CN113527468A - 一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构 - Google Patents
一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构 Download PDFInfo
- Publication number
- CN113527468A CN113527468A CN202110886161.5A CN202110886161A CN113527468A CN 113527468 A CN113527468 A CN 113527468A CN 202110886161 A CN202110886161 A CN 202110886161A CN 113527468 A CN113527468 A CN 113527468A
- Authority
- CN
- China
- Prior art keywords
- collagen
- bone
- skin
- amino acid
- promoting skin
- 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
- 102000008186 Collagen Human genes 0.000 title claims abstract description 47
- 108010035532 Collagen Proteins 0.000 title claims abstract description 47
- 229920001436 collagen Polymers 0.000 title claims abstract description 47
- 210000003491 skin Anatomy 0.000 title claims abstract description 17
- 210000000988 bone and bone Anatomy 0.000 title claims abstract description 16
- 230000001737 promoting effect Effects 0.000 title claims abstract description 13
- 230000004221 bone function Effects 0.000 title claims abstract description 9
- 230000004215 skin function Effects 0.000 title claims abstract description 9
- 230000004220 muscle function Effects 0.000 title claims abstract description 7
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 22
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 4
- 210000003205 muscle Anatomy 0.000 abstract description 8
- 230000006870 function Effects 0.000 abstract description 5
- 150000001413 amino acids Chemical group 0.000 description 10
- 210000004027 cell Anatomy 0.000 description 10
- 230000000694 effects Effects 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 4
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 4
- 239000013078 crystal Substances 0.000 description 4
- 210000002950 fibroblast Anatomy 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 3
- 210000002449 bone cell Anatomy 0.000 description 3
- 230000004663 cell proliferation Effects 0.000 description 3
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 229960002591 hydroxyproline Drugs 0.000 description 3
- 125000001841 imino group Chemical group [H]N=* 0.000 description 3
- 210000000963 osteoblast Anatomy 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 230000009878 intermolecular interaction Effects 0.000 description 2
- 210000000663 muscle cell Anatomy 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 210000001626 skin fibroblast Anatomy 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 206010002091 Anaesthesia Diseases 0.000 description 1
- 206010010356 Congenital anomaly Diseases 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- YQEZLKZALYSWHR-UHFFFAOYSA-N Ketamine Chemical compound C=1C=CC=C(Cl)C=1C1(NC)CCCCC1=O YQEZLKZALYSWHR-UHFFFAOYSA-N 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 238000005411 Van der Waals force Methods 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 210000000683 abdominal cavity Anatomy 0.000 description 1
