CN115819498A - Blood brain barrier penetrating antioxidant polypeptide and preparation method and application thereof - Google Patents
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Abstract
The invention discloses an antioxidant polypeptide penetrating through a blood brain barrier, and a preparation method and application thereof, and belongs to the technical field of preparation of functional active peptides. The amino acid sequence of the polypeptide is one or more of SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 or SEQ ID NO. 5. The antioxidant polypeptide obtained by fermenting yak milk with lactobacillus plantarum JLAU103 has high antioxidant activity, can penetrate through a blood brain barrier and enter the brain to exert the functional activity of the yak milk, can be widely applied to preparation of anti-aging functional foods, health-care products and skin-care cosmetics, can be obtained by solid-phase chemical synthesis, and has good application prospect.
Description
Technical Field
The invention relates to an antioxidant polypeptide penetrating blood brain barrier and a preparation method and application thereof, belonging to the technical field of preparation of functional active peptides.
Background
Oxidation can cause rapid reaction of body functions, when oxidation and antioxidation in a body are unbalanced and tend to be oxidized, neutrophil inflammatory infiltration can be caused, protease secretion is increased, a large number of oxidation intermediate products such as free radicals and the like are generated, the original environment of normal metabolism of the human body is damaged, the body is damaged, and the microenvironment of the human body is changed. The change is considered to be an important factor causing aging and diseases, and brain tissues, which are the most active organs of the body in oxidative metabolism, are more easily attacked by active oxygen, so that the imbalance of an oxidation-oxidation resistance system in cells is caused, neuroinflammation and apoptosis are induced, mitochondrial functions are damaged, synaptic plasticity dysfunction, blood brain barrier integrity damage, toxic edema of neurons, DNA oxidative damage, protein expression abnormality and the like are caused, and further, the neurons are damaged, learning and memory ability is reduced, and the serious patient gradually develops dementia. Under certain conditions, the peptide bonds of proteins are broken down to form protein hydrolysates with antioxidant properties, which contain only a few hydrophobic or other types of amino acids, called antioxidant peptides, which regulate the availability of the body, bind to free radicals and scavenge free radicals, thus protecting human tissues and organs from excess free radicals.
The Blood Brain Barrier (BBB) is a specific defense mechanism of the central nervous system of mammals, and can prevent pathogenic factors (including bacterial and viral pathogens) in the peripheral system from entering the brain tissue from the blood, maintain the normal physiological functions of the brain, and selectively transport nutrients from the peripheral system to the central nervous system. Thus, the structure of the BBB differs from the peripheral vascular system. First, the tight junctions and adhesion junctions of the BBB confer megaohm (m Ω) resistance and prevent entry of molecules greater than 500Da, and the matrix proteins, pericytes and astrocyte ends further increase the resistance of the BBB. Therefore, selective transport of the blood-brain barrier prevents the intracerebral delivery of many neuroprotective factors while maintaining a relatively stable milieu within the nervous system. Almost all macromolecular substances and 98% small molecular substances are difficult to cross the blood-brain barrier. The problem that the antioxidant peptide passes through a blood brain barrier is firstly solved to realize the protection of brain tissues by utilizing the antioxidant peptide.
Disclosure of Invention
The invention aims to overcome the defects of the prior art and provides an antioxidant polypeptide capable of penetrating through a blood brain barrier, and a preparation method and application thereof.
The purpose of the invention is realized by the following technical scheme: the antioxidant polypeptide penetrating through the blood brain barrier comprises one or more of amino acid sequences of SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 or SEQ ID NO. 5.
It is another object of the present invention to provide a method for preparing the above blood-brain barrier penetrating antioxidant polypeptide, comprising the steps of:
s1, inoculating lactobacillus plantarum JLAU103 into yak milk, fermenting for 16-20 hours, performing solid-liquid separation, and taking supernatant;
s2, carrying out ultrafiltration treatment on the supernatant obtained in the S1, and collecting fermentation supernatant with the molecular weight less than 3 kDa;
s3, performing gel chromatography on the fermentation supernatant collected in the S2, and collecting the components with the retention time of 17000-20000S; and (3) carrying out gel chromatography purification again on the collected components, wherein the particle size of gel used for purification is smaller than that used for gel chromatography for the first time, and collecting the components with the retention time of 8000-9000 s to obtain the antioxidant polypeptide.
