CN115634169A - Application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin - Google Patents
Application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin Download PDFInfo
- Publication number
- CN115634169A CN115634169A CN202210459406.0A CN202210459406A CN115634169A CN 115634169 A CN115634169 A CN 115634169A CN 202210459406 A CN202210459406 A CN 202210459406A CN 115634169 A CN115634169 A CN 115634169A
- Authority
- CN
- China
- Prior art keywords
- protein
- beta
- parts
- myoglycan
- extracellular matrix
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 40
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 39
- 229940088597 hormone Drugs 0.000 title claims abstract description 31
- 239000005556 hormone Substances 0.000 title claims abstract description 31
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 title claims abstract description 25
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 title claims abstract description 25
- 210000002744 extracellular matrix Anatomy 0.000 title claims abstract description 25
- 239000002537 cosmetic Substances 0.000 title claims abstract description 19
- 230000001419 dependent effect Effects 0.000 title claims abstract description 17
- 102000016942 Elastin Human genes 0.000 claims description 37
- 108010014258 Elastin Proteins 0.000 claims description 37
- 229920002549 elastin Polymers 0.000 claims description 37
- 235000018102 proteins Nutrition 0.000 claims description 37
- FYGDTMLNYKFZSV-URKRLVJHSA-N (2s,3r,4s,5s,6r)-2-[(2r,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1[C@@H](CO)O[C@@H](OC2[C@H](O[C@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-URKRLVJHSA-N 0.000 claims description 24
- 229920002498 Beta-glucan Polymers 0.000 claims description 24
- 108010017384 Blood Proteins Proteins 0.000 claims description 19
- 102000004506 Blood Proteins Human genes 0.000 claims description 19
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 16
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 claims description 16
- 241000269851 Sarda sarda Species 0.000 claims description 3
- 235000021120 animal protein Nutrition 0.000 claims description 3
- 230000000694 effects Effects 0.000 abstract description 10
- 230000009759 skin aging Effects 0.000 abstract description 5
- 238000012423 maintenance Methods 0.000 abstract description 2
- 210000003491 skin Anatomy 0.000 description 35
- 210000004027 cell Anatomy 0.000 description 11
- 239000003814 drug Substances 0.000 description 11
- 210000004177 elastic tissue Anatomy 0.000 description 11
- 210000001519 tissue Anatomy 0.000 description 11
- 102000008186 Collagen Human genes 0.000 description 10
- 108010035532 Collagen Proteins 0.000 description 10
- 201000004624 Dermatitis Diseases 0.000 description 10
- 229920001436 collagen Polymers 0.000 description 10
- 201000010099 disease Diseases 0.000 description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 8
- 238000002360 preparation method Methods 0.000 description 8
- 238000000034 method Methods 0.000 description 7
- 235000014113 dietary fatty acids Nutrition 0.000 description 6
- 229930195729 fatty acid Natural products 0.000 description 6
- 239000000194 fatty acid Substances 0.000 description 6
- 150000004665 fatty acids Chemical class 0.000 description 6
- 229920001503 Glucan Polymers 0.000 description 5
- 150000001413 amino acids Chemical group 0.000 description 5
- 229940079593 drug Drugs 0.000 description 5
- 230000001815 facial effect Effects 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 108010088751 Albumins Proteins 0.000 description 4
- 102000009027 Albumins Human genes 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 210000002919 epithelial cell Anatomy 0.000 description 4
- 210000002950 fibroblast Anatomy 0.000 description 4
- 210000004698 lymphocyte Anatomy 0.000 description 4
- 210000002540 macrophage Anatomy 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 108090000695 Cytokines Proteins 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 102000006395 Globulins Human genes 0.000 description 3
- 108010044091 Globulins Proteins 0.000 description 3
- 239000000835 fiber Substances 0.000 description 3
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 210000001724 microfibril Anatomy 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 102000016359 Fibronectins Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 208000002193 Pain Diseases 0.000 description 2
- 208000012641 Pigmentation disease Diseases 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- 230000002016 colloidosmotic effect Effects 0.000 description 2
- 210000002808 connective tissue Anatomy 0.000 description 2
- UQHKFADEQIVWID-UHFFFAOYSA-N cytokinin Natural products C1=NC=2C(NCC=C(CO)C)=NC=NC=2N1C1CC(O)C(CO)O1 UQHKFADEQIVWID-UHFFFAOYSA-N 0.000 description 2
- 239000004062 cytokinin Substances 0.000 description 2
- VEVRNHHLCPGNDU-MUGJNUQGSA-O desmosine Chemical compound OC(=O)[C@@H](N)CCCC[N+]1=CC(CC[C@H](N)C(O)=O)=C(CCC[C@H](N)C(O)=O)C(CC[C@H](N)C(O)=O)=C1 VEVRNHHLCPGNDU-MUGJNUQGSA-O 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000002500 effect on skin Effects 0.000 description 2
- 229920001971 elastomer Polymers 0.000 description 2
