Drug molecule for inhibiting formation of collagenous fibers and application thereof

Abstract

The invention relates to a drug molecule for inhibiting formation of collagenous fibers and application thereof. The drug molecule comprises a hydrophilic unit, a lysyl oxidase inhibition unit, a matrix metalloproteinase 2 response peptide, a collagen self-assembly interference peptide, a matrix metalloproteinase 2 response peptide and a hydrophobic unit which are connected in sequence. The drug molecule comprises two main active components, namely a lysyl oxidase inhibition unit capable of inhibiting the activity of lysyl oxidase in the collagen crosslinking process and a collagen self-assembly interference peptide capable of inhibiting collagen self-assembly, and can inhibit the collagen covalent crosslinking process in multiple aspects and reduce the generation of collagen fibers. Meanwhile, the MMP2 response peptide in the drug molecules can respond to MMP2, promote the drug molecules to disintegrate, realize release of the two main active components, inhibit excessive deposition of collagen at the wound, and promote collagen remodeling at the skin wound to develop closer to normal skin collagen characteristics.

Description

Technical Field

[0001] The invention relates to the field of biotechnology, and in particular to a drug molecule for inhibiting collagen fiber formation and application thereof. Background Art

[0002] Skin scar is a general term for the appearance and histopathological changes of normal skin tissue caused by various traumas. It is a common fibrotic disease. Scar formation affects the patient's appearance and is accompanied by itching and pain. The resulting contracture can lead to varying degrees of functional disorders, such as tendon contracture, joint dislocation, motor dysfunction, occupational psychological disorders, etc., which reduces the patient's quality of life and brings a heavy economic and psychological burden to subsequent treatment.

[0003] In the process of skin scar formation, the destruction of collagen homeostasis leads to excessive deposition of type I collagen, which is the main cause of scar thickening and hardening. Therefore, developing an efficient inhibitory strategy for the deposition of type I collagen is of great significance for reducing scar formation, reducing scar area, reducing scar thickness and improving scar texture.

[0004] CN114286816A discloses a difluorohalogenated allylamine sulfone derivative inhibitor of lysyl oxidase, which can inhibit the activity of lysyl oxidase and can be used to treat fibrosis, cancer and / or scar formation.

[0005] However, the drugs used to treat skin scars in the prior art rely solely on a single inhibitor, which is unable to fully inhibit collagen cross-linking and unable to achieve the best anti-scar effect.

[0006] Therefore, developing a drug molecule that can inhibit collagen fiber formation from multiple aspects and improve the inhibition efficiency of collagen deposition and anti-scar effect has become a technical problem that needs to be solved urgently. Summary of the invention

[0007] In view of the shortcomings of the prior art, the present invention aims to provide a drug molecule for inhibiting collagen fiber formation and its application. The drug molecule can inhibit both the collagen covalent cross-linking process and the collagen self-assembly process before the collagen covalent cross-linking, thereby improving the efficiency of collagen deposition inhibition in many aspects and promoting scar-free wound healing.

[0008] In order to achieve the purpose of the invention, the present invention adopts the following technical solutions:

[0009] In a first aspect, the present invention provides a drug molecule for inhibiting collagen fiber formation, wherein the drug molecule comprises a hydrophilic unit, a lysyl oxidase inhibition unit (LOX inhibition unit), a matrix metalloproteinase 2 response peptide (MMP2 response peptide), a collagen self-assembly interfering peptide, a matrix metalloproteinase 2 response peptide (MMP2 response peptide) and a hydrophobic unit connected in sequence.

[0010] During the assembly of collagen fibers, the covalent cross-linking of collagen can promote the transformation of collagen from soluble monomer molecules to stable insoluble collagen fibers, which plays an important role in the collagen deposition process. The covalent cross-linking of collagen is dominated by lysyl oxidase, so lysyl oxidase is an effective target for intervening in collagen assembly. The collagen self-assembly process occurs before the covalent cross-linking of collagen. The collagen self-assembly constitutes the regular periodic arrangement of collagen molecules and is the basis for the subsequent covalent cross-linking of collagen molecules. Intervention in the collagen self-assembly process has an inhibitory effect on various subsequent cross-linking mechanisms.

