Search

JP-7855811-B2 - Novel polypeptides for promoting tissue repair and their use

JP7855811B2JP 7855811 B2JP7855811 B2JP 7855811B2JP-7855811-B2

Inventors

  • 葉文才
  • 王磊
  • 張冬梅
  • 劉俊珊
  • 范春林
  • 曹佳青

Assignees

  • 広州華鋭生物医薬科技有限公司
  • 広州曁南大学科技園管理有限公司

Dates

Publication Date
20260511
Application Date
20220408
Priority Date
20211125

Claims (7)

  1. A novel polypeptide for promoting tissue repair, The novel polypeptide is characterized in that it has the structure shown in any one of TRF1 to TRF12.
  2. Use of the novel polypeptide described in claim 1 in the preparation of products for promoting tissue repair or improving skin aesthetics.
  3. The aforementioned product is a pharmaceutical, medical device, or daily chemical product, and is used in the preparation of a novel polypeptide according to claim 2 for promoting tissue repair or improving skin aesthetics.
  4. The use of the novel polypeptide according to claim 3 in the preparation of a product for promoting tissue repair or improving skin appearance, wherein the aforementioned pharmaceutical, medical device, or daily chemical product comprises one or more novel polypeptides in an effective amount, or a pharmaceutically acceptable salt thereof or a stereoisomer thereof, with the remainder being an additive or other compoundable agent.
  5. The use of the novel polypeptide according to claim 3 in the preparation of products for promoting tissue repair or improving skin appearance, wherein the pharmaceutical product, medical device, or daily chemical product is a tablet, capsule, injection, liposome nanoparticle , release control agent, gel cream, ointment, liniment, patch, cream, cleanser, lotion, gel, or toner.
  6. The use of the novel polypeptide according to claim 4 in the preparation of a product for promoting tissue repair or improving skin appearance, wherein the additive is a solvent, a disintegrant, a flavor enhancer, a preservative, a colorant, or a binder.
  7. A pharmaceutical composition characterized by containing a novel polypeptide as described in claim 1 and a pharmaceutically acceptable carrier.

Description

This invention relates to the fields of pharmaceuticals, medical devices, and daily chemicals, and more particularly to novel polypeptides for promoting tissue repair and their use. With the accelerating development of society and the aging of the population, tissue trauma now includes not only burns and wounds, but also intractable wounds and ulcers such as gastric ulcers, oral ulcers, diabetic ulcers, autoimmune skin ulcers, venous stasis ulcers, and pressure ulcers caused by prolonged bed rest. The pathology of intractable wounds and ulcers is complex, the course is long, treatment is difficult, and treatment costs are high, placing a heavy physical and mental burden on patients, as well as a significant financial burden. Currently, growth factor preparations are widely used to treat intractable wounds and ulcers, showing good therapeutic effects. Among these, epidermal growth factor, basic fibroblast growth factor, and vascular endothelial growth factor are all important for wound and ulcer healing. However, these endogenous factors have high preparation costs and poor stability, limiting their clinical application. Therefore, there is a great need to find and develop highly active substances with low manufacturing costs and excellent stability for the treatment of tissue trauma, intractable wounds, and ulcers. Figure A shows the mass spectrum of the novel polypeptide TRF1, with A being the ESI-MS, B being the MS2 (m/z 50-580), and C being the MS2 (m/z 580-1110).Figure A shows the mass spectrum of the novel polypeptide TRF2, with A being the ESI-MS, B being the MS2 (m/z 50-420), C being the MS2 (m/z 390-810), and D being the MS2 (m/z 810-1170).Figure A shows the mass spectrum of the novel polypeptide TRF3, with A being the ESI-MS, B being the MS2 (m/z 50-600), and C being the MS2 (m/z 600-1300).Figure A shows the mass spectrum of the novel polypeptide TRF4, with A being the ESI-MS, B being the MS2 (m/z 50-510), and C being the MS2 (m/z 510-1250).Figure A shows the mass spectrum of the novel polypeptide TRF5, with A being the ESI-MS, B being the MS2 (m/z 50-650), and C being the MS2 (m/z 620-1200).Figure A shows the mass spectrum of the novel polypeptide TRF6, with A being the ESI-MS, B being the MS2 (m/z 50-400), C being the MS2 (m/z 400-900), and D being the MS2 (m/z 850-1800).Figure A shows the mass spectrum of the novel polypeptide TRF7, with A being the ESI-MS, B being the MS2 (m/z 50-400), C being the MS2 (m/z 400-970), and D being the MS2 (m/z 970-1700).Figure A shows the mass spectrum of the novel polypeptide TRF8, with A being the ESI-MS, B being the MS2 (m/z 50-620), and C being the MS2 (m/z 620-1150).Figure A shows the mass spectrum of the novel polypeptide TRF9, with A being the ESI-MS, B being the MS2 (m/z 50-420), C being the MS2 (m/z 390-810), and D being the MS2 (m/z 800-1200).Figure A shows the mass spectrum of the novel polypeptide TRF10, with A being the ESI-MS, B being the MS2 (m/z 50-500), and C being the MS2 (m/z 450-1250).Figure A shows the mass spectrum of the novel polypeptide TRF11, with A being the ESI-MS, B being the MS2 (m/z 50-420), C being the MS2 (m/z 390-820), and D being the MS2 (m/z 800-1270).This is a mass spectrum of the novel polypeptide TRF12. Figure A shows its ESI-MS, Figure B shows its MS2 (m/z 50-380), Figure C shows its MS2 (m/z 380-920), and Figure D shows its MS2 (m/z 920-1560).This figure shows the results of an analysis of the effects of novel polypeptides TRF1 to TRF12 on the proliferation of HaCAT cells.This figure shows the results of an analysis of the effects of novel polypeptides TRF1 to TRF12 on HSF cell migration. The present invention will be described in detail below with reference to the drawings, but the embodiments of the present invention are not limited to these. Example 1 Synthesis of Novel Polypeptides TRF1 to TRF12 (1) Solid-phase synthesis of novel polypeptide TRF1 0.3 to 0.5 mmol/g of tyrosine-Wang resin having an Fmoc group and a side-chain protecting group was placed in a solid-phase synthesizer, and 20 mL of N,N-dimethylformamide was added to completely dissolve it. After extracting the solvent, 20% piperidine (dissolved in N,N-dimethylformamide by volume) was added, and after stirring for about 10 minutes, the solvent was extracted, and this operation was repeated twice to completely remove the Fmoc group, then 20 mL of N,N-dimethylformamide was added to wash, the solvent was extracted, and this operation was repeated three times. 0.5 mmol of cysteine having an Fmoc group and a side-chain protecting group was added, and then the same amount of HBTU/N,N-dimethylformamide and N,N-diisopropylethylamine/N,N-dimethylformamide solution were added, and the mixture was reacted under an N2 atmosphere for 40 to 60 minutes. Unreacted drugs and reagents were eluted with N,N-dimethylformamide and detected with ninhydrin. Subsequently, the remaining amino acids were bonded using the same method, and peptides were synthesized bound to the resin thr