Antibacterial peptide for maintaining scalp flora health and preparation method and application thereof

Abstract

The invention relates to the technical field of antibacterial peptides, in particular to an antibacterial peptide for maintaining scalp flora health and a preparation method and application thereof. The antibacterial peptide for maintaining scalp flora health comprises a polypeptide of which the amino acid sequence comprises an amino acid sequence as shown in SEQ ID NO.1, and a polypeptide of which the amino acid sequence comprises an amino acid sequence as shown in SEQ ID NO.2; or a polypeptide of which the amino acid sequence is composed of amino acid residues as shown in SEQ ID NO.1; or a polypeptide having 99% or more, 95% or more, 90% or more, 85% or more or 80% or more homology with the defined amino acid sequence. The antibacterial peptide for maintaining scalp flora health is good in safety and can be used for treating scalp problems such as dandruff, seborrheic dermatitis, scalp itching and alopecia caused by scalp flora imbalance.

Description

[0001] This application is a divisional application of the application with the application date of September 12, 2024, application number CN202411281077.0, and invention name "An Antimicrobial Peptide for Maintaining the Health of Scalp Microbiota, Its Preparation Method and Application". Technical Field

[0002] The present invention belongs to the technical field of antimicrobial peptides, and specifically relates to an antimicrobial peptide for maintaining the health of scalp microbiota, its preparation method and application. Background Art

[0003] The scalp is a unique ecological niche. Characteristics such as dense hair, a large number of sweat glands, sebaceous glands, and high relative humidity create suitable conditions for the colonization and growth of microorganisms. Shed keratinocytes, mineral ions secreted by sweat glands, and fats secreted by sebaceous glands provide rich nutrient sources for microorganisms. The microbiota of normal scalp mainly consists of bacteria and fungi, etc., with a colonization density of 10 3 -10 5 per square millimeter, mainly including Staphylococcus, Propionibacterium, Malassezia, etc.

[0004] When the scalp microecological environment is damaged and imbalanced, the scalp microecology is out of balance, the biodiversity of the scalp microbiome decreases, the flora structure changes, and the host skin function and metabolic activities are abnormal, thus causing a series of scalp problems and scalp diseases, such as dandruff, seborrheic dermatitis, scalp itching, hair loss, etc.

[0005] As a new type of antibacterial agent, antimicrobial peptides have a very wide range of sources, have broad-spectrum antibacterial activity, and compared with traditional antibiotics, most antimicrobial peptides mainly kill bacteria by destroying the bacterial cell membrane and are not easily resistant to bacteria, and are considered good alternatives to antibiotics. The production cost of natural antimicrobial peptides is high, the antibacterial activity is low, and the stability is poor, which cannot meet the needs of practical applications. With the continuous in-depth study of the properties, structures and action mechanisms of existing natural antimicrobial peptides, more and more research focuses on the development of artificially synthesized antimicrobial peptides, and researchers have successfully used various modern biotechnology to molecularly modify antimicrobial peptides or synthesize new antimicrobial peptides. At present, there is less research on antimicrobial peptides for maintaining the health of scalp microbiota. Summary of the Invention

[0006] To solve the problems in the prior art, in the first aspect of the present invention, an antimicrobial peptide for maintaining the health of scalp microbiota is provided, and the antimicrobial peptide is any one of the following polypeptides (a)-(e):

[0007] (a) A polypeptide whose amino acid sequence includes the amino acid sequence shown in SEQ ID NO.1, or a polypeptide whose amino acid sequence is composed of the amino acid residues shown in SEQ ID NO.1;

[0008] (b) A polypeptide whose amino acid sequence includes the amino acid sequence shown in SEQ ID NO.2, or a polypeptide whose amino acid sequence consists of the amino acid residues shown in SEQ ID NO.2;

[0009] (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);

[0010] (d) A polypeptide obtained by acetylation modification of the N-terminus and / or C-terminus of the polypeptide defined in (a) or (b);

[0011] (e) A polypeptide having a homology of more than 99%, more than 95%, more than 90%, more than 85% or more than 80% with the amino acid sequence defined in (a) or (b).