[0011] Based on this, the present invention has developed a drug molecule that inhibits the formation of collagen fibers, which comprises two main active ingredients: a lysyl oxidase inhibition unit (LOX inhibition unit) that can inhibit the activity of lysyl oxidase (LOX) in the collagen cross-linking process, and a collagen self-assembly interfering peptide that can inhibit collagen self-assembly. It can inhibit the process of collagen covalent cross-linking in many aspects and reduce collagen fiber formation.

[0012] At the same time, the drug molecule of the present invention contains a matrix metalloproteinase 2 response peptide (MMP2 response peptide). Matrix metalloproteinase 2 (MMP2) is highly expressed during tissue repair and is the initiator of matrix remodeling. During matrix remodeling, the MMP2 response peptide in the drug molecule of the present invention can respond to MMP2, thereby disintegrating the drug molecule, releasing two active ingredients, lysyl oxidase inhibition unit (LOX inhibition unit) and collagen interfering peptide, to achieve more comprehensive inhibition of collagen cross-linking and collagen production, so that the number of mature collagen fibers generated is reduced and the anti-enzymatic ability is weakened, inhibiting excessive deposition of collagen at the wound, and promoting collagen remodeling at the skin wound to develop closer to the collagen characteristics of normal skin.

[0013] Preferably, the amino acid sequence of the collagen self-assembly interfering peptide includes SEQ ID NO:1.

[0014] Preferably, the amino acid sequence of the matrix metalloproteinase 2-responsive peptide comprises SEQ ID NO:2.

[0015] Among them, the specific sequence of SEQ ID NO: 1 is: GGGYDFGYD, and the specific sequence of SEQ ID NO: 2 is PLGIAG.

[0016] Preferably, the lysyl oxidase inhibitory unit comprises a copper ion chelator modified with an amino acid residue, wherein the amino acid is selected from lysine or cysteine.

[0017] Preferably, the copper ion chelating agent comprises N-hydroxysuccinimide.

[0018] The present invention creatively finds that N-hydroxysuccinimide can well inhibit the activity of LOX, and synergistically improves the inhibition efficiency of collagen deposition with collagen self-assembly interfering peptide.

[0019] Preferably, the hydrophilic unit comprises methoxy-terminated polyethylene glycol.

[0020] Preferably, the number average molecular weight of the polyethylene glycol is 200-2000.

[0021] Among them, the specific point values ​​between 200 and 2000 can be selected as 200, 400, 600, 800, 1000, 1200, 1400, 1600, 1800, 2000, etc.

[0022] Preferably, the hydrophobic unit comprises an alkyl chain having 10 to 25 carbon atoms modified by an amino acid residue, wherein the amino acid is selected from lysine or cysteine.

[0023] Among them, the specific point values ​​from 10 to 25 can be selected as 10, 12, 14, 16, 18, 20, 22, 25, etc.

[0024] The hydrophilic unit and the hydrophobic unit provide hydrophilicity and hydrophobicity for the drug molecules, which is beneficial for the self-assembly of the drug molecules under specific conditions to form a stable micelle structure, thereby improving the solubility, stability and bioavailability of the drug molecules.

[0025] Preferably, the drug molecule has a structure as shown in Formula I.

[0026]

[0027] The schematic diagram of the structure of the drug molecule is as follows Figure 1 shown.

[0028] In a second aspect, the present invention provides a nanoparticle for inhibiting collagen fiber formation, wherein the nanoparticle is formed by self-assembly of the drug molecules for inhibiting collagen fiber formation described in the first aspect in a solvent.

[0029] Preferably, the particle size of the nanoparticles is 80 to 150 nm.

[0030] Among them, the specific point values ​​in 80-150nm can be selected as 80nm, 90nm, 100nm, 110nm, 120nm, 130nm, 140nm, 150nm, etc.

