Antibacterial peptides for maintaining scalp microbiota health and methods of making and using the same

Abstract

The present application relates to the technical field of antibacterial peptides, and particularly relates to an antibacterial peptide for maintaining scalp microbial flora health, a preparation method and application thereof.The antibacterial peptide for maintaining scalp microbial flora health comprises the following: a polypeptide with an amino acid sequence comprising SEQ ID NO.1 or SEQ ID NO.2; or a polypeptide with an amino acid sequence consisting of the amino acid residues shown in SEQ ID NO.1 or SEQ ID NO.2; or a polypeptide with 99% or more, 95% or more, 90% or more, 85% or more, or 80% or more homology with the amino acid sequence defined above.The antibacterial peptide for maintaining scalp microbial flora health has good safety and can be used for treating scalp problems such as dandruff, seborrheic dermatitis, scalp itching and hair loss caused by scalp microbial flora imbalance.

Description

TECHNICAL FIELD

[0001] The application belongs to the technical field of antibacterial peptides, and particularly relates to an antibacterial peptide for maintaining the health of scalp microbial flora, and a preparation method and application thereof. BACKGROUND

[0002] The scalp is a unique niche, with characteristics such as dense hair, a large number of sweat glands, sebaceous glands, and high relative humidity, which create suitable conditions for the colonization and growth of microorganisms. The exfoliated keratinocytes, mineral ions produced by sweat gland secretion, and fats produced by sebaceous gland secretion provide abundant nutrients for microorganisms. The normal scalp microbiota is mainly composed of bacteria and fungi, with a colonization density of 10 3 -10 5 per square millimeter, mainly including Staphylococcus, Propionibacterium, and Malassezia, etc.

[0003] When the scalp microecological environment is destroyed and imbalanced, the scalp microecology is imbalanced, the biodiversity of the scalp microbiome decreases, the flora structure changes, and the host skin function and metabolic activity are abnormal, thereby causing a series of scalp problems and scalp diseases, such as dandruff, seborrheic dermatitis, scalp itching, and hair loss, etc.

[0004] As a new type of antibacterial agent, antibacterial peptides have a wide source, have broad-spectrum antibacterial activity, and compared with traditional antibiotics, most of the antibacterial peptides mainly kill bacteria by destroying bacterial cell membranes, and are not easy to make bacteria resistant, and are considered to be good antibiotic substitutes. Natural antibacterial peptides have high production cost, low antibacterial activity, and poor stability, and cannot meet the needs of actual application. With the continuous in-depth study of the properties, structure, and mechanism of action of existing natural antibacterial peptides, more and more research focuses on the development of artificial synthetic antibacterial peptides, and researchers have successfully used various modern biological technologies to improve or synthesize new antibacterial peptides. At present, there are few studies on antibacterial peptides for maintaining the health of scalp microbial flora. SUMMARY

[0005] In order to solve the problems in the prior art, the first aspect of the present application provides an antibacterial peptide for maintaining the health of scalp microbial flora, the antibacterial peptide being any one of the following (a)-(e) polypeptide:

[0006] (a) a polypeptide whose amino acid sequence comprises or consists of the amino acid residues shown in SEQ ID NO. 1;

[0007] (b) a polypeptide whose amino acid sequence comprises or consists of the amino acid residues shown in SEQ ID NO. 2;

[0008] (c) a polypeptide formed by substitution and / or deletion and / or addition of one or more amino acid residues in the amino acid sequence defined in (a) or (b);

[0009] (d) a polypeptide obtained by acetylation modification of the N-terminus and / or C-terminus of the polypeptide defined in (a) or (b);

[0010] (e) a polypeptide having 99% or more, 95% or more, 90% or more, 85% or more, or 80% or more homology with the amino acid sequence defined in (a) or (b).

[0011] Further preferably, the antibacterial peptide is any one of P7, P7L, P7K, P7R, P7I, or P7F.

[0012] Preferably, the antibacterial peptide P7 has an amino acid sequence as shown in SEQ ID NO. 1;

[0013] The antibacterial peptide P7L has an amino acid sequence as shown in SEQ ID NO. 3;

[0014] The antibacterial peptide P7K has an amino acid sequence as shown in SEQ ID NO. 4.