- 238000002679 ablation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000037005 anaesthesia Effects 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000007640 basal medium Substances 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 208000018631 connective tissue disease Diseases 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 239000001257 hydrogen Chemical group 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 230000008863 intramolecular interaction Effects 0.000 description 1
- 229960003299 ketamine Drugs 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000003098 myoblast Anatomy 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000002997 osteoclast Anatomy 0.000 description 1
- 210000000062 pectoralis major Anatomy 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 210000000515 tooth Anatomy 0.000 description 1
- 238000009966 trimming Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0821—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp
- C07K5/0823—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp and Pro-amino acid; Derivatives thereof
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
本发明公开了一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,胶原蛋白肽的氨基酸序列为Pro‑Hyp‑Gly。本发明采用上述的一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,胶原三肽结构稳定,有效的促进皮肤和骨骼、肌肉的发育。
Description
技术领域
本发明涉及胶原蛋白技术领域,尤其是涉及一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构。
背景技术
胶原蛋白是很多脊椎动物和无脊椎动物体内含量最丰富的蛋白质,属于结构蛋白质,是皮肤、骨、软骨、血管和牙齿的主要纤维成分,存在于所有的器官中。
胶原的高机械强度与胶原的蛋白质结构有密切的关系。在胶原蛋白中,特殊的氨基组成使其具有稳定的三股螺旋结构,氨基酸和肽链之间的各种作用力维持着胶原的稳定,而胶原的性能特点正是氨基酸序列排布的外在反映。
胶原的氨基酸排列可以引发某些氨基酸残基的变异,使原来的稳定性丧失,并引发病变。性质依赖结构,胶原的稳定性是其特殊结构的外在表现。对于先天性和后天性结缔组织病变的人群,其胶原蛋白的结构具有重要意义。
发明内容
本发明的目的是提供一种促进皮肤、骨骼功能的胶原蛋白肽,胶原结构稳定,有效的促进皮肤和骨骼的发育。
为实现上述目的,本发明提供了一种促进皮肤、骨骼功能的胶原蛋白肽,胶原蛋白肽的基础氨基酸序列为Pro-Hyp-Gly。
优选的,胶原蛋白肽的浓度为1-5μg/mL。
优选的,胶原蛋白的衍生序列在基础氨基酸序列的基础上进行扩展,氨基酸的序列不大于10个,其分子量不大于1200Da。
因此,本发明采用上述一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,三肽结构稳定,通过脯氨酸、羟脯胺酸、甘氨酸这种定向三肽结构,对皮肤骨骼发育效果明显好,促进身体的功能增强。
胶原螺旋的稳定性有赖于分子间和分子内各种作用的协同效应,亚氨基酸、氢键、范德华力以及水化作用,在稳定胶原分子结构上共同作用,而疏水作用和离子作用提供分子间作用力。但是,胶原蛋白的氨基酸序列决定了分子的稳定性和分子间作用。本发明的胶原蛋白肽通过高含量的亚氨基酸(脯氨酸、羟脯氨酸)提高螺旋的稳定性。甘氨酸通过优化多肽链折叠中的构想范围,提高其稳定性。脯氨酸的羟基化在螺旋结构提高稳定性。脯氨酸、羟脯胺酸均为亚氨基酸,提高了三股螺旋结构的稳定性。
下面通过实施例,对本发明的技术方案做进一步的详细描述。
具体实施方式
以下通过实施例对本发明的技术方案作进一步说明。
一种促进皮肤、骨骼功能的胶原蛋白肽,胶原蛋白肽的基础氨基酸序列为Pro-Hyp-Gly。胶原蛋白肽的浓度为1-5μg/mL。
胶原蛋白的衍生序列在基础氨基酸序列的基础上进行扩展,氨基酸的序列不大于10个,其分子量为1200Da。
试验测试
(一)胶原蛋白肽对成纤维细胞的影响
人皮肤成纤维细胞(Hs27细胞(ATCC))使用完全培养基进行培养,完全培养基主要由基础培养基高糖DMEM、10%胎牛血清(v/v)、1%双抗(青霉素和链霉素)组成。
将成纤维细胞置于37℃、5%CO2的培养箱中,每隔2d换液1次。待细胞长满培养瓶的90%左右,取其接种于96孔培养板中,每孔100μL,浓度为5×104cells/mL。细胞生长24h后,吸弃培养液,用200μLPBS洗1次。再加入200μLPBS,用80mJ/cm2UVB照射,吸弃PBS。其中试验组每孔加入200μL 2μg/mL的三肽型胶原蛋白肽,对照组加入等量的PBS,继续培养72h后,吸弃培养液,检测细胞存活率。
结果发现,试验组的成纤维细胞数量明显多于对照组的成纤维细胞数量。
(二)胶原蛋白肽含量的变化
将Hs27皮肤成纤维细胞在24孔培养容器中散布各1*104个之后,在5%CO2、37℃下培养24h后,试验组每孔加入200μL 2μg/mL的三肽型胶原蛋白肽,对照组加入等量的PBS,再培养72h后。用结晶紫法测定细胞的增殖。
再除去各孔的培养基之后,每1孔添加500ml的0.1%结晶紫溶液并染色5分钟之后,除去结晶紫溶液,用蒸馏水清洗3次并重复进行4次,至孔成为清澈。再添加95%乙醇1ml并搅拌20min,使细胞所染色的结晶紫溶解。将该溶液以各孔200ml分配到96孔容器中,针对试验组与对照组计算相对的细胞增殖。