[0031] Preferably, the solvent comprises phosphate buffered saline.

[0032] In the present invention, the nanoparticles formed by self-assembly of drug molecules inhibiting collagen fiber formation have uniform particle size and stable structure. When the nanoparticles are co-incubated with MMP2, the MMP2 response peptide in the nanoparticles responds to MMP2, and the nanoparticles disintegrate, thereby releasing active substances.

[0033] In a third aspect, the present invention provides a use of the drug molecule for inhibiting collagen fiber formation as described in the first aspect or the nanoparticle for inhibiting collagen fiber formation as described in the second aspect in the preparation of a scar removing drug.

[0034] In a fourth aspect, the present invention provides a drug-loaded gel for inhibiting collagen fiber formation, wherein raw materials for preparing the drug-loaded gel include modified gelatin and the nanoparticles for inhibiting collagen fiber formation described in the second aspect.

[0035] The drug-loaded gel constructed by the present invention is suitable for application scenarios of skin wound repair. The moist healing environment provided by the gel can promote the closure of the wound, and the nanoparticles can interfere with the formation of collagen fibers and inhibit excessive deposition of collagen at the wound.

[0036] Preferably, the modified gelatin comprises methacrylated gelatin;

[0037] Preferably, the mass ratio of the modified gelatin to the nanoparticles that inhibit collagen fiber formation is (100-150):1.

[0038] Preferably, the solid content of the drug-loaded gel is 1-5%.

[0039] Among them, the specific point values ​​in 100-150 can be selected from 100, 110, 120, 130, 140, 150, etc., and the specific point values ​​in 1-5% can be selected from 1%, 1.5%, 2%, 2.5%, 3%, 3.5%, 4%, 4.5%, 5%, etc.

[0040] When the modified gelatin and the nanoparticles that inhibit collagen fiber formation meet the above-mentioned specific ratio relationship, the loading capacity of the nanoparticles can be increased while ensuring the gel properties.

[0041] In a fifth aspect, the present invention provides a method for preparing the drug-loaded gel for inhibiting collagen fiber formation as described in the fourth aspect, the preparation method comprising the following steps:

[0042] The modified gelatin, nanoparticles inhibiting the formation of collagen fibers and a photoinitiator are mixed in a solvent and subjected to light irradiation for cross-linking reaction to form the drug-loaded gel inhibiting the formation of collagen fibers.

[0043] Preferably, the photoinitiator comprises 2-hydroxy-4'-(2-hydroxyethoxy)-2-methylpropiophenone.

[0044] Preferably, the wavelength of the light is 350-380 nm, and the power density is 50-100 mW·cm -2 .

[0045] Among them, the specific point value in 350-380nm can be selected from 350nm, 360nm, 370nm, 380nm, etc., 50-100mW·cm -2 The specific point value can be selected as 50mW·cm -2 、60mW·cm -2 、70mW·cm -2 、80mW·cm -2 、90mW·cm -2 、100mW·cm -2 wait.

[0046] Preferably, the cross-linking reaction is carried out at a temperature of 15 to 40° C. and for a time of 10 to 60 minutes.

[0047] Among them, the specific point values ​​in 15-40℃ can be selected as 15℃, 20℃, 25℃, 30℃, 35℃, 40℃, etc., and the specific point values ​​in 10-60min can be selected as 10min, 20min, 30min, 40min, 50min, 60min, etc.

[0048] Preferably, the method for preparing methacrylic acid acylated gelatin comprises the following steps:

[0049] The gelatin is mixed and dissolved with a phosphate buffer solution, and then mixed with methacrylamide for reaction. After the reaction is completed, a phosphate buffer solution is added to terminate the reaction, thereby obtaining methacrylic acid acylated gelatin.

[0050] Preferably, the mixed dissolution is carried out at a temperature of 40 to 70° C. and for a time of 2 to 30 minutes.

[0051] Preferably, the temperature of the mixed reaction with methacrylamide is 40-70° C. and the time is 1-5 hours.