- 210000002615 epidermis Anatomy 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 230000003054 hormonal effect Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 210000003041 ligament Anatomy 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 230000005012 migration Effects 0.000 description 2
- 238000013508 migration Methods 0.000 description 2
- 210000004493 neutrocyte Anatomy 0.000 description 2
- 235000016709 nutrition Nutrition 0.000 description 2
- 230000035764 nutrition Effects 0.000 description 2
- 230000019612 pigmentation Effects 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 230000037394 skin elasticity Effects 0.000 description 2
- 210000003518 stress fiber Anatomy 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 208000002874 Acne Vulgaris Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- GHXZTYHSJHQHIJ-UHFFFAOYSA-N Chlorhexidine Chemical compound C=1C=C(Cl)C=CC=1NC(N)=NC(N)=NCCCCCCN=C(N)N=C(N)NC1=CC=C(Cl)C=C1 GHXZTYHSJHQHIJ-UHFFFAOYSA-N 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 206010048768 Dermatosis Diseases 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 206010015150 Erythema Diseases 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 206010020649 Hyperkeratosis Diseases 0.000 description 1
- 208000031226 Hyperlipidaemia Diseases 0.000 description 1
- HEFNNWSXXWATRW-UHFFFAOYSA-N Ibuprofen Chemical compound CC(C)CC1=CC=C(C(C)C(O)=O)C=C1 HEFNNWSXXWATRW-UHFFFAOYSA-N 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- 108010014603 Leukocidins Proteins 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 206010033733 Papule Diseases 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 208000003251 Pruritus Diseases 0.000 description 1
- 206010037888 Rash pustular Diseases 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 206010040844 Skin exfoliation Diseases 0.000 description 1
- 208000007271 Substance Withdrawal Syndrome Diseases 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 108010051583 Ventricular Myosins Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 206010000496 acne Diseases 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 210000001789 adipocyte Anatomy 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 210000000709 aorta Anatomy 0.000 description 1
- 210000001367 artery Anatomy 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000037365 barrier function of the epidermis Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000003592 biomimetic effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000004566 building material Substances 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000011712 cell development Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000019522 cellular metabolic process Effects 0.000 description 1
- 229960003260 chlorhexidine Drugs 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000009223 counseling Methods 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000008260 defense mechanism Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 230000035618 desquamation Effects 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 210000004728 ear cartilage Anatomy 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 231100000321 erythema Toxicity 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000003862 glucocorticoid Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000004727 humoral immunity Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 229960001680 ibuprofen Drugs 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 150000002605 large molecules Chemical class 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000003340 mental effect Effects 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 210000003632 microfilament Anatomy 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 208000030212 nutrition disease Diseases 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 208000037920 primary disease Diseases 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 208000029561 pustule Diseases 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000007665 sagging Methods 0.000 description 1
- 230000002000 scavenging effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000037380 skin damage Effects 0.000 description 1
- 208000017520 skin disease Diseases 0.000 description 1
- 206010040882 skin lesion Diseases 0.000 description 1
- 231100000444 skin lesion Toxicity 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 210000000434 stratum corneum Anatomy 0.000 description 1
- 230000035882 stress Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 210000002435 tendon Anatomy 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
- 230000037303 wrinkles Effects 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Cosmetics (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Abstract
The invention discloses an application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin, relates to the technical field of maintenance products, and aims to solve the problems that a patient is easy to generate hormone dependence and poor skin aging delaying effect in the prior art.
Description
Technical Field
The invention relates to the technical field of maintenance products, in particular to application of extracellular matrix beta-myoglycan protein in a cosmetic for repairing hormone-dependent skin.