[0012] Further preferably, the antimicrobial peptide is any one of P7, P7L, P7K, P7R, P7I, and P7F.

[0013] Preferably, the amino acid sequence of the antimicrobial peptide P7 is as shown in SEQ ID NO.1;

[0014] The amino acid sequence of the antimicrobial peptide P7L is as shown in SEQ ID NO.3;

[0015] The amino acid sequence of the antimicrobial peptide P7K is as shown in SEQ ID NO.4.

[0016] Preferably, the amino acid sequence of the antimicrobial peptide P7R is as shown in SEQ ID NO.5;

[0017] The amino acid sequence of the antimicrobial peptide P7I is as shown in SEQ ID NO.6;

[0018] The amino acid sequence of the antimicrobial peptide P7F is as shown in SEQ ID NO.7.

[0019] Preferably, the antimicrobial peptide is any one of P16, P16L, P16K, P6R, P16I, and P16V.

[0020] Preferably, the amino acid sequence of the antimicrobial peptide P16 is as shown in SEQ ID NO.2;

[0021] The amino acid sequence of the antimicrobial peptide P16L is as shown in SEQ ID NO.8;

[0022] The amino acid sequence of the antimicrobial peptide P16K is as shown in SEQ ID NO.9.

[0023] Preferably, the amino acid sequence of the antimicrobial peptide P16R is shown as SEQ ID NO.10;

[0024] the amino acid sequence of the antimicrobial peptide P16I is shown as SEQ ID NO.11;

[0025] the amino acid sequence of the antimicrobial peptide P16V is shown as SEQ ID NO.12.

[0026] The second aspect of the present invention provides a preparation method of an antimicrobial peptide for maintaining the health of scalp flora, and the preparation method is a solid-phase synthesis method.

[0027] The third aspect of the present invention provides an application of an antimicrobial peptide for maintaining the health of scalp flora, which is used for preparing products for preventing or treating scalp diseases.

[0028] Preferably, the skin diseases include dandruff, seborrheic dermatitis, pityriasis versicolor, Malassezia folliculitis caused by fungal infection;

[0029] Preferably, the product is any one of scalp care products, hair conditioners, shampoos, and topical medicines.

[0030] The beneficial effects of the present invention are as follows:

[0031] The present invention designs and synthesizes an antimicrobial peptide for maintaining the health of scalp flora, which has good safety and can be used to treat scalp problems such as dandruff, seborrheic dermatitis, scalp pruritus, and hair loss caused by scalp flora imbalance; the antimicrobial peptide can be applied to scalp care products, hair conditioners, shampoos, or topical medicines for removing dandruff or treating seborrheic dermatitis, scalp pruritus, and hair loss. The antimicrobial peptide of the present invention has significant antibacterial effects on Malassezia furfur, Malassezia restricta, Staphylococcus hominis, Candida albicans, and Staphylococcus aureus, while having a weak inhibitory effect on Lactobacillus acidophilus, thus being more conducive to maintaining the health of scalp flora and having great application value. Description of the Drawings

[0032] Figure 1A and Figure 1B are respectively the antibacterial test result graphs of different antimicrobial peptides of the present invention in Malassezia furfur ATCC44344 with the addition amounts of 10 μg / mL and 20 μg / mL and incubation for 48 h and 72 h;

[0033] Figure 2A and Figure 2B are respectively the antibacterial test result graphs of different antimicrobial peptides of the present invention in Malassezia restricta with the addition amounts of 10 μg / mL and 20 μg / mL and incubation for 48 h and 72 h;

[0034] Figure 3A and Figure 3B are respectively the bacteriostatic result graphs of different antimicrobial peptides of the present invention detected after adding 10 μg / mL and 20 μg / mL and incubating for 24 h and 48 h in Staphylococcus hominis;

[0035] Figure 4 is the bacteriostatic result graph of different antimicrobial peptides of the present invention detected after adding 10 μg / mL and incubating for 24 h in Candida albicans;