[0052] Among them, the specific point values ​​in 40-70℃ can be selected from 40℃, 45℃, 50℃, 55℃, 60℃, 65℃, 70℃, etc., the specific point values ​​in 2-30min can be selected from 2min, 5min, 10min, 15min, 20min, 25min, 30min, etc., and the specific point values ​​in 1-5h can be selected from 1h, 2h, 3h, 4h, 5h, etc.

[0053] The numerical range described in the present invention not only includes the point values ​​listed above, but also includes any point values ​​between the above numerical ranges that are not listed. Due to space limitations and for the sake of simplicity, the present invention no longer exhaustively lists the specific point values ​​included in the range.

[0054] Compared with the prior art, the present invention has the following beneficial effects:

[0055] The present invention has developed a drug molecule that inhibits the formation of collagen fibers, which contains two main active ingredients: a lysyl oxidase inhibitory unit that can inhibit the activity of lysyl oxidase in the collagen cross-linking process and a collagen self-assembly interfering peptide that can inhibit the self-assembly of collagen. It can inhibit the process of collagen covalent cross-linking in many aspects and reduce the formation of collagen fibers. At the same time, the MMP2 response peptide in the drug molecule can respond to MMP2, promote the disintegration of the drug molecule, realize the release of the two main active ingredients, inhibit the excessive deposition of collagen at the wound, and promote the collagen remodeling at the skin wound to develop closer to the collagen characteristics of normal skin. BRIEF DESCRIPTION OF THE DRAWINGS

[0056] Figure 1 It is a schematic diagram of the structure of a drug molecule that inhibits collagen fiber formation;

[0057] Figure 2 is a flow chart of the preparation of the drug-loaded gel for inhibiting collagen fiber formation in Example 2;

[0058] Figure 3 is a transmission electron micrograph of the nanoparticles inhibiting collagen fiber formation prepared in Example 1;

[0059] Figure 4 This is a physical picture of the drug-loaded gel for inhibiting collagen fiber formation prepared in Example 2;

[0060] Figure 5 is a scanning electron micrograph of the drug-loaded gel prepared in Example 2 that inhibits collagen fiber formation;

[0061] Figure 6 This is a test diagram of the rheological properties of drug-loaded gels with different solid contents in Verification Example 3;

[0062] Figure 7 This is a test diagram of the inhibitory effect of nanoparticles on collagen fibers in Test Example 1;

[0063] Figure 8 This is a visual diagram of the wound surface changes of rabbits in different test groups in Test Example 2;

[0064] Fig. 9 These are two-photon imaging images of scar tissue of rabbits in different test groups in Test Example 2. DETAILED DESCRIPTION

[0065] The technical solution of the present invention is further described below by specific implementation methods. It should be understood by those skilled in the art that the embodiments are only to help understand the present invention and should not be regarded as specific limitations of the present invention.

[0066] Example 1

[0067] This embodiment provides a nanoparticle that inhibits collagen fiber formation, which is prepared by the following method:

[0068] (1) The drug molecule shown in formula I is synthesized by solid phase synthesis, wherein the drug molecule comprises a hydrophilic unit, a lysyl oxidase inhibitory unit, a matrix metalloproteinase 2 responsive peptide, a collagen self-assembly interfering peptide, a matrix metalloproteinase 2 responsive peptide and a hydrophobic unit connected in sequence.

[0069] The hydrophilic unit is methoxy polyethylene glycol 500 (mPEG 500 ), the hydrophobic unit is an alkyl chain of 18 carbon atoms (C18) modified by a lysine residue, the lysyl oxidase inhibitory unit is N-hydroxysuccinimide (NOTA) modified by a lysine residue, the amino acid sequence of the collagen self-assembly interfering peptide is SEQ ID NO: 1: GGGYDFGYD, and the amino acid sequence of the matrix metalloproteinase 2 responsive peptide (MMP2 responsive peptide) is SEQ ID NO: 2: PLGIAG.