Background
In multicellular organisms, the cells are surrounded by a complex network of various macromolecules, called the extracellular matrix, which does not act as an inert support only, as thought in the past, or link the cells together to form tissues, organs. But contains a large number of signal molecules, actively participates in controlling the growth, polarity, shape, migration and metabolic activity of cells, fibronectin in extracellular matrix is mainly secreted by fibroblasts, epithelial cells and the like and is attached to the surface of the cells, and the function of the fibronectin is to promote the attachment of the cells to the matrix, the adhesion between the cells, and the construction of intracellular microfilaments and stress fibers. It has been observed that transformed in vitro cultured fibroblasts have reduced amounts of surface fibrin, associated cell morphology rounding, loose attachment to the culture substrate, greatly reduced intracellular stress fibers, dense cells, and overlapping growth. When inoculated into normal organisms, the transformed cells can grow into cancer masses, infiltrate normal tissues and generate wide metastasis. In another example, epithelial cells secrete collagen and membrane mucin into the basal layer of epithelial tissue, which in turn serves as a signal to "direct" the direction of growth and migration of epithelial cells. It is along the basal layer that epithelial cells develop during embryonic development or callus regeneration. It follows that several messages regulating cell growth and development are transmitted through the extracellular matrix.
Hormone dependence is caused by the long-term topical use of glucocorticoid preparations, on which the affected skin becomes dependent. Hormonal dermatitis is non-suppurative inflammation of the skin caused by improper use or abuse of external hormone preparations. The primary disease is rapidly improved but can not be radically cured after the hormone-dependent dermatosis is taken; after the treatment lasts for weeks or months, once the medicine is stopped, erythema, papules, tenderness, fissures, pustules, desquamation, pain, pruritus, burning and tightness occur at the medicine application part within a plurality of days, and the primary morbidity is worsened; when the hormone is reapplied, the symptoms quickly subside, and if the hormone is reapplied, rebound dermatitis occurs rapidly and is heavier than before; patients completely depend on external hormones in order to avoid the pain of recurrence of rebound dermatitis after drug withdrawal. Some external original preparations have poor effect, and hormone external preparations with stronger action need to be replaced, or the dosage is increased, or the medication interval time is shortened, so as to improve symptoms; the amount of the medicine used is in direct proportion to the length of the disease course during treatment, and the longer the disease course, the more the medicine is used, the more the disease condition is serious. Hormone-dependent side effects are mainly manifested by recurrent attacks of disease, appearance of acneiform changes, persistent dryness of the skin, increased sensitivity and color spots; after the moderate and severe hormone-dependent dermatitis is clinically cured, secondary pigmentation can occur, and a great mental burden is brought to patients, particularly women who suffer from facial diseases. The female proportion of patients with facial hormone-dependent dermatitis is far greater than the male proportion, except for a part of the female patients with definite history of externally applied hormone medicines, the other patients with no history of externally applied medicines have definite history of externally applied cosmetics, particularly the history of externally applied effect cosmetics, all the symptoms are that facial dermatitis and acne appear after the patients are stopped or used for a period of time, the treatment with common medicines is ineffective, and skin lesions cannot be automatically removed. For hormone dependence, no specific therapy exists at present, and the treatment principle mainly comprises local protection and soothing, and more importantly, the self-renewal effect of the skin is promoted. The disease is slow to recover due to the long passage time of epidermis, and the addition of hormone causes epidermis nutrition disorder and the damage of epidermis barrier function. The curative effect of the traditional Chinese and western medicine combined method for treating the disease is definite; in the treatment process after the hormone preparation is stopped, the patient repeatedly has the symptoms of hormone rebound, the symptoms are reduced by two times and increased by five or six times, the time for clinical cure is at least two months, and the time for clinical cure is two years, and the cure time is in a positive proportion to the strength and the time of the hormone preparation externally applied to the patient; the skin sensitivity is still high after the facial skin damage of the patient completely disappears, and longer time is still needed for complete recovery; secondary pigmentation is also a problem after the patient is cured. Therefore, the treatment time of the hormone-dependent dermatitis is long, the curative effect is not obvious, the psychological stress of patients is large, the problems exist, and psychological counseling plays an important role in helping the patients to firmly and thoroughly cure the dermatitis and improving the curative effect; facial hormonal dermatitis has a problem of skin sensitivity.
Disclosure of Invention
In view of the problems in the prior art, the invention discloses extracellular matrix beta-myoglycan protein, which adopts the technical scheme that the extracellular matrix beta-myoglycan protein comprises the following main components in parts by weight:
use of extracellular matrix beta-myosin in cosmetics.
