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Original Title: Heyi Commercial Port: The Role of Carnosine and Decarboxylating Carnosine! In the chapter of "Antioxidant and Anti-glycation Mechanism of Carnosine and Decarboxylating Carnosine", the role of these two components is introduced in detail, but at present, as the propaganda of anti-glycation in the market, carnosine does not seem to really play a major role, perhaps the biggest reason is that the effect is not obvious, it can only play an auxiliary role. In fact, carnosine is a very important and high content of antioxidant short peptide, but its stability is relatively poor, the skin surface also contains a lot of carnosine enzyme, which has been decomposed before it works in the process of skin care. In order to give full play to the role of carnosine, scientists have modified carnosine, including acetylation, decarboxylation and other means, to make this ingredient more stable, so that this kind of ingredient can really play its due role in the field of medical treatment, skin care and health. In this paper, the interaction between carnosine and decarboxylated carnosine is described in detail according to the reference data. We preliminarily tested the effect of decarboxylating carnosine on keratinocyte wound healing in the laboratory. At 0.078% decarboxylating carnosine, the cell migration rate was 61.4% (41.5% for blank control, 78.7% for positive control, and 49.4% for 0.1625% ectoin) after 48 hours. The effect of decarboxycarnosine may exceed our expectations. Engineers are welcome to ask for samples for testing. Effects of carnosine and decarboxylating carnosine (common ground): 1. They all exist naturally in organisms. 2. They resist oxidation and complex metal ions. 3. Reduction of lipid peroxides 4. Inhibition of lipid peroxidation and collagen cross-linking caused by reducing sugar 5. Protect the activity of SOD in the skin after UV irradiation 6. Ultimate anti-aging Note: For the action pathways of carnosine and decarboxylated carnosine, please refer to the part of "Antioxidation (I)-Generation and Action of Free Radicals" in which Fe2 + and Cu + catalyze hydroxyl radicals and finally lipid peroxides to generate acrolein and 4-hydroxynonenal. All the following experimental design pathways can be referred to this figure. Expand the full text Figure. Different pathways of free radical formation Where decarboxylating carnosine is stronger than carnosine: 1, that capacity of complexe metal ions is strong,jacketed glass reactor, and the antioxidant capacity is better; 2. The ability to inhibit collagen cross-linking is much better than that of carnosine. 3. It is not easy to be hydrolyzed by enzymes on the skin surface, and the action time is longer. 4. Decarboxycarnosine is cationic, which is more closely adsorbed to the skin and more easily penetrated into the skin. Carnosine has an inner salt structure, and its electronegativity is much smaller than that of decarboxylating carnosine. 5. The stability of decarboxylating carnosine is better than that of carnosine, and its sensitivity to temperature and pH is less than that of carnosine. 6. Major brands at home and abroad have upgraded their anti-glycation products, replacing carnosine with decarboxylated carnosine, such as Peleya Double Resistance Essence 2021 Record Edition, Estee Lauder Eye Cream 2020 Record Edition, etc. Use of carnosine and decarboxylated carnosine: 1. Avoid combining with reducing sugar as far as possible,wiped film evaporator, which may lead to reaction in the system. Non-reducing sugar can 2. It is mentioned in the literature that EDTA can make the in vitro antioxidant activity of imidazole peptidomimetics lose, and EDTA should have a stronger ability to complex metal ions, but EDTA will not enter cells, so it is not recommended to use it together at present; it may affect the mutual effect with the components that can enter the membrane, such as octanoyl hydroxamic acid. 3. Because carnosine has the best stability near the isoelectric point, it is easy for carnosine to undergo conformational transition and oxidative discoloration when it deviates far from the pH. Decarboxylated carnosine has no such problem. 4. Carnosine and decarboxylated carnosine may compete with tripeptide-1 and blue copper peptide for copper ions, resulting in loss of activity of blue copper peptide. Avoid using them together. 5. The product of carnosine decarboxylate exists in the form of hydrochloride and has strong ionicity, but it is generally recommended to add about 0.1% in the formula to achieve the effect. 