Glycyl peptide
- Название продукта: Glycyl peptide
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- Производитель: Ascent Petrochem Holdings Co., Limited
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- Glycyl peptide is typically used in formulations when pH, ionic strength, and solvent composition and temperature, shear, and light exposure must be controlled within specific ranges.
| Код ТН ВЭД | 789019 |
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In leave-on facial anti-aging serums, glycyl peptide is introduced during the cooling phase after the carbomer or hydroxyethylcellulose network has been neutralised to pH 5.0–5.4. The addition ratio is 1.5–3.0 wt% of a 5000 ppm aqueous-glycerol stock, corresponding to 75–150 ppm glycyl peptide in the finished product; when HPLC assay data on the certificate of analysis differs from the nominal value, the addition weight is corrected proportionally before batching. Regulatory anchors for this leave-on class include EU 1223/2009 Article 17 safety assessment and Annex II prohibited-substance screening, ISO 22716:2007 sections 7 and 8 for raw material traceability and production control, ISO 17516:2014 for microbial quality, and ISO 11930:2019 for preservative efficacy. Production equipment is a 316L stainless-steel jacketed vessel with a side-sweep scraped-surface agitator operating at 10–20 rpm; the bulk is cooled to 38°C before the peptide stock is added through a 0.45 µm polyethersulfone filter. High-shear mixing above 3000 rpm at this late stage is avoided because it can collapse the gel network and create trapped-air defects; batch-to-batch variation in carbomer lot hydration has required agitation hold times of 45–90 min before pH adjustment. The finished mass is transferred by peristaltic pump to a nitrogen-blanketed filling line. Terminal product types include 30 mL dropper serums, airless pump serums, and single-dose 1.5 mL ampoules.
Why Does the Cooling Rate Control Peptide Integrity in Hot-Process O/W Creams?
The cooling rate from 75–80°C to 38°C is the primary process variable that determines whether glycyl peptide remains within specification in a hot-process oil-in-water emulsion. In this configuration, the oil phase and water phase are separately heated to 75–80°C, combined in a vacuum emulsifier, and dispersed by a rotor-stator at 2800–3500 rpm for 10–15 min. The peptide stock is not introduced into the hot phase; it is added only after the bulk has dropped below 40°C, typically at 38°C, with side-sweep agitation of 15–25 rpm. The addition ratio is 2.0–3.5 wt% of a 5000 ppm stock, yielding 100–175 ppm glycyl peptide in the finished cream. A slower cooling segment between 60°C and 50°C can lead to viscosity build-up at the vessel wall and larger emulsion droplets; this has required periodic side-wall scraping at 20 rpm to maintain batch consistency during production-scale runs. The preservative system must be selected without strong oxidising agents such as hydrogen peroxide because these reduce recoverable peptide assay values by 15–30% over 48 h at 40°C. Regulatory compliance for this product class requires EU 1223/2009 Article 14 CPNP notification for EEA distribution, ISO 22716:2007 section 8 batch records, and ISO 11930:2019 challenge testing of the preserved emulsion. Terminal product types include night recovery creams, neck and décolleté creams, and barrier-supporting hand creams packaged in 50 mL jars or airless tubes.
Glycerin-rich eye contour gels impose a distinct set of solvent-polymer constraints when glycyl peptide is incorporated at levels above 100 ppm. The addition ratio in this application is 1.0–2.5 wt% of the 5000 ppm stock, producing 50–125 ppm peptide in the finished eye gel. The downstream production sequence begins with hydration of a non-ionic or lightly anionic rheology modifier in a glycerin-water mixture at 25–30°C; the polymer is allowed to swell for 60–120 min before the peptide stock is added. Product development data indicate that adding the peptide before complete polymer hydration reduces viscosity by 20–35% and creates visible microgel formation at batch scale. Amine-based neutralisers are avoided in this system because residual free amine can create local pH zones above 8.0, which accelerates peptide hydrolysis and causes stringy gel defects. Compliance is maintained under EU 1223/2009 Article 17, ISO 22716:2007 section 8.2, and preservative efficacy is validated by ISO 11930:2019; patch-test data generated during safety assessment reference OECD TG 439 for reconstructed human epidermis irritation. The cooled bulk is filled into 15 mL airless eye-cream tubes, roll-on applicators, or 5 mL single-dose gel pods. Terminal product types include cooling eye cushion gels, peptide eye serums, and low-perfume eye contour creams.