Further, lactobacillus plantarum JLAU103 inoculated in S1 is obtained by inoculating and fermenting a yak seed culture medium, wherein the yak seed culture medium is an MRS culture medium added with yak fresh milk, the inoculation amount is 1-3%, and the volume ratio of the yak milk seed culture medium to the yak milk is 1:9 to 11.
Further, the lactobacillus plantarum JLAU103 inoculated in the yak seed culture medium is subjected to 1-3 times of recovery in a liquid MRS culture medium, and the recovery time is 20-28 h.
Further, solid-liquid separation in the step S1 adopts centrifugal treatment, the centrifugal rotating speed is 5000rpm/min, and the centrifugal time is 10-15 min.
Further, sephadexG-25 is adopted in the first gel chromatography in S3, and SephadexG-15 is adopted in the purification.
Further, in S3, the elution flow rate of the first gel chromatography is 1.25mL/min, the detection wavelength is 280nm, and the peak component in the retention time is collected.
Further, in S3, the purification elution flow rate is 0.5mL/min, the detection wavelength is 280nm, and the peak component in the retention time is collected. And identifying the optimal component in the components collected after purification through mass spectrometry, wherein the optimal component is the amino acid sequence recorded in the invention.
The invention also provides the method for the anti-oxidation polypeptide penetrating through the blood brain barrier, and the anti-oxidation polypeptide is synthesized by solid phase chemistry according to the amino acid sequence.
The invention also provides application of the anti-oxidation polypeptide penetrating through the blood brain barrier in preparing functional foods, health-care products and skin-care cosmetics.
The invention has the beneficial effects that:
the antioxidant polypeptide obtained by fermenting yak milk with lactobacillus plantarum has high antioxidant activity, can penetrate through a blood brain barrier and enter the brain to exert the functional activity of the antioxidant polypeptide, improves the learning and memory ability of a user, and protects neurons and synapses from being damaged. The antioxidant polypeptide can be widely applied to preparation of anti-aging functional foods, health care products and skin care cosmetics, can be obtained through solid-phase chemical synthesis, and has good application prospects.
Drawings
FIG. 1 is the sequence information of an antioxidant polypeptide according to an embodiment of the present invention.
FIG. 2 shows the structure of an antioxidant polypeptide according to an embodiment of the present invention.
FIG. 3 is an elution diagram of the first chromatography in the second S3 of the present invention.
FIG. 4 shows the antioxidant activity of each peak component in the first chromatography in the second S3 of the present invention.
FIG. 5 is an elution diagram of purification chromatography in second S3 of example of the present invention.
FIG. 6 shows the antioxidant activity of each peak fraction in the purification chromatography in the second S3 of the present invention.
FIG. 7 shows the antioxidant activity of the polypeptide prepared in the third embodiment of the present invention.
FIG. 8 is a graph showing the blood-brain barrier penetrating ability of a LYLKPR polypeptide prepared according to example three of the present invention.
Detailed Description
The technical solutions of the present invention will be described clearly and completely with reference to the following embodiments, and it should be apparent that the described embodiments are only a part of the embodiments of the present invention, and not all of the embodiments. All other embodiments, which can be obtained by a person skilled in the art without inventive effort based on the embodiments of the present invention, are within the scope of the present invention.