1. Carnosine and decarboxylating carnosine are naturally occurring components in tissues. The structure of carnosine 2HCl Structure of Decarboxycarnosine (Hydrochloride) Carnosine (β-alanyl-L-histidine), with chirality (note that carnosine has a thickened bond in its structure, while decarboxylated carnosine does not), is derived from histidine. It is one of the most abundant (1-20 mM) nitrogenous compounds in the nonprotein fraction of vertebrate skeletal muscle and certain other tissues, including the olfactory epithelium and olfactory terminal projections. Carnosine has a weak anti-inflammatory activity and a tendency to stimulate tissue repair, particularly when used after oral surgery. At higher temperature or too high or too low pH, histidine is easily oxidized and discolored, so the stability of carnosine is relatively poor. Decarboxycarnosine (β-alanyl-L-histamine), present in a variety of histamine-rich mammalian tissues (e.g., decarboxylation after extraction ,wiped film distillation, heart, kidney, stomach, and intestine) in amounts as high or higher than those reported for carnosine, histamine, and 3-methylhistamine, but lower than the concentration of free histidine. In rat tissues, histidine, labeled with the radioisotope tracer 3H, is rapidly (within minutes) incorporated into decarboxylating carnosine, carnosine, and histamine, consistent with the metabolic link between the listed compounds and their potential role in histamine synthesis or degradation (see Figure 1). Thus, decarboxylated carnosine may serve as an active intermediate in the carnosine-histidine-histamine metabolic pathway and may represent an alternative means of histamine synthesis or may be a catabolite of histamine. Figure 1. Decarboxycarnosine is involved in carnosine -Histidine-histamine metabolic pathway Known reactions correspond to the following enzymes: 1. Carnosinase; 2. Carnosine synthetase; 3. Histidine decarboxylase; 4. Decarboxylating carnosine synthetase. Solid lines represent known reactions and dashed lines represent possible reactions. The figure shows the possible role of these compounds as physiological antioxidants or pro-oxidants in the presence of transition metals. 2. Antioxidant capacity of carnosine and decarboxylated carnosine Antioxidative (antiglycation) mechanism of carnosine and decarboxylate carnosine A. Carnosine, decarboxylated carnosine and other peptidomimetics containing imidazole groups can reduce lipid peroxides (LOOH) to non-toxic alcohols; B. Carnosine and decarboxylated carnosine can be complexed with transition metal ions (such as Fe2 + and Cu2 +) to prevent metal ions from catalyzing the generation of free radicals, and the complexed components have better antioxidant effect; C. React with the end products of lipid peroxidation (malondialdehyde, nonenal, etc.) to prevent these products from cross-linking with collagen and enzymes; see Figure 2 D. It can react with reducing sugar to prevent collagen glycosylation from causing yellow color, loss of elasticity and degradation. Figure 2. Schematic diagram of cross-linking between aldehyde group and amino group of protein Experimental data and comparison of carnosine and decarboxylating carnosine on anti-oxidation (anti-glycation) a. Inhibitory effect of carnosine on lipid peroxidation Fig. 3 shows data on the change in product content after lipid peroxidation catalyzed by Fe2 + (ascorbic acid protects Fe2 + from rapid oxidation), followed by protection with different concentrations of carnosine and N-acetylcarnosine. The results showed that carnosine had a good protective effect on lipid peroxidation. Figure 3. (A) Lipid peroxidation products (calculated as malondialdehyde MDA), (B) diene conjugates, (C) triene conjugates, and ketone and aldehyde products (274 nm absorption fraction), incubated separately in liposomes (1 mg/ml) for 60 min (6, dotted line) with the addition of the peroxidation-inducing system of Fe 2 + + ascorbate (1). Antioxidants N-acetylcarnosine (NAC) (10 or 20 mM) (2, 3) or L-carnosine (10 or 20 mM) (4, 5) were added to the system containing the peroxidation-inducing agent at the 5th minute of the incubation period. At 0 time and timing sampling test. b. Decarboxycarnosine-protected protein cross-linked by lipid peroxide Linoleic acid hydroperoxide (LOOH) was used to react with bovine serum albumin (BSA), and then decarboxylated carnosine was used for protection. Decarboxycarnosine can reduce LOOH to nontoxic LOH and protect BSA from cross-linking. The effect of decarboxylated carnosine is much better than that of carnosine. Compared with natural Ve, Ve can only scavenge free radicals, but it is powerless to form hydroperoxides, as shown in Figure 6. Note: Hydroperoxide is a compound containing — Ooh Figure 4. Structure and Formation of Linoleic Acid Peroxide Figure 5. (A) 13 (S) Linoleic