Camel-derived characteristic peptide as well as detection method and application thereof
By extracting characteristic peptides from camel leather glue and using UPLC-MS/MS technology to detect, the problem of camel-derived ingredients detection in donkey-hide gelatin was solved, efficient and accurate detection results were achieved, and product quality and safety were improved.
Patent Information
- Application Number
- CN202410928969.9
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2024-07-11
- Publication Date
- 2025-02-14
AI Technical Summary
The prior art is difficult to effectively detect whether donkey-hide gelatin contains camel-derived ingredients, resulting in different product quality and infringement of consumer rights.
By extracting characteristic peptides from camel skin glue, such as GEAGPAGAAGPAGPR and GPSGPQGTR, and using UPLC-MS/MS technology for detection, we can identify whether there are camel-derived components in the sample.
It has achieved rapid, simple, high sensitivity and strong specificity detection of camel-derived ingredients in donkey-hide gelatin, which can distinguish the adulteration of camel skin from other animal skins, and improves product quality and safety.
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Figure CN119431506A_ABST
Abstract
Description
Technical Field
[0001] The present application relates to the technical field of drug analysis and detection, and specifically to a camel-derived characteristic peptide and a detection method and application thereof. Background Art
[0002] Donkey hide gelatin is a solid gelatin made by boiling and concentrating the dried or fresh skin of the donkey Equus asinus L. It has a wide range of pharmacological effects, such as replenishing blood and activating blood circulation, optimizing immune response, improving Alzheimer's disease, anti-oxidation, anti-fatigue, protecting lung damage, delaying aging, and treating gynecological diseases. Related formula preparations include donkey hide gelatin, Weishenghua granules, Yunkang oral liquid, Zaizaoshengxue tablets, etc.
[0003] As people's health awareness increases, donkey-hide gelatin, which is known for its blood-nourishing and nourishing effects, has attracted more and more attention. However, since donkeys are not the main livestock, the increase in demand for donkey-hide gelatin will inevitably lead to a shortage of raw materials. At present, there are relatively cheap camel skins instead of donkey skins to make donkey-hide gelatin, or donkey skins are mixed with some camel skins to make donkey-hide gelatin, which will lead to uneven quality of related donkey-hide gelatin products and infringe on the rights and interests of consumers.
[0004] Therefore, there is an urgent need for a highly specific and sensitive method for the detection of camel-derived ingredients in donkey-hide gelatin or other products, which can be used to identify whether the product contains camel-derived ingredients. Summary of the invention
[0005] In order to solve the above technical problems existing in the prior art, the present application provides a camel-derived characteristic peptide and a detection method and application thereof, as follows:
[0006] A camel-derived characteristic peptide, wherein the characteristic peptide segment is:
[0007] Characteristic peptide 1: GEAGPAGAAGPAGPR.
[0008] Or:
[0009] Characteristic peptide 2: GPSGPQGTR.
[0010] The method for detecting camel-derived characteristic peptides according to claim 1 comprises the following steps:
[0011] (1) preparing a reference solution of the camel-derived characteristic peptide described in claim 1;
[0012] (2) Ultra-high performance liquid chromatography tandem mass spectrometry (UPLC-MS / MS) was used to measure the samples and reference substances;
[0013] (3) If a chromatographic peak with the same retention time as that in the reference solution appears at the position corresponding to the retention time, the camel-derived characteristic peptide is detected; if no corresponding chromatographic peak appears at the position corresponding to that in the reference solution, the camel-derived characteristic peptide is not detected.
[0014] Furthermore, the reference solution is a reference solution obtained by dissolving the camel-derived characteristic peptide in 1% ammonium bicarbonate solution.