结果发现,试验组的成纤维细胞数量明显多于对照组的成纤维细胞数量。
(三)胶原蛋白肽对骨骼细胞的影响
通过骨细胞培养基对老鼠成骨细胞和破骨细胞培养24h后,分为对照组和试验组,试验组加入1mg/mL的三肽型胶原蛋白肽,对照组加入牛血清白蛋白,均再培养14d后,用荧光测定仪定量测定碱性磷酸酶活性,用显微镜观察培养基的成骨细胞图片。结果发现,试验组的碱性磷酸酶活性(2.13±0.85mU/105细胞)明显高于对照组(0.42±0.16mU/105细胞),胶原蛋白肽组成骨细胞性状改变,而牛血清白蛋白对照组组成骨细胞消融。
(四)胶原蛋白肽对肌肉细胞的影响
大鼠乙醚吸入麻醉后腹腔内注射氯胺酮(22mg/kg),以左侧第4肋水平作横切口,取胸大肌约1cm3,并将其修剪成1mm3大小的肌小粒。反复用Hanks液洗去血细胞,将肌小粒小心贴附于事先用明胶包被的细胞培养瓶底部,加入适量成肌细胞增殖培养液(Ham's F-10培养基中加入15%小牛血清、青霉素100U/ml、链霉素100U/ml)。将瓶底向上轻置于37℃、5%CO2、饱和湿度的培养箱中,4h后轻轻翻转培养瓶,使肌小粒浸浴于培养液中。3d换液一次,待细胞长满瓶底即可传代。
将传代的二代细胞取10μL加入新的培养瓶中,分为试验组和对照组,并分别加入200μL胶原蛋白肽、200μLPBS,进行培养。针对试验组与对照组计算相对的细胞增殖。
结果发现,试验组的肌肉细胞明显多于对照组的肌肉细胞数量。
因此,本发明采用上述一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,胶原三肽肽链结构稳定,有效的促进皮肤和骨骼、肌肉的发育。
最后应说明的是:以上实施例仅用以说明本发明的技术方案而非对其进行限制,尽管参照较佳实施例对本发明进行了详细的说明,本领域的普通技术人员应当理解:其依然可以对本发明的技术方案进行修改或者等同替换,而这些修改或者等同替换亦不能使修改后的技术方案脱离本发明技术方案的精神和范围。
Claims (3)
1.一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,其特征在于:胶原蛋白肽的三肽氨基酸序列为Pro-Hyp-Gly。
2.根据权利要求1所述的一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,其特征在于:胶原蛋白肽的浓度为1-5μg/mL。
3.根据权利要求1所述的一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构,其特征在于:胶原蛋白的衍生序列在基础氨基酸序列的基础上进行扩展,氨基酸的序列不大于10个,其分子量不大于1200Da。
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202110886161.5A CN113527468A (zh) | 2021-08-03 | 2021-08-03 | 一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202110886161.5A CN113527468A (zh) | 2021-08-03 | 2021-08-03 | 一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构 |
Publications (1)
Publication Number | Publication Date |
---|---|
CN113527468A true CN113527468A (zh) | 2021-10-22 |
Family
ID=78090251
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN202110886161.5A Pending CN113527468A (zh) | 2021-08-03 | 2021-08-03 | 一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构 |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN113527468A (zh) |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2014001182A (ja) * | 2012-06-20 | 2014-01-09 | Nitta Gelatin Inc | 骨、軟骨または皮膚に関連する疾患の治療もしくは予防剤 |
CN110869064A (zh) * | 2017-04-06 | 2020-03-06 | 莎思坦控股有限责任公司 | 基于胶原的药物组合物和装置和生产方法及其用途 |
US20200353056A1 (en) * | 2019-04-22 | 2020-11-12 | Sustain Holdings, Llc | Collagen peptide-based medicament compositions and devices and methods of production and use thereof |
-
2021
- 2021-08-03 CN CN202110886161.5A patent/CN113527468A/zh active Pending
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2014001182A (ja) * | 2012-06-20 | 2014-01-09 | Nitta Gelatin Inc | 骨、軟骨または皮膚に関連する疾患の治療もしくは予防剤 |
CN110869064A (zh) * | 2017-04-06 | 2020-03-06 | 莎思坦控股有限责任公司 | 基于胶原的药物组合物和装置和生产方法及其用途 |
US20200353056A1 (en) * | 2019-04-22 | 2020-11-12 | Sustain Holdings, Llc | Collagen peptide-based medicament compositions and devices and methods of production and use thereof |
Non-Patent Citations (1)
Title |
---|