[0015] Preferably, the antibacterial peptide P7R has an amino acid sequence as shown in SEQ ID NO. 5;

[0016] The antibacterial peptide P7I has an amino acid sequence as shown in SEQ ID NO. 6;

[0017] The antibacterial peptide P7F has an amino acid sequence as shown in SEQ ID NO. 7.

[0018] Preferably, the antibacterial peptide is any one of P16, P16L, P16K, P6R, P16I, or P16V.

[0019] Preferably, the antibacterial peptide P16 has an amino acid sequence as shown in SEQ ID NO. 2;

[0020] The antibacterial peptide P16L has an amino acid sequence as shown in SEQ ID NO. 8;

[0021] The antibacterial peptide P16K has an amino acid sequence as shown in SEQ ID NO. 9.

[0022] Preferably, the antibacterial peptide P16R has an amino acid sequence as shown in SEQ ID NO. 10;

[0023] The antibacterial peptide P16I has an amino acid sequence as shown in SEQ ID NO. 11;

[0024] The amino acid sequence of the antibacterial peptide P16V is shown as SEQ ID NO. 12.

[0025] The second aspect of the present application provides a preparation method of an antibacterial peptide for maintaining scalp microbial flora health, which is a solid-phase synthesis method.

[0026] The third aspect of the present application provides an antibacterial peptide for maintaining scalp microbial flora health, and a product for preventing or treating scalp diseases.

[0027] Preferably, the skin diseases include dandruff, seborrheic dermatitis, tinea versicolor, and Malassezia folliculitis caused by fungal infection.

[0028] Preferably, the product is any one of a scalp care product, a hair conditioner, a shampoo, and a topical medicine.

[0029] The present application has the following beneficial effects:

[0030] The present application designs and synthesizes an antibacterial peptide for maintaining scalp microbial flora health, which is safe and can be used to treat dandruff, seborrheic dermatitis, scalp itching, and hair loss caused by scalp microbial flora imbalance; the antibacterial peptide can be applied to a scalp care product, a hair conditioner, a shampoo, or a topical medicine for treating dandruff or seborrheic dermatitis, scalp itching, and hair loss. The antibacterial peptide has a significant inhibitory effect on Malassezia furfur, Malassezia restricta, Staphylococcus hominis, Candida albicans, and Staphylococcus aureus, and a weak inhibitory effect on Lactobacillus acidophilus, thereby being more conducive to maintaining scalp microbial flora health and having great application value. BRIEF DESCRIPTION OF DRAWINGS

[0031] Figure 1A and Figure 1B are the antibacterial results of different antibacterial peptides of the present application in Malassezia furfur ATCC44344 with an addition amount of 10 μg / mL and 20 μg / mL and detected after incubation for 48 h and 72 h, respectively;

[0032] Figure 2A and Figure 2B are the antibacterial results of different antibacterial peptides of the present application in Malassezia restricta with an addition amount of 10 μg / mL and 20 μg / mL and detected after incubation for 48 h and 72 h, respectively;

[0033] Figure 3A and Figure 3BFigures 1-8 are graphs showing the antibacterial results of different antibacterial peptides of the present application in Staphylococcus hominis, Candida albicans, Staphylococcus aureus, and Lactobacillus acidophilus, respectively, at an additive amount of 10 μg / mL, 20 μg / mL, 40 μg / mL, 100 μg / mL, and 10 μg / mL, 20 μg / mL, 40 μg / mL, respectively, and after incubation for 24 h, 48 h, 72 h, and 24 h, respectively.

[0034] Figure 4 Figures 1-8 are graphs showing the antibacterial results of different antibacterial peptides of the present application in Staphylococcus hominis, Candida albicans, Staphylococcus aureus, and Lactobacillus acidophilus, respectively, at an additive amount of 10 μg / mL, 20 μg / mL, 40 μg / mL, 100 μg / mL, and 10 μg / mL, 20 μg / mL, 40 μg / mL, respectively, and after incubation for 24 h, 48 h, 72 h, and 24 h, respectively.

