CN104672329B - A kind of protein - Google Patents
A kind of protein Download PDFInfo
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- CN104672329B CN104672329B CN201510084726.2A CN201510084726A CN104672329B CN 104672329 B CN104672329 B CN 104672329B CN 201510084726 A CN201510084726 A CN 201510084726A CN 104672329 B CN104672329 B CN 104672329B
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- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 33
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 32
- 239000002773 nucleotide Substances 0.000 claims abstract description 12
- 125000003729 nucleotide group Chemical group 0.000 claims abstract description 12
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 11
- 102000009027 Albumins Human genes 0.000 claims abstract description 8
- 108010088751 Albumins Proteins 0.000 claims abstract description 8
- 210000002966 serum Anatomy 0.000 claims abstract description 7
- 239000003814 drug Substances 0.000 abstract description 5
- 241000588724 Escherichia coli Species 0.000 abstract description 2
- 230000002018 overexpression Effects 0.000 abstract description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 10
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 10
- 108090000765 processed proteins & peptides Proteins 0.000 description 9
- 150000001413 amino acids Chemical class 0.000 description 5
- 238000000034 method Methods 0.000 description 5
- 238000001262 western blot Methods 0.000 description 5
- 230000014509 gene expression Effects 0.000 description 4
- 210000002381 plasma Anatomy 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 230000027455 binding Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 208000017667 Chronic Disease Diseases 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 239000004606 Fillers/Extenders Substances 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 206010029164 Nephrotic syndrome Diseases 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 108010065323 Tumor Necrosis Factor Ligand Superfamily Member 13 Proteins 0.000 description 1
- 102000013081 Tumor Necrosis Factor Ligand Superfamily Member 13 Human genes 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-N ammonia Natural products N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000003809 bile pigment Substances 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000013024 dilution buffer Substances 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000002526 effect on cardiovascular system Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000005611 electricity Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 208000009928 nephrosis Diseases 0.000 description 1
- 231100001027 nephrosis Toxicity 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000012557 regeneration buffer Substances 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 239000003270 steroid hormone Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 230000009182 swimming Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
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- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Peptides Or Proteins (AREA)
Abstract
Present invention discloses a kind of protein, nucleotide sequence and amino acid sequence.Protein and human serum albumins (HSA) proposed by the invention is specifically bound, compatibility increases compared with HSA antibody in the market, the protein can be used Escherichia coli and carry out soluble overexpression simultaneously, be expected to have good application in field of medical biology and biological medicine exploitation.
Description
Technical field
The invention belongs to genetic engineering field and Medical Immunology field, in particular to a kind of protein.
Background technique
Human serum albumins (Human Serum Albumin, abbreviation HSA) is protein important in people's blood, non-saccharide
The single chain polypeptide of base includes 585 amino acid, molecular weight 66kD.Its concentration is 42g/L in blood plasma, accounts for about the total egg of blood plasma
White 60%.Human serum albumins can be with transport of fatty acids, BILE PIGMENTS, amino acid, steroid hormone, metal ion in body fluid
With many treatment molecules etc., while maintaining the normal osmotic pressure of blood.Clinically human serum albumins can be used for treating shock
With burn, for supplementing because of operation, contingency or big bleeding caused by blood loss, can also be used as plasma extender.Together
When clinically by discovery patient be metabolized albumin exception, to speculate whether patient suffers from diabetes, nephrosis, cardiovascular and cerebrovascular
Chronic diseases.Therefore, be capable of providing it is a kind of can efficiently, the protein of specific binding HSA is of great significance.
HSA has very long Half-life in vivo (two weeks or so), therefore it is also main medicament transport in human plasma
Albumen, many drug peptide or proteins can effectively improve its dynamic metabolism characteristic in conjunction with human serum albumins in vivo,
Extend half-life period, improves its stability and physiological activity.International application WO 09/127691, entitled " Peptides
capable of binding to serum proteins and compounds,consteucts and
Polypeptides comprising the same (being capable of compound, structure in conjunction with the peptide of haemocyanin and comprising the peptide
Build body and polypeptide) " describe for generate can with peptide, the amino acid sequence in conjunction with seralbumin, in conjunction with peptide, amino
Acid sequence can combine or merge with therapeutic structure division, compound, albumen or other treatment entity to increase half-life period.