Ethanol-Tolerant Scalp Tonic Formulation Windows
In 50–70 vol% ethanol scalp tonics, the peptide stock must remain clear after ethanol dilution and must not form visible aggregates at 25–30°C. The addition ratio is 0.8–2.0 wt% of the 5000 ppm stock, corresponding to 40–100 ppm glycyl peptide in the finished tonic. Production begins by dissolving ethanol-soluble emollients, menthol or fragrance into a 304 stainless-steel tank with spark-proof motorised stirring; deionised water cooled to 30°C is then metered in, and the peptide stock is added as the final component. Adding the stock before the water phase has reached final volume can generate transient local ethanol concentration above 80 vol%, causing peptide precipitation and filter fouling on the subsequent 0.22 µm cartridge. Batch throughput loss from premature peptide addition has been observed as a reduction in filtrate flow from 60 L/h to 20 L/h at 1.5 bar differential pressure. Regulatory compliance includes EU 1223/2009 Article 17 and Annex III screening for solvent residues, ISO 22716:2007 section 8.2 batch control, ISO 11930:2019 for preservation in hydroalcoholic systems, and ISO 17516:2014 for microbial limits. Filling is completed through a 0.22 µm cartridge into 100 mL spray tonics, dropper scalp serums, or pre-wash root essences. Terminal product types include leave-in scalp sprays, anti-thinning drop serums, and cooling pre-shampoo treatments.
Production-scale batches of post-procedure repair emulsions have shown that glycyl peptide addition must occur after the preservative-free cooling phase and after any magnesium aluminium silicate has fully developed yield value. In this application, the addition ratio is kept at 0.25–1.0 wt% of the 5000 ppm stock, yielding 12.5–50 ppm peptide, because the finished formula is applied to compromised skin and is often preservative-free or relies on low water activity. The downstream process uses a 316L vacuum vessel with a 10–15 rpm anchor stirrer; the aqueous phase is cooled to 32–35°C before the peptide solution is added through a 0.22 µm sterilising-grade filter in an ISO 7 cleanroom environment. Microbiological control follows USP <61> and USP <62> for enumeration and specified organism absence, or ISO 18415:2017 as part of product release. Water activity is maintained below 0.65, and pH is held at 5.0–5.5 to reduce peptide hydrolytic depletion during shelf storage. The regulatory file references EU 1223/2009 Article 17 and ISO 22716:2007 section 8. Terminal product types include single-use 1 mL post-peel ampoules, aluminium tubes of repair balm, and occlusive barrier ointments. Published data for this specific preservative-free configuration is limited; batch-specific stability under ISO/TR 18811:2018 is required before distribution.
When Anhydrous Concentrates Require Water-Free Glycyl Peptide Delivery
Direct addition of aqueous glycyl peptide solution to an anhydrous ester or oil phase produces localised destabilisation if the water content of the finished formulation must remain below 1.0 wt%. The peptide stock is therefore pre-mixed with 1,3-propanediol or anhydrous glycerin at a ratio of 1:1 to 1:2 before introduction into the mixing vessel. The final addition ratio is 0.5–2.0 wt% of the pre-diluted peptide system, corresponding to 25–100 ppm peptide in the anhydrous concentrate. Production is carried out in a vacuum planetary mixer at 40–45°C with a 20 rpm blade and 800 rpm disperser; water activity is monitored at 0.60–0.70 after dispersion to verify that no free-water phase has been introduced. If the water activity rises above 0.75, the batch is reworked by vacuum dehydration at 45°C for 30–45 min; no more than two rework cycles are permitted before the batch is quarantined. Compliance is established through EU 1223/2009 Article 17, ISO 22716:2007 section 8, and stability evaluation under ISO/TR 18811:2018. Terminal product types include 5 mL anhydrous ampoule concentrates, oil-based facial boosters, and two-phase serum concentrates packaged with a separate aqueous phase.