[0070] Hydrophilic group at one end: mPEG 500 , NOTA and the MMP2 response peptide are connected through the lysine residue in the lysyl oxidase inhibition unit; in the middle part: the MMP2 response peptide, the collagen self-assembly interfering peptide and the MMP2 response peptide are connected through an amide bond; on the hydrophobic group side: the MMP2 response peptide and C18 are connected through the lysine residue in the hydrophobic unit. The structure of the prepared drug molecule is shown in Formula I.

[0071]

[0072] In this drug molecule, mPEG 500 The introduction of C18 provides amphiphilicity to the drug molecule, and the critical micelle concentration (CMC) of the drug molecule is measured to be 2.17 μM.

[0073] (2) Preparation of nanoparticles: A concentration 50 times that of CMC was selected as the assembly concentration, and the drug molecules synthesized in step (1) were dropped into PBS, and ultrasonicated at 25°C for 10 min to initiate self-assembly to obtain nanoparticles that inhibit collagen fiber formation (abbreviated as NRCIP).

[0074] Example 2

[0075] This embodiment provides a drug-loaded gel with a solid content of about 1.8%, which is prepared by the following method:

[0076] (1) Preparation of methacrylated gelatin: 1 g of gelatin (purchased from VETEC) was dissolved in 10 mL of sterile PBS and stirred at 50°C for 10 min to dissolve. After dissolution, 50 μL of methacrylamide (MA) was added dropwise and reacted at 50°C in the dark for 3 h. 40 mL of PBS was added to terminate the reaction. The unreacted MA was removed by dialyzing in deionized water using a 3.5 kD dialysis bag for 36 h. After freeze-drying, white solid methacrylated gelatin (GelMA) was obtained.

[0077] (2) 50 mg of freeze-dried GelMA was dissolved in 2 mL of 2-hydroxy-4'-(2-hydroxyethoxy)-2-methylpropiophenone (Irgacure 2959, 1%, w / v) in PBS, 4 μL of NRCIP (1 mg / 10 μL) prepared in Example 1 was added, and the mixed liquid was immediately exposed to UV-LED light (365 nm UV, 75 mW·cm -2 ) for 30 min to obtain a drug-loaded gel (abbreviated as GelMA@NRCIP) with a solid content of about 1.8%. The preparation process of the drug-loaded gel is as follows: Figure 2 shown.

[0078] Example 3

[0079] This embodiment provides a drug-loaded gel with a solid content of about 7.2%. The only difference between this embodiment and embodiment 2 is that 50 mg of freeze-dried GelMA is replaced with 200 mg of freeze-dried GelMA, and the remaining steps are consistent with those of embodiment 2.

[0080] Verification Example 1

[0081] This verification example characterizes the structure of the nanoparticles prepared in Example 1 that inhibit collagen fiber formation.

[0082] The nanoparticles (NRCIP) for inhibiting collagen fiber formation prepared in Example 1 were dissolved in water three times, ultrasonicated for 15 min, stained with uranyl acetate, and the structure of the nanoparticles was observed under a transmission electron microscope (Hitachi, model HT7700). Figure 3 As shown, the particle size of NRCIP is about 115 nm and is evenly dispersed.

[0083] Verification Example 2

[0084] This verification example characterizes the structure of the drug-loaded gel with a solid content of 2.5% prepared in Example 2.

[0085] The actual picture of the drug-loaded gel prepared in Example 2 is as follows Figure 4 As shown, it can be seen that the drug-loaded gel has a uniform texture and is easy to apply.

[0086] The drug-loaded gel prepared in Example 2 was fractured by liquid nitrogen, freeze-dried, and then treated with gold spraying. The structure of the drug-loaded gel was observed under a scanning electron microscope (Hitachi, model SU8220). The results are as follows: Figure 5 As shown, it indicates that the prepared drug-loaded gel has a porous structure, which can absorb wound exudate, provide a moist healing environment, and is beneficial to wound healing.

[0087] Verification Example 3

[0088] In this verification example, the rheological properties of the drug-loaded gels prepared in Examples 2 and 3 were tested.