[0035] Figure 5 Figures 1-8 are graphs showing the antibacterial results of different antibacterial peptides of the present application in Staphylococcus hominis, Candida albicans, Staphylococcus aureus, and Lactobacillus acidophilus, respectively, at an additive amount of 10 μg / mL, 20 μg / mL, 40 μg / mL, 100 μg / mL, and 10 μg / mL, 20 μg / mL, 40 μg / mL, respectively, and after incubation for 24 h, 48 h, 72 h, and 24 h, respectively.

[0036] Figure 6A and Figure 6B Figures 1-8 are graphs showing the antibacterial results of different antibacterial peptides of the present application in Staphylococcus hominis, Candida albicans, Staphylococcus aureus, and Lactobacillus acidophilus, respectively, at an additive amount of 10 μg / mL, 20 μg / mL, 40 μg / mL, 100 μg / mL, and 10 μg / mL, 20 μg / mL, 40 μg / mL, respectively, and after incubation for 24 h, 48 h, 72 h, and 24 h, respectively. DETAILED DESCRIPTION

[0037] In order to make the objects, technical solutions, and advantages of the present application clearer, the technical solutions of the present application will be described in detail below. Obviously, the described embodiments are only a part of the embodiments of the present application, rather than all the embodiments. Based on the embodiments of the present application, all other embodiments obtained by those of ordinary skill in the art without creative work fall within the scope of the present application.

[0038] The first aspect of the present application provides an antibacterial peptide for maintaining scalp microbiota health, the antibacterial peptide being any one of the polypeptides in (a)-(e) below:

[0039] (a) a polypeptide having an amino acid sequence comprising or consisting of the amino acid residues set forth in SEQ ID NO. 1;

[0040] (b) a polypeptide having an amino acid sequence comprising or consisting of the amino acid residues set forth in SEQ ID NO. 2;

[0041] (c) a polypeptide formed by substitution and / or deletion and / or addition of one or more amino acid residues to the amino acid sequence defined in (a) or (b);

[0042] (d) a polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a) or (b);

[0043] (e) a polypeptide having 99% or more, 95% or more, 90% or more, 85% or more, or 80% or more homology with the amino acid sequence defined in (a) or (b).

[0044] Further preferably, the antibacterial peptide is any one of P7, P7L, P7K, P7R, P7I, P7F.

[0045] Preferably, the antibacterial peptide is P7, and the amino acid sequence of P7 is shown as SEQ ID NO. 1.

[0046] The amino acid sequence of the antibacterial peptide P7L is shown as SEQ ID NO. 3;

[0047] The amino acid sequence of the antibacterial peptide P7K is shown as SEQ ID NO. 4.

[0048] The amino acid sequence of the antibacterial peptide P7R is shown as SEQ ID NO. 5;

[0049] The amino acid sequence of the antibacterial peptide P7I is shown as SEQ ID NO. 6;

[0050] The amino acid sequence of the antibacterial peptide P7F is shown as SEQ ID NO. 7.

[0051] Further preferably, the antibacterial peptide is any one of P16, P16L, P16K, P6R, P16I, P16V.

[0052] The amino acid sequence of the antibacterial peptide P16 is shown as SEQ ID NO. 2;

[0053] The amino acid sequence of the antibacterial peptide P16L is shown as SEQ ID NO. 8;

[0054] The amino acid sequence of the antibacterial peptide P16K is shown as SEQ ID NO. 9.

[0055] The amino acid sequence of the antibacterial peptide P16R is shown as SEQ ID NO. 10;

[0056] The amino acid sequence of the antibacterial peptide P16I is shown as SEQ ID NO. 11;

[0057] The amino acid sequence of the antibacterial peptide P16V is shown as SEQ ID NO. 12.

[0058] The second aspect of the present application provides a preparation method of the antibacterial peptide for maintaining the health of scalp microbial flora, which is a solid-phase synthesis method.

[0059] The third aspect of the present application provides an application of the antibacterial peptide for maintaining the health of scalp microbial flora, which is applied to the preparation of a product for preventing or treating scalp diseases caused by imbalance of scalp microbial flora.