The extracellular matrix beta-myoglycan protein is applied to the preparation of cosmetics for repairing hormone-dependent skin, and cosmetics for improving skin morphology and repairing skin hormone dependence can be obtained.
The glucan is a homotype polysaccharide which is composed of glucose as monosaccharide, and glucose units are connected by glycosidic bonds. The beta-glucan active structure is a polysaccharide composed of glucose units, most of which are bound by beta-13, which is the way glucose chains are linked. It can activate macrophage, neutrophilic leucocyte, etc., so that it can raise the content of leukocytin, cytokinin and special antibody, and can stimulate the immune system of body comprehensively. The body is more prepared against diseases caused by microorganisms. The beta-glucan can quickly restore the capability of lymphocyte of an injured organism to generate cell factors and effectively regulate the immune function of the organism.
Experiments show that the beta-glucan can promote the generation of IgM antibodies in vivo so as to improve the immunity of body fluid. Such glucan-activated cells stimulate host non-specific defense mechanisms, and thus are attracting much attention for applications in tumors, infectious diseases, and wound healing. Beta-13 glucan extracted by a special step and free from endotoxin is recognized as a safe substance by the FDA in the United states, can be added into general foods, and has the effects of scavenging free radicals, resisting radiation, dissolving cholesterol, preventing hyperlipidemia and resisting infection caused by filtering virus, fungi, bacteria and the like. Therefore, the method is widely applied to industries such as medicine, food, cosmetics and the like. Yeast glucan is now industrialized, and gels made from glucan are often used for biochemical separations such as column chromatography.
Fermenting with sucrose to obtain a chemically modified dextran named as Sephadex. The dextran has cross-linked network structure in its molecule, and can be used as molecular sieve to separate low molecular weight compound from high molecular weight compound.
Elastin is the main component of elastic fibres. Elastic fibers are found primarily in ligaments and vessel walls. The presence of elastic fibers in combination with collagen fibers imparts elasticity and tensile strength to the tissue. Although elastin represents only 2% of the total dermal protein, it plays an important role in skin elasticity. Elastin is the major cause of sagging, drooping and fine wrinkles resulting from skin aging, and as skin naturally ages, elastic fibers break down more and more significantly, with most elastic fibers being affected.
Elastin is the main component of the elastic fibers in the rawhide tissue. The peptide chain of elastin contains 713 or more amino acid residues. Unlike collagen and keratin, elastin has an amino acid sequence in which there is no continuous repetitive periodic structure throughout the peptide chain, but there are alternating hydrophobic and hydrophilic skin segments. Desmosine and open-chain desmosine formed from oxidized lysyl are unique cross-linked structures of elastin. These cross-linked structures are combined in more than two pairs.
Connective tissue is one of the major scleroproteins in the elastic tissues of inter alia tendons and arteries. Is a water-insoluble and high-crossing hydrolyzed protein. The elastin molecule contains nonpolar amino acid 95%, glycine content close to 1/3 of the total amount, proline 10%, and hydroxyproline 1%.
The natural elastin is surrounded by a shell composed of microfibrils. Microfibrils are composed of several glycoproteins. Necessary to maintain the integrity of the elastic fiber. Within developing elastic tissue, glycoprotein microfibrils often appear prior to elastin, and appear to be the framework for elastin attachment, having a organizing effect on the assembly of elastin molecules into elastic fibers. The production of elastin in aged tissues is reduced and degradation is enhanced, such that the tissues lose elasticity.
Elastin constitutes an elastic fiber, which is a fiber having rubber-like elasticity, can be elongated several times and restored to its original shape, which is a major factor of the elasticity of connective tissues, and is therefore known as "human rubber". The presence of elastic fibers in combination with collagen fibers imparts elasticity and tensile strength to the tissue. Elastin is less widespread than collagen, but is also present in large quantities in tissues such as elastic-rich tissues, lungs, aorta, certain ligaments, skin and ear cartilages.
Although the elastin accounts for about 2% -3% of the skin, the elastin can activate fibroblasts, provide structural assistance for the skin, and make the skin compact and elastic, elastin amino acids are amino acids for synthesizing elastin, like collagen, elastin in the skin is also provided by the synthesis of fibroblasts, and in human dermal tissue, the ratio of elastin to collagen is 4; the cosmetic containing elastin can supplement elastin content in aged skin, increase skin softness, and lubricate skin stratum corneum; elastin has a better affinity for skin than collagen.