Example one
This example provides a blood brain barrier-penetrating antioxidant polypeptide, which has an amino acid sequence of SEQ ID No.1 (Glu-Leu-Pro (ELPP) whose sequence information and structure are shown as a in fig. 1 and fig. 2), SEQ ID No.2 (Phe-Asp-Gly-Asp-Phe (FDGDF) whose sequence information and structure are shown as b in fig. 1 and fig. 2), SEQ ID No.3 (Leu-Tyr-Leu-Lys-Pro-Arg (LYLKPR) whose sequence information and structure are shown as c in fig. 1 and fig. 2), SEQ ID No.4 (Leu-Gly-Asp-Lys-Leu-Phe (lgdkf) whose sequence information and structure are shown as d in fig. 1 and fig. 2), SEQ ID No.5 (Lys-Leu-Val-Ala-Trp-Val-Pro (lvklawvpp) whose sequence information and structure are shown as e in fig. 1 and fig. 2, respectively.
Example two
This example provides a method for preparing an antioxidant polypeptide that penetrates the blood-brain barrier, comprising the steps of:
s1, firstly putting the lactobacillus plantarum JLAU103 in a liquid MRS culture medium for resuscitation for 24 hours, resuscitating for three times, wherein the inoculation ratio of each time is 1%. And then adding the fresh yak milk into an MRS culture medium to prepare a yak seed culture medium (the volume ratio of the added fresh yak milk to the MRS culture medium is 10: 1), and inoculating the recovered lactobacillus plantarum JLAU103 into the yak seed culture medium according to the inoculation amount of 1% for fermentation for 24h. Mixing the fermentation product with yak milk according to the proportion of 1:10, inoculating lactobacillus plantarum JLAU103 into yak milk, fermenting for 18 hours, centrifuging at 5000rpm/min for 15min, and collecting the centrifuged supernatant.
And S2, carrying out ultrafiltration treatment on the supernatant obtained in the S1 in ice bath, adopting a tangential flow ultrafiltration system and a Biomax modified polyether sulfone composite membrane, adopting an ultrafiltration membrane with the molecular weight cutoff of the membrane being 3kDa for separation, and collecting the fermentation supernatant with the molecular weight being less than 3 kDa.
And S3, performing gel chromatography on the fermentation supernatant collected in the S2, wherein the chromatography adopts SephadexG-25, the mass concentration of a sample is 100mg/mL, the loading amount is 10mL, the elution flow rate is 1.25mL/min, the detection wavelength is 280nm, and the elution diagram is shown in figure 3, wherein the component of F1 is not in the target retention time, and the component of F2 is in the retention time period of 17000-20000S. And (3) carrying out gel chromatography purification again on the collected components, wherein the purification adopts SephadexG-15, the mass concentration of the sample is 50mg/mL, the loading amount is 2.5mL, the elution flow rate is 0.5mL/min, the detection wavelength is 280nm, the elution diagram is shown in figure 5, wherein the components of C1 and C2 are not in the target retention time, the component of C3 is located in the retention time period of 8000-9000 s, the component of C3 is collected to be the antioxidant polypeptide, and the polypeptide screened by mass spectrometry is consistent with the amino acid sequence in the first embodiment.
EXAMPLE III
This example provides another method for preparing an antioxidant polypeptide capable of penetrating blood brain barrier, which comprises the steps of synthesizing the antioxidant polypeptide according to the amino acid sequence of example one by solid-phase chemistry, wherein the steps of the synthesis are as follows: fmoc solid phase synthesis was used and purification was performed using Gemini-NX 5. Mu.C 18110A, 4.6X 250mm liquid column. Mobile phase A:0.1% trichloroacetic acid and 100% acetonitrile; and (3) mobile phase B:0.1% trichloroacetic acid and 100% water.
Example four
This example provides assays for antioxidant activity of the antioxidant polypeptides prepared in examples two and three, including the following assays:
ABTS radical scavenging Activity
ABTS. Cndot. +, was generated by reaction of 7mM ATBTS with 2.49mM potassium persulfate in water and then stored at Room Temperature (RT) for 16 hours protected from light. ABTS + solution was diluted with ethanol to an absorbance of 0.70 at 734nm before use. The peptide sample solution (10. Mu.L, 1 mg/mL) was added to the 190 mLABTS. + solution and the mixture was incubated in the dark at room temperature for 5min. The absorbance of the mixed solution was measured at 734nm, and ABTS radical scavenging activity was calculated by the following formula using Glutathione (GSH) as a positive control:
ABTS clearance (%) =1- (A1-A2)/(A0-A3) × 100
Wherein, A0: distilled water + ABTS, A1: peptide sample solution + ABTS, A2: peptide sample solution + PBS, A3: distilled water + PBS.