That develops in existing market can be with the protein less varieties in conjunction with HSA, and compatibility is inconsistent.Therefore height is filtered out
The protein of specific binding HSA is of great significance.
Summary of the invention
In view of the problems of the above-mentioned prior art, the purpose of the present invention is to propose to a kind of protein.
The purpose of the invention will be achieved through the following technical solutions: a kind of protein, the amino acid of the protein
Sequence is selected from:
(a) amino acid sequence as shown in SEQ ID NO.2 in sequence table；Or
(b) with 52-56,71-87,120-132,170- of amino acid sequence shown in SEQ ID NO.2 in sequence table
179, the amino acid sequence of 195-201,234-242 core sequences at least 85% similitude.
A kind of nucleotide sequence of protein described in coding, the nucleotide sequence are selected from:
(a) nucleotide sequence as shown in SEQ ID NO.1 in sequence table；Or
(b) with 154-168,211-261 of nucleotide sequence shown in SEQ ID NO.1 in sequence table, 358-396,
The nucleotide sequence of 508-537,583-603,700-726 core sequences at least 85% similitude.
Preferably, above-mentioned a kind of protein, wherein the protein and human serum albumins are specifically bound.
As used herein, " similitude " refer to be used to describe during nucleotide or amino acid alignment detection sequence and
Identical DNA base or the height of amino acid residue sequence proportion between target sequence, are a kind of direct quantitative relations, are led to
The same or similar percentage in part is crossed to measure similar degree between nucleotide sequence or amino acid sequence, this similitude
Percentage can be calculated by the existing comparison method in this field, and example has the comparison method FASTA program between sequence two-by-two
(Person,W.R.and Lipman,D.J.1988.Improved tools for biological sequence compa
Rison.Proc.Natl.Acad.Sci.85:2444-2448), blast program (Altschul, S.F., et
Al.1990Basic local alignment search tool.J.Mol.Biol.215:403-410) etc. or multisequencing ratio
To method CLUSTAL W (CORPET, F.1998Multiple sequence alignment with hierarchical
Clustering.Nucleic Acids Res., 16:10881-10890) etc..
There is provided a kind of protein that CDR region is different, DNA molecular nucleotide sequence such as SEQ for protrusion effect of the invention
Shown in ID NO.1, core function sequence is 154-168,211-261,358-396,508-537,583-603,700-726
Position；For protein molecule amino acid sequence as shown in SEQ ID NO.2, core function sequence is 52-56,71-87,120-
132,170-179,195-201,234-242.The protein can be specifically bound with HSA, with HSA antibody in the market
It increases compared to compatibility, while the protein can be used Escherichia coli and carry out soluble overexpression, be expected in medicine
There is good application in field of biology and biological medicine exploitation.
Just attached drawing in conjunction with the embodiments below, the embodiment of the present invention is described in further detail, so that of the invention
Technical solution is more readily understood, grasps.
Detailed description of the invention
Fig. 1 is 1pBZ1-1 vector construction schematic diagram of the embodiment of the present invention；
Fig. 2 is 2 recombinant bacterial strain abduction delivering schematic diagram of the embodiment of the present invention；
Fig. 3 is 3 protein purification result of the embodiment of the present invention；
Fig. 4 is april protein sample affinity measurement result of the embodiment of the present invention；
Fig. 5 is the HSA affinity of antibody measurement result in the market of the embodiment of the present invention 4；
Fig. 6 is 5 protein WESTERN-BLOTTING result of the embodiment of the present invention；
Fig. 7 is 6 protein WESTERN-BLOTTING result of the embodiment of the present invention.