[0036] Figure 5 is the bacteriostatic result graph of different antimicrobial peptides of the present invention detected after adding 100 μg / mL and incubating for 24 h in Staphylococcus aureus;

[0037] Figure 6A and Figure 6B are respectively the bacteriostatic result graphs of different antimicrobial peptides of the present invention detected after adding 10 μg / mL, 20 μg / mL, 40 μg / mL and incubating for 48 h and 72 h in Lactobacillus acidophilus. Detailed implementation manners

[0038] To make the objectives, technical solutions and advantages of the present invention clearer, the technical solutions of the present invention will be described in detail below. Obviously, the described embodiments are only a part of the embodiments of the present invention, rather than all the embodiments. Based on the embodiments of the present invention, all other implementation manners obtained by those of ordinary skill in the art without making creative efforts fall within the scope protected by the present invention.

[0039] The first aspect of the present invention provides an antimicrobial peptide for maintaining the health of scalp flora, and the antimicrobial peptide is any one of the following polypeptides (a)-(e):

[0040] (a) A polypeptide whose amino acid sequence includes the amino acid sequence shown in SEQ ID NO.1, or a polypeptide whose amino acid sequence is composed of the amino acid residues shown in SEQ ID NO.1;

[0041] (b) A polypeptide whose amino acid sequence includes the amino acid sequence shown in SEQ ID NO.2, or a polypeptide whose amino acid sequence is composed of the amino acid residues shown in SEQ ID NO.2;

[0042] (c) A polypeptide formed by substituting and / or deleting and / or adding one or more amino acid residues to the amino acid sequence defined in (a) or (b);

[0043] (d) A polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a) or (b);

[0044] (e) A polypeptide having a homology of more than 99%, more than 95%, more than 90%, more than 85% or more than 80% with the amino acid sequence defined in (a) or (b).

[0045] More preferably, the antimicrobial peptide is any one of P7, P7L, P7K, P7R, P7I, and P7F.

[0046] Preferably, the amino acid sequence of the antimicrobial peptide P7 is as shown in SEQ ID NO.1.

[0047] The amino acid sequence of the antimicrobial peptide P7L is as shown in SEQ ID NO.3;

[0048] The amino acid sequence of the antimicrobial peptide P7K is as shown in SEQ ID NO.4.

[0049] The amino acid sequence of the antimicrobial peptide P7R is as shown in SEQ ID NO.5;

[0050] The amino acid sequence of the antimicrobial peptide P7I is as shown in SEQ ID NO.6;

[0051] The amino acid sequence of the antimicrobial peptide P7F is as shown in SEQ ID NO.7.

[0052] More preferably, the antimicrobial peptide is any one of P16, P16L, P16K, P6R, P16I, and P16V.

[0053] The amino acid sequence of the antimicrobial peptide P16 is as shown in SEQ ID NO.2;

[0054] The amino acid sequence of the antimicrobial peptide P16L is as shown in SEQ ID NO.8;

[0055] The amino acid sequence of the antimicrobial peptide P16K is as shown in SEQ ID NO.9.

[0056] The amino acid sequence of the antimicrobial peptide P16R is as shown in SEQ ID NO.10;

[0057] The amino acid sequence of the antimicrobial peptide P16I is as shown in SEQ ID NO.11;

[0058] The amino acid sequence of the antimicrobial peptide P16V is as shown in SEQ ID NO.12.

[0059] In the second aspect of the present invention, a method for preparing an antimicrobial peptide for maintaining the health of scalp flora is provided, and the preparation method is solid-phase synthesis method.

[0060] In the third aspect of the present invention, an application of an antimicrobial peptide for maintaining the health of scalp flora is provided, which is applied to the preparation of products for preventing or treating scalp diseases caused by the imbalance of scalp microbial flora;

[0061] The product is any one of scalp care products, hair conditioners, shampoos, and topical medications.

[0062] The above technical solutions will be described in detail below in conjunction with specific embodiments.