The polypeptide sample solution is the polypeptide prepared in the third embodiment, and the calculation result is shown in fig. 7, the antioxidant polypeptides synthesized in the third embodiment of the invention all have ABTS free radical scavenging ability, wherein the polypeptide having LYLKPR (amino acid sequence SEQ ID No. 3) has a particularly significant antioxidant effect, the polypeptide having KLLVAWVPP (amino acid sequence SEQ ID No. 5) has an excellent antioxidant effect, and other polypeptides have certain antioxidant ability.
2. Hydroxyl radical scavenging Activity
Hydroxyl radical scavenging activity: 1mL of the peptide sample solution (8 mg/mL), 1.0mL of salicylic acid (0.435 mM), 2.0mL of LFeSO 4 (0.5 mM) and 1.5mLH 2 O 2 (3.0%, w/v) was added to the tube and mixed to start the reaction. The tubes were incubated at 37 ℃ for 30 minutes. Then, absorbance was measured at 510nm, and with GSH as a positive control, hydroxyl radical scavenging activity was calculated by the following formula:
hydroxyl radical scavenging activity (%) = [1- (A1-A2)/A0 ] × 100
Wherein, A0: h 2 O 2 +FeSO 4 + distilled water + salicylic acid, A1: h 2 O 2 +FeSO 4 + peptide sample solution + salicylic acid, A2: h 2 O 2 +FeSO 4 + peptide sample solution + ethanol. Adjusting 0 component by a spectrophotometer: h 2 O 2 +FeSO 4 + distilled water + ethanol.
The peptide samples used in this assay were all peak fractions collected from two gel chromatographs in preparation S3 of example two, and the calculations are shown in FIGS. 4 and 6. As can be seen from FIG. 4, of the peak components collected by the first gel chromatography in S3 of example two, the peak component (F2) having a retention time of 17000 to 20000S had a higher hydroxyl radical scavenging activity. FIG. 6 shows that the peak fractions collected by the purification gel chromatography in S3 of example two have higher hydroxyl radical scavenging activity for the peak fractions with different retention times.
3. Oxygen radical absorbance measurement (ORAC)
To each well of a 96-well fluorescent plate, 25. Mu.L of a sample to be tested (the peptide sample to be tested was dissolved in 75mmol/LPBS buffer solution at a sample concentration of 100 mmol/L), 25. Mu.L of 75mmol/L PBS buffer solution and 150. Mu.L of 63mmol/L sodium Fluorescein (FL), shaking for 10s,37 ℃ for Wen Yu for 20min, rapidly adding 25. Mu.L of 6mmol/L azobisisobutyramidine hydrochloride (AAPH, ready-to-use) to each well with a multiwell pipette gun to start the reaction, and placing the 96-well fluorescent plate in a preheated (37 ℃) fluorescence microplate analyzer, and measuring the fluorescence intensity of each well once every 4min at an excitation wavelength of 485nm and an emission wavelength of 538nm, and terminating the measurement when the fluorescence intensity is 5% of the initial fluorescence intensity. Calculating the area under the fluorescence decay curve (AUC) by adopting an approximate integration method relative to the fluorescence intensity:
AUC＝2×[(f0+f1+……+fn-1+fn)-f0-fn]/2×Δt
wherein fn is the relative fluorescence intensity of the nth measurement spot; Δ t is the interval time 4min between adjacent time points. The results of the measurement are expressed as ORAC values, and the ORAC values of the samples to be measured are expressed as umol/Trolox/g.
ORAC value = (AUC) Sample (I) -AUC Blank space )/(AUC trolox -AUC Blank space )×C sample/Ctrox
Wherein, AUC Sample (I) : area under the fluorescence decay Curve, AUC, of the sample Blank space : area under the fluorescence decay Curve, AUC, without sample addition trolox : area under the fluorescence decay curve of trolox standard.