[0089] The rheological properties of the drug-loaded gels with different solid contents obtained in Example 2 and Example 3 were tested. The results are as follows: Figure 6 As shown, it can be seen that the storage modulus and loss modulus of the drug-loaded gel with a solid content of 7.2% have increased to varying degrees, the gel texture has become hard, and it is not suitable for smearing.

[0090] Test Example 1

[0091] The inhibitory effect of NRCIP on collagen fibrillogenesis was tested.

[0092] (1) Experimental groups:

[0093] Control group: 50 μL of 3 μg / mL collagen solution was dripped onto the quartz plate, and the collagen was allowed to self-assemble at 37°C. After 1 h of self-assembly, an atomic force microscope (purchased from Oxford Instruments, model Cypher VRS) was used to observe the number of fibers formed;

[0094] NRCIP group: 50 μL of 100 μM NRCIP solution was mixed with 50 μL of 0.2 μg / mL MMP2 solution in advance, and placed at 37°C for 3 h to allow NRCIP to be enzymatically hydrolyzed. Then 2 μL of the above solution was added to 100 μL of 3 μg / mL collagen solution. 50 μL of the above collagen solution was placed on a quartz plate, and the collagen was allowed to self-assemble at 37°C. After 1 h of self-assembly, the number of fibers formed was observed using an atomic force microscope.

[0095] (2) Test results:

[0096] Comparing the inhibitory effect of adding NRCIP on collagen fiber formation, the results are as follows Figure 7 As shown, it can be seen that the number of collagen fibers formed by collagen self-assembly in the NRCIP group was significantly reduced, proving that NRCIP can effectively inhibit collagen self-assembly.

[0097] Test Example 2

[0098] The effect of drug-loaded gel in promoting wound healing was tested.

[0099] (1) Construction of injured rabbit model: New Zealand white rabbits (adult, 2.5 kg, purchased from Beijing Jinmuyang Experimental Animal Breeding Co., Ltd.) were anesthetized and circular incisions with a diameter of 7 mm were made on the ventral side of both ears. The epidermis, dermis, and perichondrium of each wound were completely removed, and the cartilage was kept intact. Pressure was applied to stop bleeding. One day after surgery, antibiotics were injected to prevent infection. At the same time, the wound was routinely disinfected daily for 1 to 5 days after surgery to remove secretions.

[0100] (2) Experimental groups: On the sixth day after surgery, the treatment group covered the wound with 100 μL of drug-loaded gel and wrapped it with gauze. The dressing was changed every other day until the 30th day after surgery. From the sixth day after surgery, the control group only wrapped it with gauze without covering it with drug-loaded gel.

[0101] The changes in the wound surface are shown in the following figure: Figure 8 As shown, the wounds in the treatment group healed significantly on the 10th day after surgery, and the scar protrusion was significantly lower than that in the control group 30 days after surgery.

[0102] (3) Scar tissue treatment effect test:

[0103] On the 30th day after surgery, all New Zealand rabbits were given sodium pentobarbital injected into the auricular vein to cause the rabbits to die of overdose. Hypertrophic scar tissue specimens were quickly removed, with 0.3 cm of normal tissue retained at the cutting edge, deep into the cartilage. The removed scar tissue was fixed in 4% formaldehyde solution, routinely dehydrated, and paraffin-embedded before being used to observe collagen using a two-photon microscope. The results are shown in the figure. Fig. 9 As shown. Fig. 9 It can be seen that obvious collagen fibers can be observed in the control group and are arranged in a disorderly manner, while the number of collagen fibers in the treatment group applied with the drug-loaded gel is relatively small, indicating that the drug in the drug-loaded gel has been released, thereby intervening in the formation of collagen fibers and inhibiting the excessive deposition of collagen at the wound.

