Peptide modification
| 【Numbering】BK2021071302 | 【CAS】CAS | ||
| 【Item No.】 | 【specification】 | ||
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Peptide modification
Peptides are active substances that realize various functions in organisms. The modification of peptides is mainly the modification of the main chain structure and side chain groups of the peptide chain. Peptides can be changed by modification
The physicochemical properties of these compounds optimize their effective utilization in the body. Modified peptide drugs can significantly reduce immunogenicity, reduce toxic effects,
Increase water solubility, prolong the action time in the body, change the distribution in the body, and so on. Common peptide modifications include: C-terminal modification, N-terminal modification, intermediate residue modification,
And cyclization modification.
In addition to conventional linear peptides, Synthbio is now sufficient to meet your needs for a variety of cyclic peptides, modified peptides and special peptides, including: N/C terminal modification
Decoration, antigen peptide, fluorescent label, cyclic peptide, biotin label and PEGylation, etc. The peptide modification service provided by Synbiotics includes
But not limited to the following types:
☆N-terminal modification/C-terminal modification
☆Disulfide bond modification
☆A(yù)mide bond to form a ring
☆Fluorescent marking
☆Biotin labeled peptide
☆Carrier protein coupling and MAPs
☆Unnatural amino acid/D type amino acid
☆Phosphorylation and sulfonation modification
☆Linker, spacers PEGylation
☆Penetrating peptide
1. Amidation and acetylation
If the synthetic peptide is the internal sequence of the protein, the charge of the peptide can be removed by N-terminal acetylation or C-terminal amidation to make it more toward the natural structure of the protein.
Enhance the resistance of the polypeptide to endopeptidase.
2. Biotin and FITC labeling
For peptides labeled with biotin at the carboxyl end, lysine needs to be added to the carboxyl end, and then biotin is attached to the side chain of lysine, which eliminates lysine
The positive charge of the acid. FITC is a fluorescently labeled active precursor. In order to effectively label the N-terminus, a seven-carbon 6-aminocaproic acid can be inserted between the N-terminus of the polypeptide and the fluorescent group.
3. Disulfide bond modification
The formation of disulfide bonds between cysteine residues can realize polypeptide cyclization, but because disulfide bonds are formed randomly, for polypeptides containing multiple cysteine residues,
This is a challenge. Synbiotics can construct disulfide bonds between designated cysteines, and we can introduce three pairs of disulfide bonds in a polypeptide location.
4. Multiple phosphorylation
Peptide phosphorylation can help to study the effect of phosphorylation on the structure of peptides and proteins, as well as the mechanism of action of protein kinases. Synbiotics has successfully synthesized large
The amount of phosphorylated peptides such as serine, threonine and tyrosine. For the sequence containing multiple hydroxyl-containing amino acids (S, T, Y), orthogonal protection or use of
Fmoc protected phosphorylated amino acid raw materials to achieve the selectivity of phosphorylated amino acids in the sequence.
5. Methylation modification
Protein methylation is considered to be an important modification that helps to regulate cell functions such as transcription, cell division and cell differentiation. Post-translational nitrogen-methylation usually occurs
Born on the side chain of lysine or arginine. Methylated protein-modified peptides can be used for protein-protein interaction studies or X-ray crystallographic structure determination. Union
Biology can synthesize polypeptides containing single, two, or three methylated lysines with a purity of >98%, and can also be combined with other methylation modifications.
6. KLH, BSA, OVA peptide coupling
The polypeptide antigen is too small to produce a significant immune response, so it is necessary to couple the polypeptide antigen to a larger protein carrier such as BSA, OVA, and KLH.
Since KLH has no inhibitory effect in ELISA or Western blotting detection, it does not affect the detection results. The commonly used coupling principle is the maleimide method,
That is, the cysteine residue in the polypeptide is coupled to the carrier protein. Therefore, when synthesizing antigenic polypeptides, adding a cysteine residue at the N-terminus or C-terminus is beneficial to the polypeptide and
Coupling of carrier protein.
Note: KLH is a very large condensed protein (MW = 4*105-1*107). Due to its special size and structure, its water solubility is limited, and samples often show up
Solution or suspension containing flocculent, but this does not affect the immunogenicity.
7. Polyethylene glycol (PEG) modification
PEG polymer is non-ionic, non-toxic, non-biologically repellent, highly hydrophilic, etc. The PEG modification chemically couples the PEG polymer to the macromolecule
On (antibodies, peptides, etc.). PEG-modified macromolecules have high solubility (mainly used for hydrophobic substances) and biological efficacy. They can deceive the host by disguising polypeptides.
The immune system of the main cell to enhance the therapeutic effect of peptides. It can also extend the metabolic time of peptides by reducing renal clearance.
8. Stable isotope labeling
In order to perform nuclear magnetic resonance experiments, Synbiotics labeled peptides with stable non-radioactive isotopes. Mark 2H, 15N, 13C or 15N and 13C at the same time mark many
Peptides can be easily detected by NMR after synthesis. If you need marking modification, please provide your sequence and marking requirements.
9. Modification of compound antigen peptide
Multiple-Antigen peptide (MAP) is an effective method for producing high-titer anti-peptide antibodies and peptide vaccines. Multiple antigen peptides
The a- or e-group of the amino acid forms the main chain, with multiple copies of the peptide antigen as the branched synthetic polypeptide on the outer surface. Depending on the number of lysines, different numbers of side chains can be synthesized
Multi-antigen peptides, so that high-titer, high-affinity antibodies can be produced without coupling the antigen to the carrier protein.