acid hydroperoxide in phosphate buffer solution (0.1 M; HPLC chromatogram after 15 minutes incubation at 37.degree.C. (pH 7.3). Absorption wavelengths used: 234 and 205 nm. (B) 13 (S) hydroxylinoleic acid phosphate buffer solution (0.1 M; PH 7.3). Monitoring absorbance wavelength used: 234 nm. (C) HPLC monitoring of oxidative degradation of protein (BSA) by linoleic acid hydroperoxide (LOOH). (D) Correlation of natural imidazole-containing peptidomimetic protection with linoleic acid hydroperoxide (LOOH) reduction. (E) HPLC spectrum recorded at 234 nm wavelength. BSA (0.33 G/l) was incubated in 0.1 M phosphate buffer, pH = 7.3 with 1.5 mM 13 (S) -linoleic acid hydroperoxide and 5 mM decarboxylated carnosine for 60 hours at 37 ° C. Fig. 6. (A) SDS-Page of BSA exposed to 13 (S) -linoleic acid hydroperoxide. 1: BSA; 2: BSA + LOOH; 3: BSA + LOOH + decarboxylating carnosine; 4: bovine serum albumin + LOOH + L-carnosine; 5: BSA plus LOOH plus N-acetyl-h-alanylhistamine; 6: BSA plus LOOH plus L-prolylhistamine; 7: BSA plus Looh plus vitamin E. c. Decarboxylating carnosine protection Activity of superoxide dismutase after UVA/UVB irradiation Oxidative inactivation of SOD in skin cells during UV exposure represents both a reduction in part of the skin's natural antioxidant defenses and an increase in the effects of oxidative stress. The authors treated pig ears with 0%, 0.5%, 1%, and 2% decarboxylated carnosine cream, and then cut skin fragments after UVA-UVB irradiation (0.8 J/cm 2) to measure SOD activity. Fig. 7. (A) Kinetics of SOD-like activity in extracts of non-irradiated or irradiated skin previously treated with a cream containing 0% or 0.1% decarboxylating carnosine. A slope of 0.1 OD units/min was obtained for unirradiated skin. A slope of 0.17 OD units/min was obtained for irradiated skin treated with 0% decarboxylating carnosine. Irradiated skin treated with 0.1% decarboxylating carnosine obtained a slope of 0.14 OD units/min. (B) Protection of SOD activity of isolated porcine ear derm-epidermis treated with different concentrations of decarboxylating carnosine. The average TSEM of 10 independent experiments is presented. Significant difference (p < 0.001) vs control (t test). Percent protection was calculated by comparison with the SOD activity of non-irradiated skin. d. Carnosine complexe with decarboxylated carnosine Fe2 + ions, etc. The 3D models of carnosine, N-acetylcarnosine, and decarboxylating carnosine have a "claw-like" structure, similar to a "pocket", which facilitates the complexation with metal ions, and the actual data have supported the existence of this structure, as shown in Figure 8. By computer calculation, the chelation energy of decarboxylated carnosine with Fe2 + (-7725 eV) is less than that of carnosine-Fe2 + (-883 eV). Decarboxycarnosine has stronger chelating ability with Fe2 + and is more stable. Figure 8. Computer Simulation of N-Acetylcarnosine, Carnosine and Decarboxycarnosine in the Lowest Energy State of the Ball-and-Stick Model e. Hydrolysis of Carnosine and Decarboxylating Carnosine on Skin Surface Carnosine and decarboxylating carnosine are abundant in the skin. It has been proved by experiments that carnosine and decarboxylating carnosine are incubated with skin microsomes. Carnosine can be degraded by more than 60% in 10 minutes and completely decomposed in 1 hour, while decarboxylative carnosine is degraded very slowly. The main reason is that there is no corresponding enzyme on the skin surface. Figure 9. (A) Microsomal (4 mg/ml total protein) kinetics of decarboxylated carnosine (0.5 mM) and L-carnosine (0.5 mM) measured by HPLC (fluorescence on dansyl chloride reaction band). Each point represents the average of 3 experiments. (B) Kinetics of catabolism of L-carnosine and decarboxylated carnosine in the skin microsomal fraction (4 mg/ml total protein) during NADPH2-dependent enzyme activation. The kinetics of microsomal metabolism upon addition of (0.5 mM) NADPH2, decarboxylating carnosine, and L-carnosine were measured by HPLC. Each point represents the average of 3 experiments. f. Products using decarboxylated carnosine References Babizhayev M A . Biological activities of the naturalimidazole-containing peptidomimetics n-acetylcarnosine, carcinine andL-carnosine in ophthalmic and skin care products. [J]. Life Sciences, 2006,78(20):2343-2357. Babizhayev M A ,thin film distillation, Seguin M C , Gueyne J , et al. l-carnosine(β-alanyl-l-histidine) and carcinine (β-alanylhistamine) act as naturalantioxidants with hydroxyl-radical-scavenging and lipid-peroxidase activities[J]. Biochem. J. 1994. Return to Sohu to see more Responsible Editor:. toptiontech.com

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