[0015] Furthermore, the ultra-high performance liquid chromatography tandem mass spectrometry technique specifically uses Waters BEH C 18 (2.1 mm × 50 mm, 1.7 μm) column; the guard column is Waters Van Guard BEH C 18 (2.1mm×5mm, 1.7μm) column; column temperature 40℃; mobile phase: 0.2% formic acid water (A)-0.2% formic acid acetonitrile (B), gradient elution (0-0.5min, 5%B; 0.5-3.0min, 5%-30%B; 3.0-3.5min, 30%-95%B; 3.5-4.0min, 95%B); flow rate 0.3mL / min, injection volume 5μL; electrospray ionization (ESI) positive ion mode multiple reaction monitoring (MRM), capillary voltage 3.0kV, ion source temperature 150℃, spray gas and backflush gas: N2, desolvation gas flow rate 1000L / h, desolvation gas temperature 500℃, mass spectrometry data acquisition and processing software is MassLynxV4.1 workstation.
[0016] Furthermore, the ion pairs and mass spectrometry conditions of the characteristic peptides are as follows:
[0017]
[0018] The camel-derived characteristic peptide is used in detecting and identifying camel-derived components.
[0019] Furthermore, the detection and identification of camel-derived ingredients is to detect whether the donkey-hide gelatin contains camel-derived ingredients. In particular, it is to detect and identify whether it contains camel skin ingredients. It can be used to detect camel-derived ingredients in donkey-hide gelatin or other products, and can identify whether the products contain camel-derived ingredients, especially to distinguish donkey-hide gelatin from camel glue made from camel skin, and can also specifically distinguish camel skin adulteration from horse skin, cow skin, sheep skin and pig skin adulteration.
[0020] A method for detecting and identifying whether a sample contains camel-derived components, wherein the camel-derived characteristic peptide detection method is used to detect a sample to be tested. If the camel-derived characteristic peptide is detected, the sample contains the camel-derived component; if the camel-derived characteristic peptide is not detected, the sample does not contain the camel-derived component.
[0021] Compared with the prior art, the technical effects created by this application are embodied in:
[0022] (1) This application uses proteomics methods to find two camel-derived characteristic peptides from camel hide glue, camel-derived characteristic peptide 1: GEAGPAGAAGPAGPR and camel-derived characteristic peptide 2: GPSGPQGTR, which can be used to check the adulteration of camel-derived substances in donkey-hide glue or other samples, and can specifically distinguish camel hide adulteration from horse hide, pig hide, sheep hide and cow hide adulteration. At present, the relevant content of these two characteristic peptides has not been disclosed.
[0023] (2) This application also established a detection method for camel-derived characteristic peptides based on the UPLC-MS / MS MRM method, and proposed its detection limit in donkey-hide gelatin, providing a rapid, simple, highly sensitive and specific method for authenticity identification and quality evaluation of donkey-hide gelatin, thereby improving the quality of donkey-hide gelatin and ensuring the quality safety of the product. BRIEF DESCRIPTION OF THE DRAWINGS
[0024] Figure 1 This is the secondary fragment ion pattern of camel-derived characteristic peptide 1.
[0025] Figure 2 This is the secondary fragment ion pattern of camel-derived characteristic peptide 2.
[0026] Figure 3 This is a specific test chromatogram for the determination of camel-derived characteristic peptide content, where A: mixed reference solution; B: camel skin glue solution; C: donkey-hide gelatin reference medicinal material solution; D: sheepskin glue solution; E: horsehide glue solution; F: new donkey-hide gelatin (containing pig skin) reference medicinal material solution; G: yellow gelatin (containing cow skin) reference medicinal material solution (top: camel-derived characteristic peptide 2, bottom: camel-derived characteristic peptide 1). DETAILED DESCRIPTION
[0027] The technical solution of the present application is further limited below in conjunction with specific implementation methods, but the scope of protection required is not limited to the description.