[0060] The product is any one of a scalp care product, a hair conditioner, a shampoo, and a topical medicine.

[0061] The above technical solutions are described in detail below in combination with specific embodiments.

[0062] In the following examples, the experimental methods used are conventional methods unless otherwise specified. In the following examples, the materials, reagents, etc. used are commercially available unless otherwise specified.

[0063] Example 1

[0064] The present embodiment provides an antibacterial peptide P7 for maintaining the health of scalp microbial flora, which has an amino acid sequence of KRKVRVALKVS, as shown in SEQ ID NO. 1.

[0065] The present embodiment further provides a preparation method of the antibacterial peptide, which adopts a solid-phase synthesis method, and the specific steps are as follows:

[0066] (1) The polypeptide synthesis sequence is from the C-terminal to the N-terminal: 20 g of AM resin is placed in a reaction tube, 15 mL / g of DCM (dichloromethane) is added, and shaken for 45 minutes; the solvent DCM is removed by sand core suction filtration, 3 times the molar excess of Fmoc-Linker-OH (CAS: 145069-56-3) is added, and 6.5 times the molar excess of DIEA (N,N-diisopropylethylamine) is added, and shaken for 75 minutes. Closed with methanol; rotary evaporation to remove DMF, add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes, then remove, and then add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 20 minutes. The resin is washed with DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g) in turn, and shaken for 40 minutes;

[0067] (2) The first amino acid is added: the solvent DCM is removed by sand core suction filtration, 3.5 times the molar excess of Fmoc-Ala-OH is added, and DMF (dimethylformamide) is added for dissolution, and then 6.5 times the molar excess of DIEA (N,N-diisopropylethylamine) is added, and shaken for 70 minutes. Closed with methanol.

[0068] (3) Deprotection: spin off DMF, add 20 mL / g 20% (V / V) piperidine-DMF solvent, wash for 5 minutes, remove, and then add 15 mL / g 20% (V / V) piperidine-DMF solvent, wash for 20 minutes.

[0069] (4) Detection: draw piperidine solution, take 15 resin particles, wash with ethanol three times, and then add detection reagent for detection. Heat at 105-110°C for 8 minutes, and then the color turns dark blue to be a positive reaction.

[0070] (5) Rinse resin: sequentially use DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g) to rinse the resin twice.

[0071] (6) Condensation: add a three-fold excess of DMF-dissolved next amino acid derivative (from C-terminal to N-terminal), add DMF-dissolved 3.5-fold excess of HBTU (benzotriazole-N,N,N',N'-tetramethyluronium hexafluorophosphate) in a reaction tube, and then immediately add DIEA in a molar amount of 16 times, and react for 40 minutes.

[0072] (7) Detection: take 15 resin particles, wash with ethanol three times, and then add detection reagent for detection. Heat at 105-110°C for 5 minutes, and then no color is a negative reaction.

[0073] (8) Rinse resin: sequentially use DMF (10 mL / g), DCM (10 mL / g), and DMF (10 mL / g) to rinse the resin twice.

[0074] (9) Repeat (3) to (8) to sequentially connect the amino acids shown in SEQ ID No. 1 from right to left.

[0075] (10) Dry, and then wash the resin according to the following method: DMF (15 mL / g) twice, methanol (15 mL / g) twice, DMF (15 mL / g) twice, DCM (15 mL / g) twice, and dry for 10 minutes.

[0076] (11) Cut the polypeptide from the resin: the composition of the cutting solution used at 25°C is 95% (V / V) TFA (trifluoroacetic acid), 1% (V / V) water, 2% (V / V) EDT (mercaptoethanol), and 2% (V / V) TIS (triisopropylsilane); the cutting time is 120 minutes, and the cleavage solution is obtained.

[0077] (12) Blow dry and wash: blow dry the cleavage solution with nitrogen, wash with ether six times, and then evaporate at room temperature.

[0078] (13) Analysis and purification of freeze-drying: the crude polypeptide was purified by high performance liquid chromatography; the polypeptide solution was collected and placed in a freeze dryer for concentration and freeze-drying to produce a white powder, obtaining an antibacterial peptide with the structure KRKVRVALKVS.