The peptide samples used in this assay were all peak fractions collected from two gel chromatographs in preparation S3 of example two and the polypeptides prepared in example three, and the results of the calculations are shown in FIGS. 4, 6 and 7. As can be seen from fig. 4, of the peak components collected by the first gel chromatography in S3 of example two, the peak component (F2) having a retention time of 17000 to 20000S had a higher oxygen radical absorbance capacity. Fig. 6 shows that, among peak components collected by the purification gel chromatography in S3 of example two, the peak component (C3) having a retention time within a range of 8000 to 9000S has a stronger oxygen radical-absorbing ability. The calculation results in FIG. 7 show that LYLKPR (amino acid sequence SEQ ID NO. 3) has the best oxygen radical absorption capacity of polypeptide, and KLLVAWVPP (amino acid sequence SEQ ID NO. 5) is the next, and other polypeptides also have better oxygen radical absorption capacity and oxidation resistance.
4.Fe 2+ Chelating Activity
2.75mL of water, 1mL of the peptide sample solution (8 mg/mL), 0.2mL of the ferrozine solution (5 mM) and 0.05mL of FeCl 2 The solutions (4 mM) were mixed, shaken vigorously and incubated for 10 minutes at room temperature. The absorbance of the reaction mixture was measured at 562 nm. Fe 2+ The chelating activity was calculated from the following formula:
Fe 2+ chelating activity (%) = [ A0- (A1-Ai)/A0]×100
Wherein A0 is the absorbance of a mixed solution containing no peptide sample, and A1 is the absorbance of a mixed solution containing all the above componentsLuminosity, ai being FeCl-free 2 Absorbance of the mixed solution of (1).
The peptide samples used in this assay were all peak fractions collected from two gel chromatographs in preparation S3 of example two, and the results are shown in FIGS. 4 and 6. As can be seen from FIG. 4, of the peak components collected by the first gel chromatography in S3 of example two, the peak component (F2) having a retention time of 17000 to 20000S had a higher Fe content 2+ Chelating activity. FIG. 6 also shows that, among the peak components collected by the purification gel chromatography in S3 of example two, the peak component (C3) having a retention time of 8000 to 9000S had stronger Fe 2+ Chelating activity.
EXAMPLE five
This example provides the following specific measurement method for the blood-brain barrier penetration ability of the antioxidant polypeptide LYLKPR (amino acid sequence is SEQ ID NO. 3) prepared in the third example: using a transwell plate, 0.5ml of cultured BEND3 cells (5X 10 cells) was added to each upper well 4 Per well), 1.5ml of cell-free complete medium was added to the lower macropore. The culture medium is replaced every two days until the resistance value reaches 180 omega cm 2 It is demonstrated that the blood brain barrier reaches a stable state and the blood brain barrier model is established. 200 μ M peptide LYLKPR was added to the upper well for 2h, and the medium was removed from the small and large wells and subjected to reverse phase high performance liquid chromatography (RP-HPLC) to determine whether the peptide could cross the blood-brain barrier.
The results are shown in FIG. 8, where most LYLKPR polypeptides are able to cross the blood-brain barrier and enter the central nervous system of the brain to exert their antioxidant activity.
As can be seen from the fourth and fifth examples, the antioxidant polypeptide of the invention can be widely applied to the preparation of functional foods and health-care products for resisting aging and improving memory, and can also be used for preparing skin-care cosmetics for resisting aging
The foregoing is illustrative of the preferred embodiments of this invention, and it is to be understood that the invention is not limited to the precise form disclosed herein and that various other combinations, modifications, and environments may be resorted to, falling within the scope of the concept as disclosed herein, either as described above or as apparent to those skilled in the relevant art. And that modifications and variations may be effected by those skilled in the art without departing from the spirit and scope of the invention as defined by the appended claims.