[0028] Example 1 Search and application of a camel-derived characteristic peptide
[0029] 1 Materials
[0030] nano LC-Q-Exactive-MS / MS liquid-mass spectrometry system (ThermoFisher Technology Co., Ltd.); ACQUITYUPLC H-Class ultra-high performance liquid chromatograph, Xevo TQS triple quadrupole mass spectrometer (Waters Corporation, USA); VX-Ⅲ multi-tube vortex oscillator (Beijing Tengjin Pharmaceutical Technology Co., Ltd.); EL204 electronic balance (Mettler-Toledo Instrument Co., Ltd.); WP-UP-Ⅳ-20 ultrapure water machine (Sichuan Water Technology Development Co., Ltd.); Allegra 30R Centrifuge low-temperature high-speed centrifuge (Beckman Coulter, USA); KQ-500DE CNC ultrasonic cleaner (Kunshan Ultrasonic Instrument Co., Ltd.).
[0031] Donkey hide gelatin control materials, yellow gelatin (containing cowhide) control materials, and new donkey hide gelatin (containing pig skin) control materials were purchased from the China Food and Drug Inspection Institute (Beijing, China), with batch numbers 121274-20190, 121695-201802, and 121745-201701, respectively; 45 batches of donkey hide gelatin: 42 batches were purchased from different manufacturers across the country, with batch numbers 20220208, 20100602, and 21090, respectively. 13, 220204, 220302, 202038, 21120429, 220303, 21112213, 202111110, 21052001, 20220225, 20220114, 211203, 21120101, 01190207, 21092803, 2010067, 21090601, 21100501 、21110401、21110301、22010117、20220113、22030401、22010118、20220301、20220210、22030501、21120701、21120901、21121001、21120601、20220101、20220201、20220202、 20220302, 20220114, 20220110, 21100401, 2110010, 21110201, numbered S41-S42, two batches of laboratory-prepared donkey-hide gelatin adulterated with camel skin, numbered S43 and S44, and one batch of donkey-hide gelatin control medicinal materials, numbered S45; two camel-derived characteristic peptides were synthesized by Shanghai Qiangyao Biological Co., Ltd. (Shanghai), with a purity of ≥95%. Take appropriate amounts of camel skin, sheep skin and horse skin, remove the hair, cut into small pieces, add ultrapure water for ultrasonic cleaning, add 1% sodium carbonate, heat at 60℃ for 30min, add 2.6 times water to boil the gelatin juice for 8h, filter; then add 1.4 times water to boil the gelatin juice for 3h, filter; finally add
[0032] 1.2 times water to boil the glue juice for 3 hours, filter it, combine the glue juice, add appropriate amount of rock sugar, rice wine and soybean oil, concentrate it and dry it in a vacuum oven at 100℃ to make glue respectively.
[0033] Formic acid and acetonitrile, both mass spectrometry grade, were purchased from Merck (Darmstadt, Germany); trypsin (sequencing grade) was purchased from Promega (Wisconsin, USA); ultrapure water prepared using Milli-Q Reference (Millipore, Boston, MA, USA) was used to prepare buffers and other solutions, including LC eluent and SDT lysis buffer; sodium dodecyl sulfate (SDS) and urea were purchased from Bio-Rad (California, USA); dithiothreitol (DTT) and tris-HCl were purchased from Sigma-Aldrich (St. Louis, MO, USA).
[0034] 2 Methods and Results
[0035] 2.1 Preparation of test solution
[0036] 2.1.1 Search for characteristic camel-derived peptides
[0037] Take an appropriate amount of camel skin glue powder and add SDT (composed of 4% SDS, 100mM Tris-HCl, 1mM DTT, pH7.6) buffer for sample lysis and protein extraction. Use BCA protein detection kit to determine the protein content. The obtained protein samples were packaged separately and stored at -80°C. About 20μg of protein from each sample was mixed with 5X loading buffer (10% SDS, 0.5% bromophenol blue, 50% glycerol, 500mM DTT, 250mM Tris-HCl, pH6.8) and boiled for 5min. The protein was separated on 12.5% SDS-PAGE gel (constant current 14mA, 90min). Protein bands were visible by Coomassie Brilliant Blue R-250 staining. Protein digestion was performed with trypsin. Use C 18 The solid phase extraction column was desalted, concentrated by vacuum centrifugation, and reconstituted with 40 μL of 0.1% (v / v) formic acid.