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- Glycyl peptide Производится в соответствии с системой качества ISO 9001 и отвечает соответствующим нормативным требованиям.
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Glycyl peptide, in the unmodified dipeptide form glycylglycine (Gly-Gly), is identified by IUPAC name 2-[[2-aminoacetyl]amino]acetic acid and CAS 556-50-3. The molecular formula is C4H8N2O3, with a relative molecular mass of 132.12 g mol−1. The product is supplied as a white crystalline powder or lyophilized solid used principally as a zwitterionic hydrogen-ion buffer in enzyme assays, diagnostic reagent formulation, and protein separation systems. Catalogue models are supplier-specific and should not replace the CAS identifier in procurement documents. For biological applications, a biotech grade with bacterial endotoxin ≤0.25 EU mg−1 and total aerobic microbial count ≤102 CFU g−1 is typically specified. The free compound dissolves in water to give a clear solution with low absorbance above 240 nm, which is relevant for ultraviolet-visible detection at 340 nm and 405 nm.
What Lot-Release Tests Are Reported for Biotech-Grade Glycyl Peptide?
The certificate of analysis for lyophilized biotech-grade glycylglycine commonly includes the following release criteria. Methods are selected from compendial test procedures where applicable, and residual solvent limits are aligned with USP 467 Class 3 requirements.
| Test | Method or standard | Specification |
|---|---|---|
| Appearance | Visual inspection | White to off-white crystalline powder |
| Identification by infrared spectroscopy | USP 197 | Conforms to reference standard |
| Assay by HPLC | USP 621 | ≥ 99.0 % area |
| Water content by Karl Fischer | USP 921 | ≤ 1.0 % |
| pH of 5 % aqueous solution | Potentiometric, 25 °C | 5.5–6.5 |
| Residue on ignition | USP 281 | ≤ 0.1 % |
| Heavy metals as Pb | USP 231 | ≤ 10 ppm |
| Bacterial endotoxins | USP 85 / EP 2.6.14 | ≤ 0.25 EU mg−1 |
| Total aerobic microbial count | EP 2.6.12 | ≤ 102 CFU g−1 |
| Residual solvents | USP 467 | Meets Class 3 limits |
| Solubility in water at 20 °C | Visual inspection | ≥ 100 mg mL−1, clear |
When the product is supplied as a sterile-filtered liquid concentrate, additional release data include pH, bioburden, and filter-integrity testing. Filter-integrity test acceptance follows ASTM F838-20 for sterilizing-grade membranes, using bubble point or diffusive flow measurements appropriate to the membrane lot.
Ionization Behaviour and Buffer Capacity
Glycylglycine contains two ionizable groups. The carboxylic acid pK1 is 3.14 and the amino pK2 is 8.25 at 25 °C, giving a zwitterionic isoionic point near 5.7. Usable buffer capacity in aqueous solution spans approximately pH 7.2–9.2, with maximum capacity at pK2. The thermodynamic temperature coefficient dpK2/dT is −0.028 pH °C−1, which is similar to Tris and steeper than HEPES. A buffer adjusted to pH 8.30 at 20 °C therefore shifts by approximately 0.14 pH units when measured at 25 °C. pH adjustment must be conducted at the intended assay temperature, with electrode calibration traceable to certified pH standards under ISO 23496. At ionic strengths above 0.1 mol L−1, the apparent pK2 is lowered; high-salt formulations should therefore be prepared from buffer tables that account for ionic strength.
The compound behaves as both a primary amine and a peptide. It reacts with ninhydrin, fluorescamine, and amine-reactive electrophiles such as N-hydroxysuccinimide esters and isocyanates. Buffer exchange or solid-phase extraction is required before derivatization-based protein labelling, because the free α-amino group contributes background. The peptide bond is not chromophoric above 240 nm, but the carboxylate group produces weak absorbance below 220 nm; lot-specific background should be measured when low-wavelength HPLC detection is used.