Specific embodiment
Method of the invention is illustrated below by specific embodiment, but the present invention is not limited thereto.Following realities
Experimental method described in example is applied, is conventional method unless otherwise specified；The reagent and material, unless otherwise specified,
It obtains from commercial channels.
The building of 1 high specific combination HSA developed by molecule carrier of embodiment
Designed restriction enzyme is added by the DNA sequence dna of the artificial synthesized molecule, and at the both ends of its coded sequence
Enzyme site, recombinant clone to expression vector pBZ007, as shown in SEQ ID NO.1 in sequence table, Sequences upstream is added sequence
XhoI restriction enzyme site, the side that above-mentioned sequence is passed through gene chemical synthesis is added in NdeI restriction enzyme site, sequence downstream
Formula is connected into pBZ007 expression vector, is named as pBZ1-1, as shown in Figure 1, recombinant vector is transformed into host strain BL21 (DE3).
The inducing expression and identification of embodiment 2pBZ1-1 genetic engineering bacterium
30 DEG C of shake cultures of BL21 (DE3) containing pBZ1-1 are stayed overnight, then inoculum concentration switching and ammonia benzyl and card by 1%
In that dual anti-LB culture medium, when OD value is 0.6-0.8, the IPTG inducing expression 16h of final concentration of 0.6mM is added.
After being proportionally added into Loading buffer and PBS after centrifugation, thallus is resuspended in thallus 1ml after taking inducing expression,
5-10min is boiled into boiling water, takes 10 μ l to carry out SDS-PAGE electrophoresis after 12000rpm centrifugation 5min, while to be free of plasmid
BL21 (DE3) is as control.12% separation gel, 100V constant pressure, electrophoresis 2h, after electrophoresis, it is clear to band to decolourize, according to electricity
Swimming result will have apparent destination protein expression band, as a result as shown in Figure 2.
The purifying of 3 recombinant protein of embodiment
Induction bacterium is crushed after collecting, after 0.22 μm of membrane filtration, using the AKTA plus protein purification system of GE company
Chromatographic purifying recombinant protein.In single goal band, no miscellaneous band, as a result as shown in Figure 3 SDS-PAGE testing result shows.
The identification of embodiment 4 recombinant protein and HSA affinity
Coupling: affinity of the recombinant protein of purifying by biocore test measurement and HSA, it is special according to the isoelectric point of HSA
Property and according to Biacore × 100control soft protocol optimize coupling condition, select pH4.5 sodium acetate as
It is coupled dilution buffer, is coupled on CM5 chip after diluting HSA sample to 25 μ g/ml with this buffer, coupling is horizontal
1500RU。
KD test: with the Running buffer diluted protein matter sample of pH7.4, dilute a series of concentration to 0nM,
50nM,100nM,200nM,400nM,800nM.Setting binding time is 180s, Dissociation time 10min, regeneration buffer use
50mMpH1.7.Gly-HCl.Examination with computer is carried out according to the protocol of Biacore × 100control soft.
Data processing: it is analyzed using the included analysis software in Biacore × 100.Data are interpreted, and protein sample KD is
1.444E (- 12) M, as a result as shown in Figure 4；Simultaneously operation the preferable HSA antibody KD of performance currently on the market be 5.090E (-
10) M, as a result as shown in Figure 5.
The results show that the protein molecule affinity in the present invention is substantially better than, to show preferable HSA currently on the market anti-
Body.
The WESTERN-BLOTTING of 5 recombinant protein of embodiment is identified
Recombinant protein passes through SDS-PAGE, then is detected with the HSA of HRP label, carries out WESTERN-BLOTTING, as a result
Display recombinant protein can be specifically bound with HSA, as a result as shown in Figure 6.