[0079] The detection reagent is indantrione.

[0080] Example 2

[0081] The present embodiment provides an antibacterial peptide P16 for maintaining scalp microbial flora health, which has an amino acid sequence of KWLKRIKKLFAN, as shown in SEQ ID NO. 2.

[0082] The present embodiment further provides a preparation method of the antibacterial peptide, which adopts a solid-phase synthesis method, and the specific steps are as follows:

[0083] (1) The polypeptide synthesis sequence is from the C-terminal to the N-terminal: 20 g of AM resin is placed in a reaction tube, 15 mL / g of DCM (dichloromethane) is added, and shaken for 45 minutes; the solvent DCM is removed by sand core suction filtration, 3 times molar excess of Fmoc-Linker-OH (CAS: 145069-56-3) is added, and 6.5 times molar excess of DIEA (N,N-diisopropyl ethylamine) is added, and shaken for 75 minutes. Closed with methanol; rotary evaporation to remove DMF, add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes, then remove, and add 20 mL / g of 20% (V / V) piperidine DMF solvent, wash for 20 minutes. The resin is washed with DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g) in turn, and shaken for 40 minutes;

[0084] (2) Add the first amino acid: remove the solvent DCM by sand core suction filtration, add 3.5 times molar excess of Fmoc-Ala-OH, dissolve in DMF (dimethylformamide), and add 6.5 times molar excess of DIEA (N,N-diisopropyl ethylamine), and shake for 70 minutes. Closed with methanol.

[0085] (3) Deprotection: rotary evaporation to remove DMF, add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes, then remove, and add 15 mL / g of 20% (V / V) piperidine DMF solvent, wash for 20 minutes.

[0086] (4) Detection: adjust the piperidine solution, take 15 resin particles, wash with ethanol three times, and add a detection reagent for detection. Heat at 105-110°C for 8 minutes, and the color turns dark blue, which is a positive reaction.

[0087] (5) Washing the resin: DMF (15 mL / g), DCM (15 mL / g), DMF (15 mL / g) twice, respectively.

[0088] (6) Condensation: add a three-fold excess of the next amino acid derivative (from C-terminal to N-terminal) dissolved in DMF, add 3.5-fold excess of HBTU (benzotriazole-N,N,N',N'-tetramethyluronium hexafluorophosphate) dissolved in DMF in the reaction tube, and immediately add 16-fold molar amount of DIEA, and react for 40 minutes.

[0089] (7) Detection: take 15 grains of resin, wash with ethanol three times, add a detection reagent for detection, heat at 105-110°C for 5 minutes, and if it is colorless, it is a negative reaction.

[0090] (8) Washing the resin: DMF (10 mL / g), DCM (10 mL / g), DMF (10 mL / g) twice, respectively.

[0091] (9) Repeat (3) to (8) to sequentially connect the amino acids shown in SEQ ID No. 2 from right to left.

[0092] (10) Dry and wash the resin according to the following method: DMF (15 mL / g) twice, methanol (15 mL / g) twice, DMF (15 mL / g) twice, DCM (15 mL / g) twice, and dry for 10 minutes.

[0093] (11) Cut the polypeptide from the resin: the composition of the cutting solution used at 25°C is: 95% (V / V) TFA (trifluoroacetic acid), 1% (V / V) water, 2% (V / V) EDT (mercaptoethanol), and 2% (V / V) TIS (triisopropylsilane); the cutting time is: 120 minutes, and the cleavage solution is obtained.

[0094] (12) Blow dry and wash: blow dry the cleavage solution with nitrogen, wash with ether six times, and then volatilize at room temperature.

[0095] (13) Analytical purification and freeze-drying: purify the polypeptide crude product by high-performance liquid chromatography; collect the polypeptide solution and place it in a freeze dryer for concentration and freeze-drying to produce a white powder, obtaining an antibacterial peptide with the structure KWLKRIKKLFAN.

[0096] The detection reagent is indanetrione.