A 100 mmol L−1 glycylglycine-NaOH buffer is prepared by dissolving 13.21 g of anhydrous glycylglycine in 900 mL of water conforming to ISO 3696 Grade 2 or higher. The solution is titrated to pH 8.20 ± 0.02 at 25 °C with 1 mol L−1 sodium hydroxide, made up to 1 L, filtered through a 0.22 µm polyethersulfone membrane, and degassed under vacuum at 50 mbar for 5 min. The prepared buffer is stored at 2–8 °C and is used within 7 days. It is discarded if turbidity develops or pH drift exceeds 0.05. Conductivity and osmolality depend on the amount of sodium hydroxide and added sodium chloride; published data for a proprietary diagnostic formulation may be limited, and lot-specific values should be requested when the buffer is used in cell-based perfusion systems.
When Glycylglycine Replaces Tris, Phosphate, or HEPES in Downstream Assays
The selection of glycylglycine as a replacement buffer depends on its pKa, temperature sensitivity, primary-amine interference, and metal-binding behaviour. Table 2 summarizes these parameters against three common alternatives.
| Buffer | pKa at 25 °C | dpKa/dT | UV absorbance above 260 nm | Primary-amine interference | Metal interaction and incompatibility |
|---|---|---|---|---|---|
| Glycylglycine | 8.25 | −0.028 | Negligible | Yes | Moderate Cu2+/Ni2+ coordination; peptide bond susceptible to peptidases |
| Tris | 8.06 | −0.028 | Negligible | Yes | Moderate Zn2+/Cd2+ coordination; incompatible with aldehydes and hypochlorite |
| HEPES | 7.55 | −0.014 | Negligible | No | Low metal binding; oxidation risk with H2O2/UV |
| Phosphate | pK2 7.2 | −0.0028 | Negligible | No | Precipitates Ca2+/Mg2+; low capacity above pH 8 |
Replacement of phosphate with glycylglycine eliminates calcium phosphate precipitation but introduces a primary amino group and a temperature coefficient approximately 10-fold steeper. Replacement of Tris with glycylglycine may reduce interference in assays where the tertiary amine of Tris crosses biological membranes or participates in Schiff-base chemistry; it does not remove primary-amine interference in labelling steps. Compared with HEPES, glycylglycine provides a higher useful pH range but requires tighter temperature control and is more likely to undergo proteolytic degradation in crude biological matrices. For long-duration incubations with protease-rich lysates, HEPES or a protease inhibitor may be more stable.
Pilot-scale dissolution of lyophilized glycylglycine is performed by slow addition through an eductor or into a vortex produced by an overhead impeller at 200–400 rpm. Uncontrolled dumping into a static receiving vessel forms a hydrated surface crust and prolongs mixing in 316L stainless steel vessels. Dissolution is endothermic; water at 20–25 °C is preferred because heating above 60 °C accelerates peptide-bond hydrolysis. For large-volume filtration, a peristaltic pump with a 0.22 µm capsule filter is used, and filter integrity is recorded using ASTM F838-20. Sterilization of sealed aqueous glycylglycine solutions by autoclaving above 121 °C is not recommended because prolonged exposure can reduce peptide content and buffer capacity through hydrolysis to free glycine.
Evaluating Storage, Incompatibilities, and Operational Boundaries
The dry powder is hygroscopic. Repeated opening at relative humidity above 60 % increases water content and may reduce assayable peptide content. Storage at 2–8 °C in sealed polyethylene-lined packaging with desiccant is specified for biotech-grade lots. The product should not be combined with nitrosating agents, strong oxidizers, or amine-reactive electrophiles. Transition-metal additives at millimolar concentrations may coordinate with the carboxamide and amino groups, shifting free ion activity; strict metal-free workflows require passage through a chelating resin after pH adjustment and storage in acid-washed polypropylene containers. Dry heat sterilization of the bulk solid is not recommended because it may promote discoloration and peptide bond degradation. The material is not classified as a sterilizing agent and must not be substituted for buffer-component sterilization in aseptic manufacturing.