[0063] Unless otherwise specified, the experimental methods used in the following examples are all conventional methods. The materials, reagents, etc. used in the following examples can be obtained from commercial sources unless otherwise specified.

[0064] Example 1

[0065] This example provides an antimicrobial peptide P7 for maintaining the health of scalp flora, and its amino acid sequence is KRKVRVALKVS, as shown in SEQ ID NO.1.

[0066] This example further provides a preparation method of the antimicrobial peptide, which adopts the solid-phase synthesis method, and the specific steps are as follows:

[0067] (1) The polypeptide synthesis sequence is from the C-terminus to the N-terminus: Put 20 g of AM resin into a reaction tube, add 15 mL / g of DCM (dichloromethane), and shake for 45 minutes; Filter off the solvent DCM through a fritted filter, add 3-fold molar excess of Fmoc-Linker-OH (CAS: 145069-56-3), and then add 6.5-fold molar excess of DIEA (N,N-diisopropylethylamine), and shake for 75 minutes. Block with methanol; Evaporate DMF by rotary evaporation, add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes and then remove, and then add 20 mL / g of 20% (V / V) piperidine DMF solvent and wash for 20 minutes. Rinse the resin twice with DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g) respectively, and shake for 40 minutes;

[0068] (2) Connect the first amino acid: Filter off the solvent DCM through a fritted filter, add 3.5-fold molar excess of Fmoc-Ala-OH, dissolve in DMF (dimethylformamide), and then add 6.5-fold molar excess of DIEA (N,N-diisopropylethylamine), and shake for 70 minutes. Block with methanol.

[0069] (3) Deprotection: Evaporate DMF by rotary evaporation. Add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes, then discard. Add another 15 mL / g of 20% (V / V) piperidine-DMF solvent and wash for 20 minutes.

[0070] (4) Detection: Withdraw the piperidine solution. Take 15 resin beads, wash them three times with ethanol, and add the detection reagent for testing. Heat at 105 - 110 °C for 8 minutes. A dark blue color change indicates a positive reaction.

[0071] (5) Rinse the resin: Rinse the resin twice successively with DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g).

[0072] (6) Condensation: Add three-fold excess of the next amino acid derivative dissolved in DMF (from C-terminus to N-terminus), dissolve 3.5-fold excess of HBTU (benzotriazol-1-yloxytris(dimethylamino)phosphonium hexafluorophosphate) in DMF in the reaction tube, and immediately add 16-fold molar amount of DIEA. React for 40 minutes.

[0073] (7) Detection: Take 15 resin beads, wash them three times with ethanol, add the detection reagent for testing, and heat at 105 °C - 110 °C for 5 minutes. A colorless result indicates a negative reaction.

[0074] (8) Rinse the resin: Rinse the resin twice successively with DMF (10 mL / g), DCM (10 mL / g), and DMF (10 mL / g).

[0075] (9) Repeat the operations from (3) to (8) to sequentially connect the amino acids shown in SEQ ID No.1 from right to left.

[0076] (10) Drain and wash the resin as follows: twice with DMF (15 mL / g), twice with methanol (15 mL / g), twice with DMF (15 mL / g), twice with DCM (15 mL / g), and drain for 10 minutes.

[0077] (11) Cleave the polypeptide from the resin: At 25 °C, the cleavage solution consists of: 95% (V / V) TFA (trifluoroacetic acid), 1% (V / V) water, 2% (V / V) EDT (2-mercaptoethanol), 2% (V / V) TIS (triisopropylsilane); the cleavage time is: 120 minutes to obtain the cleavage solution.

[0078] (12) Dry and wash: Blow dry the cleavage solution with nitrogen, wash six times with ether, and then let it volatilize at room temperature.

[0079] (13) Analytical purification and freeze-drying: The crude polypeptide is purified by high-performance liquid chromatography; the polypeptide solution is collected and placed in a freeze dryer for concentration, and then freeze-dried to form a white powder, obtaining an antibacterial peptide with the structure of KRKVRVALKVS.

[0080] The detection reagent is ninhydrin.