[0104] The applicant declares that the present invention illustrates the technical solution of the present invention through the above-mentioned embodiments, but the present invention is not limited to the above-mentioned embodiments, that is, it does not mean that the present invention must rely on the above-mentioned embodiments to be implemented. Those skilled in the art should understand that any improvement of the present invention, equivalent replacement of various raw materials of the product of the present invention, addition of auxiliary components, selection of specific methods, etc., all fall within the protection scope and disclosure scope of the present invention.

[0105] The preferred embodiments of the present invention are described in detail above. However, the present invention is not limited to the specific details in the above embodiments. Within the technical concept of the present invention, a variety of simple modifications can be made to the technical solution of the present invention, and these simple modifications all belong to the protection scope of the present invention.

[0106] It should also be noted that the various specific technical features described in the above specific embodiments can be combined in any suitable manner without contradiction. In order to avoid unnecessary repetition, the present invention will not further describe various possible combinations.

Claims

1. A drug molecule that inhibits collagen fiber formation, characterized in that: The drug molecule comprises a hydrophilic unit, a lysyl oxidase inhibition unit, a matrix metalloproteinase 2 response peptide, a collagen self-assembly interference peptide, a matrix metalloproteinase 2 response peptide and a hydrophobic unit which are connected in sequence.

2. The drug molecule according to claim 1, characterized in that The amino acid sequence of the collagen self-assembly interfering peptide includes SEQ ID NO: 1; Preferably, the amino acid sequence of the matrix metalloproteinase 2 responsive peptide comprises SEQ ID NO: 2; Preferably, the lysyl oxidase inhibitory unit comprises a copper ion chelator modified with an amino acid residue, wherein the amino acid is selected from lysine or cysteine; Preferably, the copper ion chelating agent comprises N-hydroxysuccinimide.

3. The drug molecule according to claim 1 or 2, characterized in that The hydrophilic unit comprises methoxy-terminated polyethylene glycol; Preferably, the number average molecular weight of the polyethylene glycol is 200 to 2000; Preferably, the hydrophobic unit comprises an alkyl chain having 10 to 25 carbon atoms modified by an amino acid residue, wherein the amino acid is selected from lysine or cysteine.

4. The drug molecule according to any one of claims 1 to 3, characterized in that The drug molecule has a structure as shown in Formula I.

5. A nanoparticle for inhibiting collagen fiber formation, characterized in that: The nanoparticles are formed by self-assembly of the drug molecules for inhibiting collagen fiber formation according to any one of claims 1 to 4 in a solvent.

6. The nanoparticle according to claim 5, characterized in that The particle size of the nanoparticles is 80 to 150 nm; Preferably, the solvent comprises phosphate buffered saline.

7. Use of the drug molecule for inhibiting collagen fiber formation as claimed in any one of claims 1 to 4 or the nanoparticle for inhibiting collagen fiber formation as claimed in claim 5 or 6 in the preparation of scar removing drugs.

8. A drug-loaded gel for inhibiting collagen fiber formation, characterized in that: The raw materials for preparing the drug-loaded gel include modified gelatin and the nanoparticles for inhibiting collagen fiber formation according to claim 5 or 6.

9. The drug-loaded gel according to claim 8, characterized in that: The modified gelatin includes methacrylate acylated gelatin; Preferably, the mass ratio of the modified gelatin to the nanoparticles inhibiting collagen fiber formation is (100-150):1; Preferably, the solid content of the drug-loaded gel is 1-5%.

10. A method for preparing a drug-loaded gel for inhibiting collagen fiber formation as claimed in claim 8 or 9, characterized in that: The preparation method comprises the following steps: The modified gelatin, nanoparticles inhibiting the formation of collagen fibers and a photoinitiator are mixed in a solvent and subjected to light irradiation for cross-linking reaction to form the drug-loaded gel inhibiting the formation of collagen fibers; Preferably, the photoinitiator comprises 2-hydroxy-4'-(2-hydroxyethoxy)-2-methylpropiophenone; Preferably, the wavelength of the light is 350-380 nm, and the power density is 50-100 mW·cm -2 ; Preferably, the cross-linking reaction is carried out at a temperature of 15 to 40° C. and for a time of 10 to 60 minutes.

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