The similitude of embodiment six amino acid sequence
SEQ ID NO.3, SEQ ID NO.4, SEQ ID NO.5 are the 52- with SEQ ID NO.2 respectively in sequence table
56,71-87,120-132,170-179,195-201,234-242 core sequences have 85%, 90%, 95% similitude
Amino acid sequence.The preparation method and reality of SEQ ID NO.3, SEQ ID NO.4, the corresponding recombinant protein of SEQ ID NO.5
The preparation method for applying the recombinant protein of SEQ ID NO.2 in a 1-3 is consistent.
With embodiment 5, SEQ ID NO.2, SEQ ID NO.3, SEQ ID NO.4 and SEQ ID NO.5 are carried out
WESTERN-BLOTTING, as a result as shown in fig. 7, SEQ ID NO.2 and SEQ ID NO.3, SEQ ID NO.4, SEQ ID
The recombinant protein of NO.5 bioactivity having the same has similar high pathoklisis with HSA.
Still there are many embodiment, all technical sides formed using equivalents or equivalent transformation by the present invention
Case is within the scope of the present invention.
Claims (3)
1. a kind of protein, which is characterized in that the amino acid sequence of the protein is selected from:
The amino acid sequence as shown in SEQ ID NO.2 in sequence table.
2. a kind of nucleotide sequence for encoding protein described in claim 1, which is characterized in that the nucleotides sequence column selection
From:
The nucleotide sequence as shown in SEQ ID NO.1 in sequence table.
3. a kind of protein according to claim 1, which is characterized in that the protein and human serum albumins specificity
In conjunction with.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510084726.2A CN104672329B (en) | 2015-02-16 | 2015-02-16 | A kind of protein |
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| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510084726.2A CN104672329B (en) | 2015-02-16 | 2015-02-16 | A kind of protein |
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| Publication Number | Publication Date |
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| CN104672329A CN104672329A (en) | 2015-06-03 |
| CN104672329B true CN104672329B (en) | 2019-08-06 |
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Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN105273079B (en) * | 2015-11-26 | 2018-07-06 | 张癸荣 | The screening and application of human serum albumin dominant antigen epitope |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101646689A (en) * | 2006-09-08 | 2010-02-10 | 埃博灵克斯股份有限公司 | Serum albumin binding proteins with long half-lives |
| CN102089325A (en) * | 2008-04-17 | 2011-06-08 | 埃博灵克斯股份有限公司 | Peptides capable of binding to serum proteins and compounds, constructs and polypeptides comprising the same |
| CN102875675A (en) * | 2012-04-26 | 2013-01-16 | 拜明(苏州)生物技术有限公司 | Anti-human serum albumin single-chain antibody and method for connecting polypeptide medicine with nitrogen terminal of antibody |
-
2015
- 2015-02-16 CN CN201510084726.2A patent/CN104672329B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101646689A (en) * | 2006-09-08 | 2010-02-10 | 埃博灵克斯股份有限公司 | Serum albumin binding proteins with long half-lives |
| CN102089325A (en) * | 2008-04-17 | 2011-06-08 | 埃博灵克斯股份有限公司 | Peptides capable of binding to serum proteins and compounds, constructs and polypeptides comprising the same |
| CN102875675A (en) * | 2012-04-26 | 2013-01-16 | 拜明(苏州)生物技术有限公司 | Anti-human serum albumin single-chain antibody and method for connecting polypeptide medicine with nitrogen terminal of antibody |
Non-Patent Citations (1)
| Title |
|---|
| Development and characterization of small bispecific albumin-binding domains with high affinity for ErbB3;Johan Nilvebrant et al;《Cell Mol Life Sci》;20130602;3973-3985 |
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Effective date of registration: 20151127 Address after: Unit Ell7 No. 218 BioBAY Al building in Suzhou Industrial Park in Suzhou city of Jiangsu Province, 215000 Star Lake Street Applicant after: Suzhou Zhisheng biological science and Technology Co Ltd Address before: 214122 Jiangsu Province, Wuxi City Lake Road No. 1800 National Engineering Laboratory A403 Applicant before: Yang Yankun Applicant before: Yang Dong Applicant before: Zhang Pipi |
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