Message
Peptides are active substances that realize various functions in organisms. The modification of peptides is mainly the modification of the main chain structure and side chain groups of the peptide chain. Peptides can be changed by modification
The physicochemical properties of these compounds optimize their effective utilization in the body. Modified peptide drugs can significantly reduce immunogenicity, reduce toxic effects,
Increase water solubility, prolong the action time in the body, change the distribution in the body, and so on. Common peptide modifications include: C-terminal modification, N-terminal modification, intermediate residue modification,
And cyclization modification.
In addition to conventional linear peptides, Synthbio is now sufficient to meet your needs for a variety of cyclic peptides, modified peptides and special peptides, including: N/C terminal modification
Decoration, antigen peptide, fluorescent label, cyclic peptide, biotin label and PEGylation, etc. The peptide modification service provided by Synbiotics includes
But not limited to the following types:
☆N-terminal modification/C-terminal modification
☆Disulfide bond modification
☆A(yù)mide bond to form a ring
☆Fluorescent marking
☆Biotin labeled peptide
☆Carrier protein coupling and MAPs
☆Unnatural amino acid/D type amino acid
☆Phosphorylation and sulfonation modification
☆Linker, spacers PEGylation
☆Penetrating peptide
1. Amidation and acetylation
If the synthetic peptide is the internal sequence of the protein, the charge of the peptide can be removed by N-terminal acetylation or C-terminal amidation to make it more toward the natural structure of the protein.
Enhance the resistance of the polypeptide to endopeptidase.
2. Biotin and FITC labeling
For peptides labeled with biotin at the carboxyl end, lysine needs to be added to the carboxyl end, and then biotin is attached to the side chain of lysine, which eliminates lysine
The positive charge of the acid. FITC is a fluorescently labeled active precursor. In order to effectively label the N-terminus, a seven-carbon 6-aminocaproic acid can be inserted between the N-terminus of the polypeptide and the fluorescent group.
3. Disulfide bond modification
The formation of disulfide bonds between cysteine residues can realize polypeptide cyclization, but because disulfide bonds are formed randomly, for polypeptides containing multiple cysteine residues,
This is a challenge. Synbiotics can construct disulfide bonds between designated cysteines, and we can introduce three pairs of disulfide bonds in a polypeptide location.
4. Multiple phosphorylation
Peptide phosphorylation can help to study the effect of phosphorylation on the structure of peptides and proteins, as well as the mechanism of action of protein kinases. Synbiotics has successfully synthesized large
The amount of phosphorylated peptides such as serine, threonine and tyrosine. For the sequence containing multiple hydroxyl-containing amino acids (S, T, Y), orthogonal protection or use of
Fmoc protected phosphorylated amino acid raw materials to achieve the selectivity of phosphorylated amino acids in the sequence.
5. Methylation modification
Protein methylation is considered to be an important modification that helps to regulate cell functions such as transcription, cell division and cell differentiation. Post-translational nitrogen-methylation usually occurs
Born on the side chain of lysine or arginine. Methylated protein-modified peptides can be used for protein-protein interaction studies or X-ray crystallographic structure determination. Union
Biology can synthesize polypeptides containing single, two, or three methylated lysines with a purity of >98%, and can also be combined with other methylation modifications.
6. KLH, BSA, OVA peptide coupling
The polypeptide antigen is too small to produce a significant immune response, so it is necessary to couple the polypeptide antigen to a larger protein carrier such as BSA, OVA, and KLH.
Since KLH has no inhibitory effect in ELISA or Western blotting detection, it does not affect the detection results. The commonly used coupling principle is the maleimide method,
That is, the cysteine residue in the polypeptide is coupled to the carrier protein. Therefore, when synthesizing antigenic polypeptides, adding a cysteine residue at the N-terminus or C-terminus is beneficial to the polypeptide and
Coupling of carrier protein.
Note: KLH is a very large condensed protein (MW = 4*105-1*107). Due to its special size and structure, its water solubility is limited, and samples often show up
Solution or suspension containing flocculent, but this does not affect the immunogenicity.
7. Polyethylene glycol (PEG) modification
PEG polymer is non-ionic, non-toxic, non-biologically repellent, highly hydrophilic, etc. The PEG modification chemically couples the PEG polymer to the macromolecule
On (antibodies, peptides, etc.). PEG-modified macromolecules have high solubility (mainly used for hydrophobic substances) and biological efficacy. They can deceive the host by disguising polypeptides.
The immune system of the main cell to enhance the therapeutic effect of peptides. It can also extend the metabolic time of peptides by reducing renal clearance.
8. Stable isotope labeling
In order to perform nuclear magnetic resonance experiments, Synbiotics labeled peptides with stable non-radioactive isotopes. Mark 2H, 15N, 13C or 15N and 13C at the same time mark many
Peptides can be easily detected by NMR after synthesis. If you need marking modification, please provide your sequence and marking requirements.
9. Modification of compound antigen peptide
Multiple-Antigen peptide (MAP) is an effective method for producing high-titer anti-peptide antibodies and peptide vaccines. Multiple antigen peptides
The a- or e-group of the amino acid forms the main chain, with multiple copies of the peptide antigen as the branched synthetic polypeptide on the outer surface. Depending on the number of lysines, different numbers of side chains can be synthesized
Multi-antigen peptides, so that high-titer, high-affinity antibodies can be produced without coupling the antigen to the carrier protein.
| Warm tips: Suzhou Beike nano products are only used for scientific research, not for human body,different batches of products have different specifications and performance |
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| Warm tips: Suzhou Beike nano products are only used for scientific research, not for human body,different batches of products have different specifications and performance.The website pictures are from the Internet. The pictures are for reference only. Please take the real object as the standard. In case of infringement, please contact us to delete them immediately. |
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