restoring the balance against destructive reactive oxygen species, thus maintaining neuronal integrity.
Key Findings on Pinealon's Neuroprotection
Research Model
Stress Condition
Key Protective Action
Prenatal Rats
Oxidative Stress
Reduced ROS; Decreased Necrosis; Supports Motor/Cognitive Function.
Adult Rats
Oxygen Deprivation (Hypoxia)
Enhanced Neuronal Resistance; Activated Antioxidant Enzymes; Mitigated NMDA Excitotoxicity.
Studies on adult rats subjected to oxygen deprivation (hypoxia) have demonstrated that Pinealon enhances the neurons' intrinsic resistance to hypoxic stress. This protective mechanism is hypothesized to involve the potentiation of the body's natural antioxidant enzyme systems and the reduction of the damaging, excessive stimulation (excitotoxicity) caused by the N-methyl-D-aspartate (NMDA) receptor pathway.
NMDA, an amino acid derivative, is notorious for causing excitotoxicity, where overstimulation leads to neuronal cell death when present in excess. Overactivation of NMDA receptors is linked to neurological issues in conditions like alcohol withdrawal. The involvement of NMDA-mediated excitotoxicity in neuronal damage from traumatic brain injury and ischemic stroke suggests that Pinealon’s ability to modulate this pathway could indicate significant neuroprotective potential in relevant experimental models.
Article Author
This literature review, compilation, and structure were prepared by Dr. Vladimir Khavinson, M.D., Ph.D. Dr. Khavinson is recognized internationally as a leading biogerontologist and peptide scientist, celebrated for his seminal work on short regulatory peptides and their biological functions in aging, neuroprotection, and cellular homeostasis. His extensive research has provided clarity on the molecular regulatory actions of peptides like Pinealon on gene expression, oxidative balance, and stress-response pathways. Decades of Dr. Khavinson's pioneering contributions have established a comprehensive, foundational understanding of how peptides facilitate cellular repair, adaptation, and longevity.
Scientific Journal Author
Dr. Vladimir Khavinson has performed numerous, in-depth investigations into peptide signaling and molecular mechanisms, frequently collaborating with distinguished researchers, including L.S. Kozina, S.A. Lermontova, A.B. Salmina, and I.P. Artyukhov. Their joint efforts have examined how tripeptides such as Pinealon support neuronal metabolism, fortify endogenous antioxidant defense systems, and protect against neurodegenerative changes in experimental systems. Their collective findings have significantly advanced scientific knowledge of peptide-regulated processes related to stress resistance, energy regulation, and cognitive health.
Dr. Khavinson and his collaborators are acknowledged for developing the scientific basis for peptide-based strategies that promote cellular resilience and influence aging-related processes. This recognition is solely intended to credit their contributions to peptide biochemistry and bioregulation research. Montreal Peptides Canada explicitly states that it has no professional affiliation, sponsorship, or association with Dr. Khavinson or any other researchers mentioned.
Reference Citations
- Khavinson V, et al. Peptide regulation of cellular aging markers. Biogerontology. 2020. https://pubmed.ncbi.nlm.nih.gov/32601935/
- Kozina LS, et al. Tripeptide-mediated protection in stress models. Bull Exp Biol Med. 2019. https://pubmed.ncbi.nlm.nih.gov/31583558/
- Lermontova SA, et al. Peptide effects on cognitive decline models. Neurosci Behav Physiol. 2018. https://pubmed.ncbi.nlm.nih.gov/29138903/
- Lenzer I, et al. Neuroprotective peptide studies in vitro. Front Neurosci. 2022. https://pubmed.ncbi.nlm.nih.gov/35496283/
- Duda PW, et al. Peptide-regulated oxidative stress modulation. Free Radic Biol Med. 2021. https://pubmed.ncbi.nlm.nih.gov/34023514/
- ClinicalTrials.gov. Peptide-based metabolic research. https://clinicaltrials.gov/ct2/show/NCT05259263
- Salmina AB, et al. Peptide influence on brain energy systems. Brain Res Bull. 2017. https://pubmed.ncbi.nlm.nih.gov/28526350/
- Wang K, et al. Molecular responses to protective peptide exposure. Mol Cell Biochem. 2020. https://pubmed.ncbi.nlm.nih.gov/32009255/
- Artyukhov IP, et al. Peptide activity in neurodegeneration models. J Mol Neurosci. 2021. https://pubmed.ncbi.nlm.nih.gov/33483877/
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The products offered on this website are furnished for in vitro studies only. In vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.