[0038] 2.1.2 Inspection of Camel-derived Substances in Ejiao
[0039] Accurately weigh about 0.1g of donkey-hide gelatin sample, place it in a 10mL volumetric flask, add 8mL of 1% ammonium bicarbonate solution, and ultrasonically treat for 30min (power 250W, frequency 40kHz) to completely dissolve the sample, then add 1% ammonium bicarbonate solution to dilute to the scale, shake well, take 2mL of the solution, centrifuge at 14000r / min for 10min, accurately measure 1mL of the supernatant, add 100μL of 1μg / μL trypsin solution, vortex mix for 3min, enzymatic hydrolysis at 37℃ for 12h, centrifuge at 14000r / min for 10min, take the supernatant, and obtain.
[0040] 2.2 Preparation of donkey-hide gelatin matrix solution
[0041] Accurately weigh 0.1 g of donkey-hide gelatin and medicinal materials, place in a 10 mL volumetric flask, add 40 mL of 1% ammonium bicarbonate solution, and ultrasonically treat for 30 min (power 250 W, frequency 40 kHz) to completely dissolve the sample, then add 1% ammonium bicarbonate solution to dilute to the scale, shake well, and the sample is ready.
[0042] 2.3 Preparation of reference solution
[0043] Accurately weigh appropriate amounts of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 reference substances, dissolve them in 1% ammonium bicarbonate solution to obtain stock solutions with concentrations of 1.0000 mg / mL and 11.0600 mg / mL, respectively, and store them in a -20°C refrigerator for later use. Accurately measure the camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 reference substance stock solutions, and gradually dilute them with donkey-hide gelatin matrix solution (prepared in the same way as in "2.2") to obtain a mixed series of reference substance solutions.
[0044] 2.4 Preparation of camel hide glue reference solution
[0045] Accurately weigh about 0.1g of camel hide glue powder and place it in a 10mL volumetric flask. Add 8mL of 1% ammonium bicarbonate solution and ultrasonically treat for 30min (power 250W, frequency 40kHz) to completely dissolve the sample. Then add 1% ammonium bicarbonate solution to dilute to the scale and shake well. Take 0.5mL of the above solution and place it in a 10mL volumetric flask. Add 0.1g of donkey hide glue control medicinal material powder and add 8mL of 1% ammonium bicarbonate solution. Ultrasonicate for 30min to completely dissolve the sample. Then add 1% ammonium bicarbonate solution to dilute to the scale. The camel hide glue reference solution is prepared from "shake well" under "2.1.2".
[0046] 2.5 Chromatographic and mass spectrometry conditions
[0047] 2.5.1 Search for characteristic camel-derived peptides
[0048] Easy-nLC nano-liquid chromatography system: pre-column Acclaim PepMap100, 100μm×20mm, 3μm; chromatographic column EASY, 75μm×100mm, 3μm; mobile phase is divided into two phases A and B: 0.1% formic acid water (A), 0.1% formic acid-acetonitrile: water (84:16, v / v, B); flow rate: 300nL / min; injection volume: 5μL; gradient elution program is as follows: 0-3min, 5%-8% B; 3-43min, 8%-26% B; 43-48min, 26%-40%; 48-50min, 40%-90%; 50-60min, 90%. Mass spectrometry analysis conditions: Mass spectrometry system: Q Exactive Orbitrap; detection mode: ESI + ; Spray voltage: 3.5kV; Sprayer temperature: 350℃; Sheath gas: 40arb; Auxiliary gas: 10arb; Capillary temperature: 320℃; Scan range: 300-1800; General method: Fullms-ddms2; MS1 resolution: 70,000; MS / MS resolution: 17,500; NCE: 30.