[0081] Example 2

[0082] This example provides an antibacterial peptide P16 for maintaining the health of scalp flora, and its amino acid sequence is KWLKRIKKLFAN, as shown in SEQ ID NO.2.

[0083] This example further provides a preparation method of the antibacterial peptide, which adopts the solid-phase synthesis method, and the specific steps are as follows:

[0084] (1) The polypeptide synthesis sequence is from the C-terminus to the N-terminus: Put 20 g of AM resin into a reaction tube, add 15 mL / g of DCM (dichloromethane), and shake for 45 minutes; filter off the solvent DCM through a sintered glass funnel, add 3-fold molar excess of Fmoc-Linker-OH (CAS: 145069-56-3), and then add 6.5-fold molar excess of DIEA (N,N-diisopropylethylamine), and shake for 75 minutes. Block with methanol; evaporate DMF by rotary evaporation, add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes and then remove, and then add 20 mL / g of 20% (V / V) piperidine DMF solvent and wash for 20 minutes. Wash the resin twice with DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g) respectively, and shake for 40 minutes;

[0085] (2) Connect the first amino acid: Filter off the solvent DCM through a sintered glass funnel, add 3.5-fold molar excess of Fmoc-Ala-OH, dissolve in DMF (dimethylformamide), and then add 6.5-fold molar excess of DIEA (N,N-diisopropylethylamine), and shake for 70 minutes. Block with methanol.

[0086] (3) Deprotection: Evaporate DMF by rotary evaporation, add 20 mL / g of 20% (V / V) piperidine-DMF solvent, wash for 5 minutes and then remove, and then add 15 mL / g of 20% (V / V) piperidine DMF solvent and wash for 20 minutes.

[0087] (4) Detection: Drain the piperidine solution, take 15 resin particles, wash them three times with ethanol, and add the detection reagent for detection. Heat at 105 - 110 °C for 8 minutes, and a dark blue color change indicates a positive reaction.

[0088] (5) Wash the resin: Wash the resin twice successively with DMF (15 mL / g), DCM (15 mL / g), and DMF (15 mL / g).

[0089] (6) Condensation: Add three-fold excess of the next amino acid derivative dissolved in DMF (from the C-terminus to the N-terminus), 3.5-fold excess of HBTU (benzotriazole-N,N,N',N'-tetramethyluronium hexafluorophosphate) dissolved in DMF into the reaction tube, and then immediately add 16-fold molar amount of DIEA, and react for 40 minutes.

[0090] (7) Detection: Take 15 resin beads, wash them three times with ethanol, add the detection reagent for detection, heat at 105 °C - 110 °C for 5 minutes, and a colorless solution indicates a negative reaction.

[0091] (8) Wash the resin: Wash the resin twice successively with DMF (10 mL / g), DCM (10 mL / g), and DMF (10 mL / g).

[0092] (9) Repeat the operations from (3) to (8), and connect the amino acids shown in SEQ ID No.2 in sequence from right to left.

[0093] (10) Drain, and wash the resin according to the following method: twice with DMF (15 mL / g), twice with methanol (15 mL / g), twice with DMF (15 mL / g), twice with DCM (15 mL / g), and drain for 10 minutes.

[0094] (11) Cleave the polypeptide from the resin: The cleavage solution used at 25 °C consists of: 95% (V / V) TFA (trifluoroacetic acid), 1% (V / V) water, 2% (V / V) EDT (mercaptoethanol), 2% (V / V) TIS (triisopropylsilane); the cleavage time is: 120 minutes, and the cleavage solution is obtained.

[0095] (12) Blow-dry and wash: Blow-dry the cleavage solution with nitrogen, wash it six times with ether, and then let it volatilize at room temperature.

[0096] (13) Analyze, purify, and lyophilize: Purify the crude polypeptide by high-performance liquid chromatography; collect the polypeptide solution, put it into a lyophilizer for concentration, and lyophilize it into a white powder to obtain the antibacterial peptide with the structure of KWLKRIKKLFAN.