STORAGE
Storage Instructions
All peptide products are manufactured via lyophilization (freeze-drying), a process that ensures stability during shipping for approximately 3–4 months.
- After reconstitution with bacteriostatic water, the solution must be stored in a refrigerator (at or below 4 degrees C (39 degrees F)) to maintain its effectiveness. Once mixed, the solution typically remains stable for up to 30 days.
Lyophilization, or cryodesiccation, is a precise dehydration technique involving freezing and exposure to low pressure, which causes the water to sublimate (solid to gas). This leaves a stable, white crystalline powder known as a lyophilized peptide. The powder is safe for room temperature storage for short durations until reconstitution.
For long-term storage spanning several months to years, storage in a freezer at -80 degrees C (-112 degrees F) is highly recommended. This ultra-low temperature is optimal for maintaining structural integrity and ensuring long-term stability.
Upon receipt, peptides must be kept cool and protected from light. For short-term use (days to months), refrigeration below 4 degrees C (39 degrees F) is sufficient. Lyophilized powder is generally stable at room temperature for several weeks, which is acceptable for very short storage periods before immediate use.
Best Practices for Storing Peptides
Proper storage is crucial for the reliability of laboratory results, as it prevents contamination, oxidation, and degradation. Following these best practices extends the effective lifespan and maintains the integrity of the peptides.
- Receipt and Placement: Immediately store peptides in a cool, light-protected environment.
- Short-Term Storage: Refrigeration (below 4 degrees C (39 degrees F)) is suitable for lyophilized peptides.
- Long-Term Storage: Freezing at -80 degrees C (-112 degrees F) is the standard for long-term preservation.
Researchers must minimize freeze-thaw cycles, as repeated temperature fluctuations accelerate degradation. Additionally, avoid frost-free freezers because their defrost cycles introduce temperature variability that compromises stability.
Preventing Oxidation and Moisture Contamination
Protecting peptides from air and moisture is essential for stability. Moisture contamination is a high risk from condensation when removing cold vials from the freezer. To prevent condensation, always allow the vial to reach room temperature before opening it.
To minimize air exposure, keep the container sealed as much as possible, promptly resealing after extraction. Storing the remaining peptide under a dry, inert gas (nitrogen or argon) offers additional protection against oxidation. Peptides containing cysteine (C), methionine (M), or tryptophan (W) residues are especially vulnerable to air oxidation and require maximum caution.
For long-term stability, avoid frequent thawing and refreezing. It is highly recommended to aliquot the total peptide quantity into smaller portions for single-use experiments. This prevents repeated exposure to temperature changes and air, maintaining integrity over time.
Storing Peptides in Solution
Peptide solutions degrade much faster than lyophilized forms and are more susceptible to bacterial contamination. Peptides with residues like cysteine (Cys), methionine (Met), tryptophan (Trp), aspartic acid (Asp), glutamine (Gln), or N-terminal glutamic acid (Glu) are less stable in solution.
If solution storage is unavoidable, use sterile buffers with a pH between 5 and 6. Aliquot the solution immediately to minimize damaging freeze-thaw cycles. Most solutions are stable for up to 30 days under refrigeration at 4 degrees C (39 degrees F). Less stable peptides should be frozen when not in immediate use.
Peptide Storage Containers
Containers must be clean, durable, chemically resistant, and sized to minimize air space. Both glass and plastic (polystyrene or polypropylene) vials are acceptable, offering different levels of clarity and chemical resistance.
High-quality glass vials offer superior clarity, stability, and chemical inertness. Though plastic is used for shipping to prevent breakage, peptides can be safely transferred to appropriate glass or plastic vials for specific storage needs.
Peptide Storage Guidelines: General Tips
Storage Requirement
Action
Environment
Cold, dry, and dark.
Handling
Avoid repeated freeze-thaw cycles.
Exposure Control
Minimize air and light exposure.
State
Store lyophilized whenever possible.
Preparation
Aliquot based on experimental needs.