[0049] 2.5.2 Inspection of Camel-derived Substances in Ejiao
[0050] Waters BEH C 18 (2.1 mm × 50 mm, 1.7 μm) column; guard column is Waters Van Guard BEHC 18 (2.1mm×5mm, 1.7μm) column; column temperature 40℃; mobile phase: 0.2% formic acid water (A)-0.2% formic acid acetonitrile (B), gradient elution (0-0.5min, 5%B; 0.5-3.0min, 5%-30%B; 3.0-3.5min, 30%-95%B; 3.5-4.0min, 95%B; 4.0-4.5min, 95%-5%B; 4.5-6.0min, 5%B); flow rate 0.3mL / min, injection volume 5μL. Electrospray ionization (ESI) was used in positive ion mode for multiple reaction monitoring (MRM), with a capillary voltage of 3.0 kV, an ion source temperature of 150 °C, a spray gas and backflush gas of N2, a desolvation gas flow rate of 1000 L / h, a desolvation gas temperature of 500 °C, and the mass spectrometry data acquisition and processing software was MassLynx V4.1 workstation. The ion pairs and mass spectrometry conditions of camel-derived characteristic peptides are shown in Table 1.
[0051] Table 1 Ion pairs and mass spectrometry conditions of camel-derived characteristic peptides
[0052]
[0053] Note: * indicates quantitative ion.
[0054] 2.6 Search for characteristic camel-derived peptides
[0055] Take camel skin glue powder, prepare the test solution according to the method under 2.1.1, and measure according to the conditions under 2.5.1. Import the obtained mass spectrometry data into Thermo Scientific Proteome Discoverer 2.5 software and search according to the database. The search parameters are set as follows: the database is Uniprot_Camelus bactrianus, the enzyme name is trypsin, the maximum missed cleavage site is 2, the precursor mass tolerance is 10ppm, the dynamic modification is alkylation, +57.021Da (C), oxidation, +15.995Da (M) and spontaneous deamidation +0.984Da (N, Q), dynamic modification, 217 proteins and 518 peptides were identified from camel skin glue. Then, the sequences of these proteins were aligned using BioEdit SequenceAlignment Editor software, and the trypsin cleavage sites were simulated to obtain theoretical characteristic peptides, from which the peptides that were not identified by database retrieval were removed, that is, the characteristic peptides of camel hide glue were obtained, and the peptides that could be detected by UPLC-MS / MS MRM method were screened out from these characteristic peptides, which were the target characteristic peptides. Finally, two characteristic peptides were obtained from camel hide glue, camel-derived characteristic peptide 1: GEAGPAGAAGPAGPR and camel-derived characteristic peptide 2: GPSGPQGTR, and their secondary mass spectra are shown in Figure 1-2 .
[0056] 2.7 Inspection of Camel-derived Substances in Ejiao
[0057] 2.7.1 Investigation of enzymatic hydrolysis time and enzyme concentration
[0058] Accurately weigh about 0.1g of camel hide glue powder, pre-treat according to the reference solution preparation method under 2.4, take 1mL of the supernatant and add 100μL of trypsin with concentrations of 0.25, 0.5, 1.0, 2.0, and 4.0mg / mL, respectively. After enzymatic hydrolysis for 12h, inject the samples respectively. According to the peak area of the characteristic molecular ion peak of camel hide glue, the enzyme concentration is determined to be 1.0mg / mL; the fixed enzyme dosage is
[0059] 1.0 mg / mL, the enzymatic hydrolysis time was set to 4, 8, 12, 16, 18 and 22 h, and the enzymatic hydrolysis time was determined to be 12 h.
[0060] 2.7.2 Specificity test
[0061] Accurately weigh about 0.1g of donkey-hide gelatin control medicinal materials, sheepskin glue, horsehide glue, new donkey-hide glue (containing pig skin) control medicinal materials, camel skin glue and yellow gelatin (containing cow skin) control medicinal materials, respectively, and after processing according to the method under 2.1.2, accurately aspirate 5μL of the solution and the mixed reference solution of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2, respectively, and inject and analyze according to the conditions under 2.5.2. In the chromatogram of camel skin glue solution, at the corresponding retention time position in the camel-derived characteristic peptide reference solution, chromatographic peaks with consistent retention times are presented; in the chromatograms of donkey-hide glue control medicinal materials, horsehide glue, new donkey-hide glue (containing pig skin) control medicinal materials, sheepskin glue and yellow gelatin (containing cow skin) control medicinal materials, there are no corresponding chromatographic peaks at the corresponding positions in the reference solution, indicating that the characteristic peptide of camel skin glue is only detected in camel skin glue, with strong specificity, see Figure 3 .