[0097] Example 3

[0098] This example provides an antibacterial peptide P7L for maintaining the health of scalp flora, which is only different from Example 1 in that the amino acid sequence is KRKVRVLLKVS, as shown in SEQ ID No. 3.

[0099] Example 4

[0100] This example provides an antibacterial peptide P7K for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KRKVRVKLKVS, as shown in SEQ ID NO. 4.

[0101] Example 5

[0102] This example provides an antibacterial peptide P7R for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KRKVRVRLKVS, as shown in SEQ ID NO. 5.

[0103] Example 6

[0104] This example provides an antibacterial peptide P7I for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KRKVRVILKVS, as shown in SEQ ID NO. 6.

[0105] Example 7

[0106] This example provides an antibacterial peptide P7F for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KRKVRVFLKVS, as shown in SEQ ID NO. 7.

[0107] Example 8

[0108] This example provides an antibacterial peptide P16L for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KWLKRIKKLFLN, as shown in SEQ ID NO. 8.

[0109] Example 9

[0110] This example provides an antibacterial peptide P16K for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KWLKRIKKLFKN, as shown in SEQ ID NO. 9.

[0111] Example 10

[0112] This example provides an antibacterial peptide P16R for maintaining scalp microbiota health, which differs from Example 1 only in that its amino acid sequence is KWLKRIKKLFRN, as shown in SEQ ID NO. 10.

[0113] Example 11

[0114] The present example provides an antibacterial peptide P16I for maintaining scalp microbiota health, which is only different from example 1 in that the amino acid sequence thereof is KWLKRIKKLFIN, as shown in SEQ ID NO. 11.

[0115] Example 12

[0116] The present example provides an antibacterial peptide P16V for maintaining scalp microbiota health, which is only different from example 1 in that the amino acid sequence thereof is KWLKRIKKLFVN, as shown in SEQ ID NO. 12.

[0117] Experimental Example

[0118] 1. Bacteriostatic experiment

[0119] The bacteriostatic experiment of the antibacterial peptides described in examples 1-12 in liquid medium was detected, and the bacteria detected were Malassezia furfur ATCC 44344, Malassezia restricta ATCC 33081, Staphylococcus hominis (ATCC 23976), Candida albicans ATCC 14053, Staphylococcus aureus ATCC 25913, and Lactobacillus acidophilus ATCC 4356. CAP is chloramphenicol, KCZ is ketoconazole, and all are commercially available as a control group.

[0120] 2. Experimental results

[0121] The bacteriostatic experiment results on Malassezia furfur are shown in Figure 1A and Figure 1B After adding 10 μg / mL of antibacterial peptides and incubating for 48 hours and 72 hours, the inhibition rate of all antibacterial peptides on Malassezia furfur reached 100%. Similarly, after adding 20 μg / mL of antibacterial peptides and incubating for 48 hours and 72 hours, the inhibition rate of all antibacterial peptides on Malassezia furfur reached 100%.

[0122] The bacteriostatic results on Malassezia restricta are shown in Figure 2A and Figure 2BAs shown, after incubation with 10 μg / mL antimicrobial peptides for 48 hours, the inhibition rates of antimicrobial peptides P7L, P7K, P7R, P7I, P7F, P16L, and P16R against Malassezia restriction bacteria reached 100%; after continuous incubation for 72 hours, the inhibition rates of P7K, P7R, P7F, P16L, and P16R against Malassezia restriction bacteria remained unchanged at 100%. Similarly, after incubation with 20 μg / mL antimicrobial peptides for 48 hours, the inhibition rates of antimicrobial peptides P7, P16, P7L, P7K, P7R, P7I, P16L, P16K, P16R, P16I, and P16V against Malassezia restriction bacteria reached 100%; after continuous incubation for 72 hours, the inhibition rates of antimicrobial peptides P7, P7L, P7K, P7R, P7I, P16L, P6K, and P16R against Malassezia restriction bacteria remained at 100%.

[0123] The antibacterial results against Staphylococcus aureus are as follows: Figure 3A and Figure 3B As shown, after incubation with 10 μg / mL and 20 μg / mL antimicrobial peptides for 24 hours, all antimicrobial peptides achieved 100% inhibition against Staphylococcus aureus. After continuous incubation for 48 hours, all antimicrobial peptides achieved 100% inhibition against Staphylococcus aureus.