Claims (10)
1. An antioxidant polypeptide that penetrates the blood brain barrier, characterized in that: comprises one or more of amino acid sequences SEQ ID NO.1, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 or SEQ ID NO. 5.
2. A method for preparing the blood-brain barrier penetrating antioxidant polypeptide of claim 1, characterized in that: the method comprises the following steps:
s1, inoculating lactobacillus plantarum JLAU103 into yak milk, fermenting for 16-20 hours, performing solid-liquid separation, and taking supernatant;
s2, carrying out ultrafiltration treatment on the supernatant obtained in the S1, and collecting fermentation supernatant with the molecular weight less than 3 kDa;
s3, performing gel chromatography on the fermentation supernatant collected in the S2, and collecting the components with the retention time of 17000-20000S; and (3) carrying out gel chromatography purification again on the collected components, wherein the particle size of gel used for purification is smaller than that used for gel chromatography for the first time, and collecting the components with the retention time of 8000-9000 s to obtain the antioxidant polypeptide.
3. The method for preparing a blood-brain barrier penetrating antioxidant polypeptide according to claim 1, wherein: the lactobacillus plantarum JLAU103 inoculated in the S1 is obtained by inoculating and fermenting a yak seed culture medium, wherein the yak seed culture medium is an MRS culture medium added with yak fresh milk, the inoculation amount is 1-3%, and the volume ratio of the yak milk seed culture medium to the yak milk is 1:9 to 11.
4. The method for preparing a blood-brain barrier penetrating antioxidant polypeptide of claim 3, wherein: and (3) recovering the lactobacillus plantarum JLAU103 inoculated in the yak seed culture medium for 1-3 times in a liquid MRS culture medium for 20-28 h.
5. The method for preparing a blood-brain barrier penetrating antioxidant polypeptide according to claim 1, wherein: and in the S1, solid-liquid separation adopts centrifugal treatment, the centrifugal rotation speed is 5000rpm/min, and the centrifugal time is 10-15 min.
6. The method for preparing a blood-brain barrier penetrating antioxidant polypeptide according to claim 1, wherein: in S3, sephadexG-25 is adopted for the first gel chromatography, and SephadexG-15 is adopted for the purification.
7. The method for preparing the blood brain barrier penetrating antioxidant polypeptide according to claim 1, wherein: and in S3, the elution flow rate of the first gel chromatography is 1.25mL/min, the detection wavelength is 280nm, and the peak component in the retention time is collected.
8. The method for preparing a blood-brain barrier penetrating antioxidant polypeptide according to claim 1, wherein: and in the S3, the purification elution flow rate is 0.5mL/min, the detection wavelength is 280nm, and the peak component in the retention time is collected.
9. A method for preparing the blood-brain barrier penetrating antioxidant polypeptide of claim 1, characterized in that: the amino acid sequence of claim 1 is synthesized by solid phase chemistry.
10. The use of the blood-brain barrier penetrating antioxidant polypeptide of claim 1 in the preparation of functional foods, health products and skin care cosmetics.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109666973A (en) * | 2018-11-21 | 2019-04-23 | 北京大学 | It is a kind of across the peptide library of blood-brain barrier and its screening technique |
| CN114288414A (en) * | 2021-12-07 | 2022-04-08 | 深圳先进技术研究院 | Polypeptide crossing blood brain barrier, derivative and application thereof |
| CN114751957A (en) * | 2022-03-15 | 2022-07-15 | 吉林农业大学 | Memory-improving derived peptide with high oxidation resistance and capability of penetrating blood brain barrier and application thereof |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109666973A (en) * | 2018-11-21 | 2019-04-23 | 北京大学 | It is a kind of across the peptide library of blood-brain barrier and its screening technique |
| CN114288414A (en) * | 2021-12-07 | 2022-04-08 | 深圳先进技术研究院 | Polypeptide crossing blood brain barrier, derivative and application thereof |
| CN114751957A (en) * | 2022-03-15 | 2022-07-15 | 吉林农业大学 | Memory-improving derived peptide with high oxidation resistance and capability of penetrating blood brain barrier and application thereof |
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