[0097] The detection reagent is ninhydrin.

[0098] Example 3

[0099] This example provides an antibacterial peptide P7L for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KRKVRVLLKVS, as shown in SEQ ID NO.3.

[0100] Example 4

[0101] This example provides an antimicrobial peptide P7K for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KRKVRVKLKVS, as shown in SEQ ID NO.4.

[0102] Example 5

[0103] This example provides an antimicrobial peptide P7R for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KRKVRVRLKVS, as shown in SEQ ID NO.5.

[0104] Example 6

[0105] This example provides an antimicrobial peptide P7I for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KRKVRVILKVS, as shown in SEQ ID NO.6.

[0106] Example 7

[0107] This example provides an antimicrobial peptide P7F for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KRKVRVFLKVS, as shown in SEQ ID NO.7.

[0108] Example 8

[0109] This example provides an antimicrobial peptide P16L for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KWLKRIKKLFLN, as shown in SEQ ID NO.8.

[0110] Example 9

[0111] This example provides an antimicrobial peptide P16K for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KWLKRIKKLFKN, as shown in SEQ ID NO.9.

[0112] Example 10

[0113] This example provides an antimicrobial peptide P16R for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KWLKRIKKLFRN, as shown in SEQ ID NO.10.

[0114] Example 11

[0115] This example provides an antimicrobial peptide P16I for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KWLKRIKKLFIN, as shown in SEQ ID NO.11.

[0116] Example 12

[0117] This example provides an antimicrobial peptide P16V for maintaining the health of scalp flora. The difference from Example 1 is only that its amino acid sequence is KWLKRIKKLFVN, as shown in SEQ ID NO.12.

[0118] Experimental Example

[0119] 1. Bacteriostatic experiment:

[0120] The liquid medium bacteriostatic experiments of the antimicrobial peptides described in Examples 1 - 12 were detected. The bacteria detected were Malassezia furfur ATCC 44344, Malassezia restricta ATCC96810, Staphylococcus hominis (BNCC352267), Candida albicans ATCC 10231, Staphylococcus aureus ATCC25923, and Lactobacillus acidophilus ATCC4796. CAP is chloramphenicol and KCZ is ketoconazole. As control groups, they are all commercially available.

[0121] 2. Experimental results

[0122] The bacteriostatic experiment results against Malassezia furfur are as shown in Figure 1A and Figure 1B After incubating with 10 μg / mL antimicrobial peptide for 48 hours and 72 hours, the inhibition rate of all antimicrobial peptides against Malassezia furfur reached 100%. Similarly, after incubating with 20 μg / mL antimicrobial peptide for 48 hours and 72 hours, the inhibition rate of all antimicrobial peptides against Malassezia furfur reached 100%.

[0123] The bacteriostatic results against Malassezia restricta are as shown in Figure 2A and Figure 2BAs shown, after incubating with 10 μg / mL antimicrobial peptide for 48 hours, the inhibition rates of antimicrobial peptides P7L, P7K, P7R, P7I, P7F, P16L, and P16R against Malassezia restricta reached 100%; after continuously incubating for 72 hours, the antibacterial rates of P7K, P7R, P7F, P16L, and P16R against Malassezia restricta remained at 100% unchanged. Similarly, after incubating with 20 μg / mL antimicrobial peptide for 48 hours, the inhibition rates of antimicrobial peptides P7, P16, P7L, P7K, P7R, P7I, P16L, P16K, P16R, P16I, and P16V against Malassezia restricta reached 100%; after continuously incubating for 72 hours, the antibacterial rates of antimicrobial peptides P7, P7L, P7K, P7R, P7I, P16L, P6K, and P16R against Malassezia restricta remained at 100%.

[0124] The antibacterial results against Staphylococcus hominis are as Figure 3A and Figure 3B shown. After incubating with 10 μg / mL and 20 μg / mL antimicrobial peptides for 24 hours, the inhibition rates of all antimicrobial peptides against Staphylococcus hominis reached 100%. After continuously incubating for 48 hours, the inhibition rates of all antimicrobial peptides against Staphylococcus hominis reached 100%.