[0062] 2.7.3 Investigation of linear relationship and determination of detection limit and quantification limit
[0063] Take the reference solution under 2.2, inject and analyze under the conditions under 2.5.2, draw the standard curve with the quantitative ion pair peak area (Y) of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 and its corresponding mass concentration (X), and calculate the minimum detection limit (LOD, S / N ≥ 3) and the minimum quantification limit (LOQ, S / N ≥ 10) according to the signal-to-noise ratio, see Table 2. The results show that the linear relationship of each component is good within its respective range.
[0064] Table 2 Linear relationship of camel-derived characteristic peptides
[0065]
[0066] 2.7.4 Precision test
[0067] The mixed reference solution of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 was taken and tested and analyzed according to the method under 2.5.2. The sample was injected 6 times continuously, and the peak area of the quantitative ion pair of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 was recorded, and the precision was calculated. The results showed that the peak area RSD (n = 6) was 1.3% and 0.8% respectively, indicating that the precision of the instrument was good.
[0068] 2.7.5 Stability test
[0069] A camel hide gelatin reference solution was prepared according to the method under 2.4, and the samples were injected at 0, 2, 4, 6, 8, and 12 h according to the conditions under 2.5.2. The RSD (n=6) of the quantitative ion pair peak areas of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 were calculated to be less than 3.5%, indicating that the new donkey-hide gelatin (containing pig skin) characteristic peptide solution had good stability within 12 h.
[0070] 2.7.6 Repeatability test
[0071] Six camel hide glue reference solutions were prepared in parallel according to the method in 2.4, and the samples were injected and analyzed according to the conditions in 2.5.2. The peak area of each characteristic peptide was determined, and the RSD (n=6) of the quantitative ion pair peak area was calculated to be less than 3.2%, indicating that the method has good repeatability.
[0072] 2.7.7 Sample recovery rate
[0073] Accurately weigh 6 portions of camel hide glue powder of known content, each portion is about 0.1g, and place them in 10mL volumetric flasks respectively. Add 8mL of 1% ammonium bicarbonate solution, and ultrasonically treat for 30min (power 250W, frequency 40kHz) to completely dissolve the sample, then dilute to the scale with 1% ammonium bicarbonate solution, shake well, take 0.5mL of the above solution and place it in a 10mL volumetric flask, add 0.1g of donkey-hide glue control medicinal powder, and then accurately add mixed reference solution of specific concentration, add 8mL of 1% ammonium bicarbonate solution, and ultrasonically treat for 30min to completely dissolve the sample, then dilute to the scale with 1% ammonium bicarbonate solution, and make a solution from "shake well" under "2.1.2", and analyze according to the conditions under 2.5.2, record the peak area of each chromatographic peak, and calculate the sample recovery and RSD of each component, see Table 3. The average recoveries of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 were 99.9% to 103.8%, and the RSDs were 3.9% to 4.3%, indicating that the method had good accuracy.
[0074] Table 3 Camel hide glue characteristic polypeptide sample recovery rate
[0075]
[0076] 2.7.8 Investigation of the determination limit of camel-derived characteristic peptides
[0077] Weigh about 0.1g of 6 batches of camel skin glue powder made in the laboratory respectively, and prepare camel skin glue reference solution according to the method under 2.4. The quantitative ion pairs of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 were used for detection, and the peak areas were substituted into the linear equations of camel-derived characteristic peptide 1 and camel-derived characteristic peptide 2 for calculation. The contents of camel-derived characteristic peptide 1 corresponding to the 6 batches of samples were between 12.87 and 14.66μg / g, and the contents of camel-derived characteristic peptide 2 were between 12.68 and 13.86μg / g. Therefore, the detection limit of camel-derived characteristic peptide 1 is 14.66μg / g, and the detection limit of camel-derived characteristic peptide 2 is 13.86μg / g.