The elastin-like protein is artificially synthesized by imitating the characteristics of natural elastin amino acid sequence. Because of its good biocompatibility and the ability to precisely control its environmental reactivity, mechanical properties and cell metabolism pathways by recombinant DNA technology design at the gene level, elastin-like proteins are becoming popular substitutes in the development process of biomimetic collagen. Keeping the youth of skin is the key point of collagen supplement, and in fact, elastin is more important. Elastin acts as a rubber band in the skin, allowing the skin to stretch and fold, functioning as a spring in a mattress, responsible for maintaining and supporting the elasticity of the skin. Therefore, elastin plays an important role in maintaining skin elasticity.
Serum protein is usually the most abundant protein in plasma, each molecule of the protein can carry 7 fatty acid factors, and the fatty acid factors are combined in the gaps of the protein and can be buried in the gaps with carbon tails, so that some water molecules around the protein are safely avoided. Blood cells are removed from blood, the remaining components are plasma, the plasma-removed fibrinogen belongs to serum, the serum contains relatively much albumin and globulin, and the albumin is usually generated in the liver and mainly maintains the nutrition of the body.
Serum proteins are carriers of fatty acids in the blood. When the body requires energy or building materials, the fat cells release fatty acids into the blood, which are captured by serum proteins and transported to the desired site. Serum proteins are the most abundant proteins in plasma. Each protein molecule can carry seven fatty acid molecules. These fatty acid molecules are bound in the crevices of the protein, and their carbon-rich tails are buried inside to safely avoid surrounding water molecules. Serum proteins are also capable of carrying many other water insoluble molecules. In particular serum proteins, are capable of carrying a number of drug molecules, such as ibuprofen.
Just as serum protein is so ubiquitous in blood and so easily purified, it has become one of the earliest proteins studied by scientists. When a protein is required, a similar protein from bovine sources is widely used in research and is called bovine serum albumin or BSA. Many enzymes are unstable in dilute solutions and the solution is to add some bovine serum proteins. It stabilizes the enzyme in the assay and is relatively neutral and does not affect the properties of the enzyme.
The serum protein is the protein in the serum as the name implies, and has two components in the serum, one is albumin, and the other is globulin. Albumin is produced in the liver, has a very small molecular weight but a very high density, and plays an important role in maintaining the nutrition of the body and the colloid osmotic pressure in the human body.
Clinically, if the serum protein concentration of an organism is lower than 25g/L, the colloid osmotic pressure of a human body is reduced, and then water in blood vessels seeps out of the blood vessels, so that the condition of tissue edema is caused. In addition, globulin is an antibody secreted by B lymphocytes, has a large molecular weight and mainly plays an important role in humoral immunity.
In a preferred embodiment of the present invention, the serum protein is an animal protein.
In a preferred embodiment of the present invention, the elastin is bonito protein.
In a preferred embodiment of the present invention, the yeast β -glucan is derived from baker's yeast.
As a preferable technical scheme of the invention, the beta-glucan is taken from oat.
The invention has the beneficial effects that: the invention provides extracellular matrix beta-myoglycan protein, which contains beta-glucan, elastin, serum protein and yeast beta-glucan and can activate macrophages, neutrophilic leukocytes and the like, so that the content of leukocidin, cytokinin and special antibodies can be increased.
Detailed Description
Example 1
The embodiment discloses a first implementation mode of the invention, which adopts the technical scheme that the main components and the weight parts of the components are as follows:
the extracellular matrix beta-myoglycan protein is applied to cosmetics for repairing hormone-dependent skin, and cosmetics for improving skin morphology, delaying skin aging process and repairing hormone dependence can be obtained, wherein yeast beta-glucan can activate macrophages, so that the ability of lymphocytes of injured organisms to generate cytokines can be quickly restored to be normal, and the skin can be repaired.
Example 2
The embodiment discloses a second implementation mode of the invention, which adopts the technical scheme that the main components and the weight parts of the components are as follows:
the extracellular matrix beta-myoglycan protein is applied to cosmetics for repairing hormone-dependent skin, and cosmetics for improving skin morphology, delaying skin aging process and repairing hormone-dependent skin can be obtained, wherein the yeast beta-glucan can enhance the expression level of antibodies, so that the ability of lymphocytes of injured organisms to generate cytokines can be quickly recovered to be normal, and the skin can be repaired.