[0125] The antibacterial results against Candida albicans are as Figure 4 shown. After incubating with 10 μg / mL antimicrobial peptide for 24 hours, the inhibition rates of antimicrobial peptides P16, P7K, P7R, P7I, P16L, P16K, P16R, P16I, and P16V against Candida albicans reached 100%.

[0126] The antibacterial results against Staphylococcus aureus are as Figure 5 shown. After incubating with 100 μg / mL antimicrobial peptide for 24 hours, the inhibition rates of antimicrobial peptides P7K, P7R, P7I, P16L, P16R, and P16I against Staphylococcus aureus reached 100%.

[0127] The antibacterial results against Lactobacillus acidophilus are as Figure 6A and 6B shown: After incubating with 10 μg / mL, 20 μg / mL, and 40 μg / mL antimicrobial peptides for 48 hours and 72 hours, the inhibition rates of all antimicrobial peptides against Lactobacillus acidophilus were lower than 30%.

[0128] The present invention designs and synthesizes an antimicrobial peptide for maintaining the health of scalp flora, which has good safety and can be used to treat scalp problems such as dandruff, seborrheic dermatitis, scalp itching, hair loss, etc. caused by scalp flora imbalance; the antimicrobial peptide can be applied to scalp care products, hair conditioners, shampoo or topical drugs for removing dandruff or treating seborrheic dermatitis, scalp itching, hair loss. The antimicrobial peptide of the present invention has significant antibacterial effects on Malassezia furfur, Malassezia restricta, Staphylococcus hominis, Candida albicans, and Staphylococcus aureus, while having a weak inhibitory effect on Lactobacillus acidophilus, thus being more conducive to maintaining the health of scalp flora and having great application value.

[0129] As mentioned above, the above is only the specific implementation manner of the present invention, but the protection scope of the present invention is not limited thereto. Any person skilled in the art within the technical scope disclosed by the present invention can easily think of changes or substitutions, which should all be covered within the protection scope of the present invention. Therefore, the protection scope of the present invention 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 one of the following polypeptides (a), (c), (d), and (e): (a) a polypeptide whose amino acid sequence includes the amino acid sequence shown in SEQ ID NO.1, or a polypeptide whose amino acid sequence consists of the amino acid residues shown in SEQ ID NO.1; (c) a polypeptide formed by substituting and / or deleting and / or adding one or more amino acid residues of the amino acid sequence defined in (a); (d) a polypeptide obtained by modifying the N-terminus and / or C-terminus of the polypeptide defined in (a); (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).

2. The antimicrobial peptide for maintaining healthy scalp flora according to claim 1, characterized in that: The antimicrobial peptide is any one of P7, P7L, P7K, P7R, P7I, and P7F.

3. The antimicrobial peptide for maintaining healthy scalp flora according to claim 2, characterized in that: The amino acid sequence of the antimicrobial peptide P7 is shown in SEQ ID NO.1; The amino acid sequence of the antimicrobial peptide P7L is shown in SEQ ID NO.3; The amino acid sequence of the antimicrobial peptide P7K is shown in SEQ ID NO.

4.

4. The antimicrobial peptide for maintaining healthy scalp flora according to claim 2, characterized in that: The amino acid sequence of the antimicrobial peptide P7R is shown in SEQ ID NO.5; The amino acid sequence of the antimicrobial peptide P7I is shown in SEQ ID NO.6; The amino acid sequence of the antimicrobial peptide P7F is shown in SEQ ID NO.

7.

5. A method for preparing an antimicrobial peptide for maintaining healthy scalp flora according to any one of claims 1 to 4, characterized in that: The preparation method is a solid phase synthesis method.

6. Use of the antimicrobial peptide according to any one of claims 1 to 4 in the preparation of a product for preventing or treating scalp diseases caused by an imbalance of scalp microbial flora.

7. The use according to claim 6, characterized in that: The product is any one of a scalp care product, a hair conditioner, a shampoo, and an external medicine.

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