[0078] 2.7.9 Sample measurement results
[0079] Accurately weigh 0.10 g of donkey-hide gelatin powder from different batches, prepare the test solution according to the method in 2.1.2, and analyze it under the conditions in 2.5.2. As a result, only the two batches of homemade adulterated samples, S43 and S44, were found to contain camel skin adulteration.
[0080] Finally, it should be pointed out that the above embodiments are only representative examples of the present application. Obviously, the technical solution of the present application is not limited to the above embodiments, and there may be many variations. All variations that can be directly derived or associated with the contents disclosed in the present application by a person of ordinary skill in the art should be considered as the protection scope of the present application.
Claims
1. A camel-derived characteristic peptide, characterized in that: The characteristic peptide segment is: Characteristic peptide 1: GEAGPAGAAGPAGPR.
2. A camel-derived characteristic peptide, characterized in that: The characteristic peptide segment is: Characteristic peptide 2: GPSGPQGTR.
3. The method for detecting camel-derived characteristic peptides according to claim 1 or 2, characterized in that: The following steps are involved: (1) preparing a reference solution of the camel-derived characteristic peptide according to claim 1 or 2; (2) Ultra-high performance liquid chromatography-tandem mass spectrometry is used to measure the test samples and reference substances; (3) If a chromatographic peak with the same retention time as that in the reference solution appears at the position corresponding to the retention time, the camel-derived characteristic peptide is detected; if no corresponding chromatographic peak appears at the position corresponding to that in the reference solution, the camel-derived characteristic peptide is not detected.
4. The detection method according to claim 3, characterized in that: The reference substance solution is obtained by dissolving the camel-derived characteristic peptide in 1% ammonium bicarbonate solution.
5. The detection method according to claim 3, characterized in that: The ultra-high performance liquid chromatography tandem mass spectrometry technique specifically uses Waters BEH C 18 (2.1 mm × 50 mm, 1.7 μm) column; the guard column is Waters Van GuardBEH C 18 (2.1 mm × 5 mm, 1.7 μm) column; column temperature 40 °C; Mobile phase: 0.2% formic acid water (A)-0.2% formic acid acetonitrile (B), gradient elution: 0-0.5 min, 5% B; 0.5-3.0 min, 5%-30% B; 3.0-3.5 min, 30%-95% B; 3.5-4.0 min, 95% B; flow rate 0.3 mL / min, injection volume 5 μL; multiple reaction monitoring in electrospray ionization positive ion mode, capillary voltage 3.0 kV, ion source temperature 150°C, spray gas and backflush gas: N2, desolvation gas flow rate 1000 L / h, desolvation gas temperature 500°C, mass spectrometry data acquisition and processing software is MassLynxV4.1 workstation.
6. The detection method according to claim 4, characterized in that: The ion pairs and mass spectrometry conditions of the characteristic peptides are as follows:
7. Use of the camel-derived characteristic peptide according to claim 1 or 2 in detecting and identifying camel-derived components.
8. The use according to claim 7, characterized in that: The detection and identification of camel-derived components is to detect whether the donkey-hide gelatin contains camel-derived components.
9. The use according to claim 7, characterized in that: The detection and identification of camel-derived ingredients is to detect and identify whether camel skin ingredients are contained.
10. A method for detecting and identifying whether a product contains bovine-derived ingredients, characterized in that: The sample to be tested is tested using the detection method as described in claim 2. If the camel-derived characteristic peptide is detected, the sample contains camel-derived components; if the camel-derived characteristic peptide is not detected, the sample does not contain camel-derived components.