MASAO TANIHARA 等: ""The biodegradability of poly(Pro-Hyp-Gly) synthetic polypeptide and the promotion of a dermal wound epithelialization using a poly(Pro-Hyp-Gly) sponge"", 《JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A》 * |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US8349589B2 (en) | Non-natural recombinant gelatins with enhanced functionality | |
US6268348B1 (en) | Synthetic compounds and compositions with enhanced cell binding | |
Ma et al. | Enhanced biological stability of collagen porous scaffolds by using amino acids as novel cross-linking bridges | |
Lee et al. | Collagen mimetic peptide-conjugated photopolymerizable PEG hydrogel | |
CN104395457B (zh) | 用于细胞培养的合成粘附培养基 | |
JP2019517355A (ja) | 3dバイオプリンティングバイオインクとしての細胞外マトリックス成分で修飾されたセルロースナノ原繊維の調製 | |
CN112980001B (zh) | 一种胶原蛋白复合透明质酸凝胶、细胞外基质仿生材料及制备方法 | |
Rossi et al. | Biologically and mechanically driven design of an RGD-mimetic macroporous foam for adipose tissue engineering applications | |
Kuo et al. | Surface modification with peptide for enhancing chondrocyte adhesion and cartilage regeneration in porous scaffolds | |
Mu et al. | A customized self-assembling peptide hydrogel-wrapped stem cell factor targeting pulp regeneration rich in vascular-like structures | |
Kuo et al. | Chondrogenesis in scaffolds with surface modification of elastin and poly-L-lysine | |
Lin et al. | Applications of marine collagens in bone tissue engineering | |
CN114276567A (zh) | 一种用于组织工程皮肤构建的仿生水凝胶支架及其制备方法 | |
US9157078B2 (en) | Cell-adhesive protein | |
Zhou et al. | Embryoid bodies formation and differentiation from mouse embryonic stem cells in collagen/Matrigel scaffolds | |
US5674848A (en) | Bioreactor compositions with enhanced cell binding | |
Nwe et al. | Selection of a biopolymer based on attachment, morphology and proliferation of fibroblast NIH/3T3 cells for the development of a biodegradable tissue regeneration template: Alginate, bacterial cellulose and gelatin | |
CN109943526A (zh) | 一种促间充质干细胞增殖的无血清多肽组合物 | |
CN113527468A (zh) | 一种促进皮肤、骨骼、肌肉功能的胶原蛋白三肽结构 | |
CN116333094A (zh) | 一种重组人源化I型胶原蛋白α1及表达载体和应用 | |
Hayashi et al. | 11 Fish Collagen and Tissue Repair | |
CN115521371A (zh) | 一种重组人源化iii型胶原蛋白、制备方法及应用 | |
CN114836377B (zh) | 一种干细胞体外成骨诱导分化方法 | |
KR101348096B1 (ko) | 줄기세포의 연골 분화 유도 활성을 가지는 폴리펩타이드 | |
Feng et al. | Collagen-based biomaterials in organoid technology for reproductive medicine: Composition, characteristics, and applications |
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 | ||
TA01 | Transfer of patent application right |
Effective date of registration: 20220722 Address after: Room 140, building 3, No. 161, Lane 465, Zhenning Road, Changning District, Shanghai 200050 Applicant after: AVIC (Shanghai) Biotechnology Co.,Ltd. Address before: 200000 south tower 2701-16, No. 300, Xuanhua Road, Changning District, Shanghai Applicant before: Shanghai jiaomei Trading Co.,Ltd. |
|
TA01 | Transfer of patent application right | ||
RJ01 | Rejection of invention patent application after publication |
Application publication date: 20211022 |
|
RJ01 | Rejection of invention patent application after publication |