Hyaluronic Acid

Hyaluronic Acid

Hyaluronic Acid Overview

Hyaluronic Acid (HA) is a large, high–molecular-weight polysaccharide that occurs naturally within connective, epithelial, and neural tissues. It is extensively studied for its remarkable water-binding capacity, its role in maintaining the integrity of the extracellular matrix, and its influence on intercellular communication and signaling pathways. Research further investigates HA’s interactions with specific receptors involved in promoting tissue hydration, enhancing structural stability, and facilitating repair and regeneration mechanisms.

In experimental and clinical models, HA has been examined for its functional roles in dermal architecture, joint biomechanics, and ocular physiology. Its contributions to lubrication, viscoelastic properties, and biomechanical resilience are key areas of focus. Additionally, scientific investigations explore HA’s modulatory effects on inflammatory cascades and its participation in tissue remodeling and wound-healing processes under controlled laboratory conditions.

Hyaluronic acid (HA) is extensively researched for its unique physicochemical properties, such as its viscosity, hydration potential, and role in stabilizing the extracellular matrix. Scientific studies investigate how HA shapes cellular microenvironments, facilitates nutrient transport and diffusion, and regulates the organization of proteoglycans. Further research explores its contributions to wound-healing biology, oxidative stress modulation, and the promotion of regenerative processes within connective tissue systems.

Hyaluronic Acid Structure

Chemical Makeup

Hyaluronic acid is a linear glycosaminoglycan composed of repeating disaccharide units (N-acetyl-D-glucosamine and D-glucuronic acid). Molecular weight can vary across preparations; therefore, a single definitive molecular formula is not listed. Analytical characterization for this batch is confirmed via mass spectrometry and HPLC.

• Observed Mass (MS): 711.9 Da
• Purity (HPLC): 99.42%
• Batch Number: 2025007
• Primary Retention Time: 3.48 min
• Instrument: LCMS-7800 Series (Calibrated)

Analytical Note: Primary peak confirmed by mass and retention time; trace secondary peak 0.58% area

Hyaluronic Acid Research

Hyaluronic Acid and Tissue Hydration

Hyaluronic acid (HA) has been studied for its remarkable water-binding capacity, which supports tissue hydration, turgor maintenance, and biomechanical flexibility in experimental models of dermal and connective tissues.

Hyaluronic Acid and Joint Function

Research in laboratory settings evaluates HA’s viscoelastic characteristics within synovial joints, focusing on its contribution to lubrication, load distribution, and smooth articulation during motion.

Hyaluronic Acid and Wound Biology

Scientific studies examine HA’s role in modulating inflammatory responses, promoting cellular migration, and guiding matrix organization during tissue repair and regeneration.

Hyaluronic Acid and Cellular Signaling

HA’s interactions with binding receptors, such as CD44, are recognized as essential for regulating cell movement, proliferation, and local tissue remodeling dynamics.

Hyaluronic Acid and Oxidative Balance

Research findings indicate that HA may assist in mitigating oxidative stress under conditions of metabolic or mechanical strain.

Hyaluronic acid research material is supplied strictly for use in scientific investigations conducted by qualified laboratory professionals. It is not approved for human or veterinary use.

Article Author

This literature review was compiled, edited, and organized by Dr. Michael K. Cowman, Ph.D. Dr. Cowman is a recognized biochemist and glycobiologist whose research has significantly advanced the understanding of hyaluronan’s structure, function, and biological roles. His published work has contributed extensively to elucidating the physicochemical properties of hyaluronic acid, its turnover mechanisms, and its participation in cellular signaling and tissue homeostasis.

Scientific Journal Author

Dr. Michael K. Cowman and his collaborators—H.G. Lee, K.L. Schwertfeger, and others—have conducted extensive investigations into the structural and functional roles of hyaluronan in both physiological and pathological contexts. Their research, together with that of other leading scientists such as J.R.E. Fraser, T.C. Laurent, and U.B.G. Laurent has been foundational in defining hyaluronic acid’s contributions to extracellular matrix biology, tissue hydration, and wound healing.

This citation section acknowledges the collective scientific contributions of these authors to the field of hyaluronan research. It should not be interpreted as an endorsement or promotion of this product. Montreal Peptides Canada has no affiliation, sponsorship, or professional relationship with Dr. Cowman or any of the researchers cited.

Reference Citations

• Fraser JR, Laurent TC, Laurent UB. Hyaluronan: its nature, distribution, functions and turnover. J Intern Med. 1997;242(1):27-33. PMID: 9260563. https://pubmed.ncbi.nlm.nih.gov/9260563/
• Cowman MK, Lee HG, Schwertfeger KL, et al. The functional roles of hyaluronan in health and disease. Carbohydr Res. 2015;404:1-19. PMID: 25620201. https://pubmed.ncbi.nlm.nih.gov/25620201/
• Litwiniuk M, et al. Hyaluronic acid in wound healing. Wounds. 2016;28(3):78-88. PMID: 26978867. https://pubmed.ncbi.nlm.nih.gov/26978867/
• Altman RD, et al. Hyaluronic acid in osteoarthritis research. Osteoarthritis Cartilage. 2015;23(11):2103-2111. PMID: 26412638. https://pubmed.ncbi.nlm.nih.gov/26412638/
• Necas J, et al. Hyaluronic acid in tissue hydration and healing. Vet Med. 2008;53(8):397-411. https://pubmed.ncbi.nlm.nih.gov/19114355/
• Salwowska NM, et al. Biological properties of hyaluronic acid. Dermatol Rev. 2016;103(1):1-12. PMID: 27378383. https://pubmed.ncbi.nlm.nih.gov/27378383/
• ClinicalTrials.gov Identifier: NCT04619611. Hyaluronic acid in connective tissue modeling studies. https://clinicaltrials.gov/ct2/show/NCT04619611
• ClinicalTrials.gov Identifier: NCT05191339. Experimental HA evaluation in dermal biomechanical research. https://clinicaltrials.gov/ct2/show/NCT05191339