Example 3
The embodiment discloses a third implementation mode of the invention, which adopts the technical scheme that the main components and the weight parts of the components are as follows:
the extracellular matrix beta-myoglycan protein is applied to cosmetics for repairing hormone-dependent skin, and cosmetics for improving skin morphology, delaying skin aging process and repairing hormone-dependent skin can be obtained, wherein yeast beta-glucan can activate macrophages and enhance the expression level of antibodies, so that the ability of lymphocytes of an injured organism to generate cytokines is quickly recovered to be normal, and the skin is repaired.
In a preferred embodiment of the present invention, the serum protein is an animal protein.
In a preferred embodiment of the present invention, the elastin is bonito protein.
In a preferred embodiment of the present invention, the yeast β -glucan is derived from baker's yeast.
As a preferable technical scheme of the invention, the beta-glucan is taken from oat.
The preparation method of the cosmetic containing the extracellular matrix beta-myoglycan protein comprises the following steps:
(1) Adding 20 parts of triethanolamine into the jacketed kettle, and heating the steam to 70 ℃;
(2) Adding 100 parts of deionized water into the jacketed kettle;
(3) Adding 25 parts of beta-glucan, 50 parts of elastin, 35 parts of serum protein and 15 parts of yeast beta-glucan into the jacketed kettle in sequence;
(4) Stirring for 25 minutes;
(5) Adding 2 parts of chlorhexidine;
(6) Cooling to 25 ℃;
(7) Storing and aging for 24 hours;
(8) Sterilizing by irradiation and filling.
Parts not described in detail herein are prior art.
Although the present invention has been described in detail with reference to the specific embodiments, the present invention is not limited to the above embodiments, and various changes and modifications without inventive changes may be made within the knowledge of those skilled in the art without departing from the spirit of the present invention.
Claims (9)
1. The extracellular matrix beta-myoglycan protein is characterized by comprising the following main components in parts by weight: 20-30 parts of beta-glucan, 40-60 parts of elastin, 30-40 parts of serum protein and 10-20 parts of yeast beta-glucan.
2. The extracellular matrix beta-myoglycan protein of claim 1, comprising the following major components in parts by weight: 20 parts of beta-glucan, 40 parts of elastin, 30 parts of serum protein and 10 parts of yeast beta-glucan.
3. The extracellular matrix beta-myoglycan protein of claim 1, comprising the following major components in parts by weight: 30 parts of beta-glucan, 60 parts of elastin, 40 parts of serum protein and 20 parts of yeast beta-glucan.
4. The extracellular matrix beta-myoglycan protein according to claim 1, comprising the following main components in parts by weight: 25 parts of beta-glucan, 50 parts of elastin, 35 parts of serum protein and 15 parts of yeast beta-glucan.
5. The extracellular matrix β -myoglycan protein of claim 1, characterized by: the serum protein is animal protein.
6. The extracellular matrix β -myoglycan protein of claim 1, characterized by: the elastin is bonito protein.
7. The extracellular matrix β -myoglycan protein of claim 1, characterized by: the yeast beta-glucan is obtained from baker's yeast.