[0124] The antibacterial results against Candida albicans are as follows: Figure 4 As shown, after incubation with 10 μg / mL antimicrobial peptides for 24 hours, the inhibition rate of the antimicrobial peptides against P16, P7K, P7R, P7I, P16L, P16K, P16R, P16I, and P16V of Candida albicans reached 100%.

[0125] The antibacterial results against Staphylococcus aureus are as follows: Figure 5 As shown, after incubation with 100 μg / mL antimicrobial peptides for 24 hours, the inhibition rate of antimicrobial peptides P7K, P7R, P7I, P16L, P16R, and P16I against Staphylococcus aureus reached 100%.

[0126] The antibacterial results against Lactobacillus acidophilus are as follows: Figure 6A and 6B As shown, after incubation with 10 μg / mL, 20 μg / mL, and 40 μg / mL antimicrobial peptides for 48 hours and 72 hours, the inhibition rate of all antimicrobial peptides against Lactobacillus acidophilus was less than 30%.

[0127] The application designs and synthesizes an antibacterial peptide for maintaining scalp flora health, which is safe and can be used for treating scalp problems such as dandruff, seborrheic dermatitis, scalp itching and hair loss caused by scalp flora imbalance; the antibacterial peptide can be applied to dandruff-repelling or seborrheic dermatitis, scalp itching and hair loss treating scalp care products, hair conditioners, shampoo or external use medicines. The antibacterial peptide has significant bacteriostatic effect on Pityrosporum ovale, Pityrosporum restrictum, Staphylococcus hominis, Candida albicans and Staphylococcus aureus, and weak inhibitory effect on Lactobacillus acidophilus, thereby being more conducive to maintaining scalp flora health and having great application value.

[0128] The above is only a specific embodiment of the application, but the protection scope of the application is not limited thereto, any person skilled in the art can easily think of changes or replacements within the technical range disclosed by the application, which should be covered within the protection scope of the application. Therefore, the protection scope of the application should be subject to the protection scope of the claims.

Claims

1. An antimicrobial peptide for maintaining healthy scalp flora, characterized in that, The antimicrobial peptide is any of the following polypeptides: (a) The antimicrobial peptide is P16, and the amino acid sequence of the antimicrobial peptide P16 is shown in SEQ ID NO. 2; (b) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a).

2. An antimicrobial peptide for maintaining a healthy scalp microbiota, characterized in that, (a) The antimicrobial peptide is P16L, and the amino acid sequence of the antimicrobial peptide P16L is shown in SEQ ID NO. 8; (b) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a).

3. An antimicrobial peptide for maintaining healthy scalp flora, characterized in that, (a) The antimicrobial peptide is P16K, and the amino acid sequence of the antimicrobial peptide P16K is shown in SEQ ID NO. 9; (b) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a).

4. An antimicrobial peptide for maintaining healthy scalp flora, characterized in that, (a) The antimicrobial peptide is P16R, and the amino acid sequence of the antimicrobial peptide P16R is shown in SEQ ID NO. 10; (b) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a).

5. An antimicrobial peptide for maintaining healthy scalp flora, characterized in that, (a) The antimicrobial peptide is P16I, and the amino acid sequence of the antimicrobial peptide P16I is shown in SEQ ID NO. 11; (b) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a).

6. An antimicrobial peptide for maintaining a healthy scalp microbiota, characterized in that, (a) The antimicrobial peptide is P16V, and the amino acid sequence of the antimicrobial peptide P16V is shown in SEQ ID NO. 12; (b) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a).

7. A method for preparing an antimicrobial peptide for maintaining scalp microbiota health as described in any one of claims 1-6, characterized in that, The preparation method is a solid-phase synthesis method.

8. The use of the antimicrobial peptide according to any one of claims 1-6 in the preparation of the following products, characterized in that, The product is any one of the following: scalp care products, hair conditioner, shampoo, and topical medicines.

9. The use of the antimicrobial peptide according to any one of claims 1-6 in the preparation of skin care products.

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