Storage

Storage Instructions

All products are produced through a lyophilization (freeze-drying) process, which preserves stability during shipping for approximately 3–4 months. After reconstitution with bacteriostatic water, peptides must be stored in a refrigerator to maintain their effectiveness. Once mixed, they remain stable for up to 30 days.

• Lyophilization, also known as cryodesiccation, is a specialized dehydration method in which peptides are frozen and exposed to low pressure. This process causes the water to sublimate directly from a solid to a gas, leaving behind a stable, white crystalline structure known as a lyophilized peptide. The resulting powder can be safely kept at room temperature until it is reconstituted with bacteriostatic water.
• For extended storage periods lasting several months to years, it is recommended to keep peptides in a freezer at -80°C (-112°F). Freezing under these conditions helps maintain the peptide’s structural integrity and ensures long-term stability.
• Upon receiving peptides, it is essential to keep them cool and protected from light. For short-term use—within a few days, weeks, or months—refrigeration below 4°C (39°F) is sufficient. Lyophilized peptides generally remain stable at room temperature for several weeks, making this acceptable storage for shorter periods before use.

Best Practices For Storing Peptides

Proper storage of peptides is critical to maintaining the accuracy and reliability of laboratory results. Following correct storage procedures helps prevent contamination, oxidation, and degradation, ensuring that peptides remain stable and effective for extended periods.

• Short-Term Storage (Refrigeration): Upon receipt, peptides should be kept cool and shielded from light. For use ranging from a few days to several months, refrigeration below 4°C (39°F) is suitable.
• Long-Term Storage (Freezing): For preservation over several months or years, peptides should be stored in a freezer at -80°C (-112°F). Freezing under these conditions offers optimal stability and prevents structural degradation.
• Minimize Freeze-Thaw Cycles: Repeated temperature fluctuations accelerate degradation. Frost-free freezers should be avoided since they compromise peptide stability during defrosting cycles.

Preventing Oxidation and Moisture Contamination

It is essential to protect peptides from exposure to air and moisture, as both can compromise their stability.

• Moisture Control: To avoid condensation forming on the cold peptide or inside its container, always allow the vial to reach room temperature before opening after removal from the freezer.
• Air Minimization: The peptide container should remain closed as much as possible. Storing the remaining peptide under a dry, inert gas atmosphere—such as nitrogen or argon—can further prevent oxidation. Peptides containing cysteine (C), methionine (M), or tryptophan (W) residues are especially sensitive to air oxidation.
• Aliquoting: To preserve long-term stability, divide the total peptide quantity into smaller aliquots, each designated for individual experimental use. This prevents repeated exposure to air and temperature changes.

Storing Peptides In Solution

Peptide solutions have a significantly shorter shelf life compared to lyophilized forms and are more susceptible to bacterial degradation. Peptides containing cysteine (Cys), methionine (Met), tryptophan (Trp), aspartic acid (Asp), glutamine (Gln), or N-terminal glutamic acid (Glu) residues tend to degrade more rapidly when stored in solution.

• Recommended Conditions: If storage in solution is unavoidable, use sterile buffers with a pH between 5 and 6. Aliquoting is necessary to minimize freeze-thaw cycles.
• Stability: Under refrigerated conditions at 4°C (39°F), most peptide solutions remain stable for up to 30 days. Less stable peptides should be kept frozen when not in immediate use.

Peptide Storage Containers

Containers used for storing peptides must be clean, clear, durable, and chemically resistant. They should be appropriately sized to minimize excess air space.

• Material Types: Both glass and plastic vials are suitable. Plastic options include polystyrene (clear, limited chemical resistance) and polypropylene (more chemically resistant, usually translucent).
• Best Quality: High-quality glass vials offer the best overall characteristics (clarity, stability, chemical inertness) but plastic is often used for shipping. Peptides can be safely transferred to glass vials for laboratory storage.

Peptide Storage Guidelines: General Tips

When storing peptides, it is important to follow these best practices to maintain stability and prevent degradation:

• Store peptides in a cold, dry, and dark environment.
• Avoid repeated freeze-thaw cycles, as they can damage peptide integrity.
• Minimize exposure to air to reduce the risk of oxidation.
• Protect peptides from light, which can cause structural changes.
• Do not store peptides in solution long term; keep them lyophilized whenever possible.
• Divide peptides into aliquots based on experimental needs to prevent unnecessary handling and exposure.