8. The extracellular matrix β -myoglycan protein of claim 1, characterized by: the beta-glucan is obtained from oat.
9. Use of an extracellular matrix beta-myoglycan protein according to claim 1 in a cosmetic for repairing hormone-dependent skin.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210459406.0A CN115634169A (en) | 2022-04-27 | 2022-04-27 | Application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210459406.0A CN115634169A (en) | 2022-04-27 | 2022-04-27 | Application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN115634169A true CN115634169A (en) | 2023-01-24 |
Family
ID=84940541
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202210459406.0A Pending CN115634169A (en) | 2022-04-27 | 2022-04-27 | Application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN115634169A (en) |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108283597A (en) * | 2018-04-25 | 2018-07-17 | 佛山娇芙生物科技有限公司 | A kind of polypeptide ageing-resistant skin care composition and its application |
| CN108324674A (en) * | 2018-03-26 | 2018-07-27 | 广东巴松那生物科技有限公司 | A kind of creme of cosmetic complex and preparation method thereof containing actin |
| CN109430831A (en) * | 2018-10-31 | 2019-03-08 | 吉林省恒实传食品科技发展有限公司 | A kind of beautifying face and moistering lotion anti-aging health care's food formula and preparation method thereof |
| CN111973620A (en) * | 2019-05-21 | 2020-11-24 | 浙江立恩生物科技有限公司 | Biological polysaccharide for preventing and treating hormone-dependent dermatitis and application thereof |
| CN112353736A (en) * | 2020-09-18 | 2021-02-12 | 广州真极和美生物科技有限公司 | Skin-care conditioning cream for repairing hormone face |
| CN113648239A (en) * | 2021-09-01 | 2021-11-16 | 广州市万千粉丝化妆品有限公司 | Oligonucleotide skin care preparation synthesized by polyprotein and oligopeptide and having anti-wrinkle repairing effect |
-
2022
- 2022-04-27 CN CN202210459406.0A patent/CN115634169A/en active Pending
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108324674A (en) * | 2018-03-26 | 2018-07-27 | 广东巴松那生物科技有限公司 | A kind of creme of cosmetic complex and preparation method thereof containing actin |
| CN108283597A (en) * | 2018-04-25 | 2018-07-17 | 佛山娇芙生物科技有限公司 | A kind of polypeptide ageing-resistant skin care composition and its application |
| CN109430831A (en) * | 2018-10-31 | 2019-03-08 | 吉林省恒实传食品科技发展有限公司 | A kind of beautifying face and moistering lotion anti-aging health care's food formula and preparation method thereof |
| CN111973620A (en) * | 2019-05-21 | 2020-11-24 | 浙江立恩生物科技有限公司 | Biological polysaccharide for preventing and treating hormone-dependent dermatitis and application thereof |
| CN112353736A (en) * | 2020-09-18 | 2021-02-12 | 广州真极和美生物科技有限公司 | Skin-care conditioning cream for repairing hormone face |
| CN113648239A (en) * | 2021-09-01 | 2021-11-16 | 广州市万千粉丝化妆品有限公司 | Oligonucleotide skin care preparation synthesized by polyprotein and oligopeptide and having anti-wrinkle repairing effect |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN102229705B (en) | Collagen temperature-sensitive hydrogel and preparation method thereof | |
| Gabbiani et al. | Reparative processes in mammalian wound healing: the role of contractile phenomena | |
| JP5118018B2 (en) | Plant-derived elastin-binding protein ligand and method of use thereof | |
| JPH01265970A (en) | Collagen water solution or water dispersion solution including hyaluronic acid | |
| CN107308494A (en) | A kind of injection collagen, preparation method and filler | |
| CN102166166B (en) | Method and application using compounds from fetal cells and tissues to improve skin condition | |
| CN112294668B (en) | Hyaluronic acid injection | |
| JPH03502919A (en) | Cosmetic agents and skin treatment compositions | |
| CN110339398A (en) | One kind Amvisc containing amino acid and preparation method thereof | |
| CN107189119A (en) | A kind of preparation method and applications of compound sodium hyaluronate collagen hydrogels | |
| KR100828494B1 (en) | A composition of a cosmetic essense and the method of prepating it for improvenent of wrinkle | |
| TW201517930A (en) | Use of starfish extract for manufacture of composition for enhancing secretion of collagen | |
| CN114796011A (en) | Composite solution for combined application of recombinant III-type humanized collagen and hyaluronic acid and preparation process thereof | |
| CN113521258A (en) | Tissue injection for improving aging | |
| CN105749333A (en) | Medical dressing of hyaluronic acid and preparation method of medical dressing | |
| CN109700998A (en) | A kind of compound skin injury regeneration renovation agent and preparation method thereof | |
| CN115634169A (en) | Application of extracellular matrix beta-myoglycan protein in cosmetics for repairing hormone-dependent skin | |
| Forrest et al. | Comparative studies on the insoluble collagens of guinea-pig dermis and dermal scar tissue | |
| CN113576971B (en) | Fibronectin freeze-dried powder preparation and preparation method thereof | |
| EP3563829A1 (en) | Cosmetic composition | |
| US20090023631A1 (en) | Composition and Method of Use for Soft Tissue Augmentation/Drug Delivery | |
| CN104436168A (en) | Composition for promoting cell regeneration and preparation method and purpose thereof | |
| CN112754981A (en) | Collagen regeneration promoting preparation and preparation method and application thereof | |
| CN100562306C (en) | Contain the biological beauty skin care item of body keratinized cell growth factor-2 and the preparation method of recombinant human keratinized cell growth factor-2 | |
| CN105734102B (en) | The preparation method of collagen peptide |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| RJ01 | Rejection of invention patent application after publication | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20230124 |