3 ways to effectively increase the solubility of poorly soluble peptides
2024-01-14 11:09:17
Polypeptides are widely used in medicine, materials, dyes and other fields. The solubility of peptides is also an important factor in the success of laboratory experiments.
In general, the solubility of a polypeptide is usually closely related to the amino acid sequence of the entire peptide chain. Usually, when an overall acidic polypeptide is difficult to dissolve, an appropriate amount of an alkaline solution may be added, and when the alkaline polypeptide is difficult to dissolve, an appropriate amount may be added. Acidic solution, when the sequence contains a large number of hydrophobic amino acids or neutral amino acids, it is difficult to dissolve directly in water. Usually, a small amount of organic solvent is added first. After dissolution, it is diluted with distilled water. Commonly used organic solvents are acetonitrile, DMSO, DMF, C. Alcohol, isopropanol, etc. It should be noted that when the peptide chain contains Met or Cys, it cannot be dissolved in DMSO, which is likely to cause the S contained in the peptide chain to be oxidized. In addition, in order to help customers design peptides to achieve good experimental results, we usually give some effective advice to customers on the physical properties, chemical properties and molecular structure of peptide chains.
For customer orders, we usually give the following suggestions to increase the solubility of poorly soluble peptides:
1. Modification of the C-terminus and N-terminus of the peptide chain: For acidic peptides, we recommend C-terminal acetylation modification. For basic peptides, we recommend N-terminal amination modification.
2. Modifying the amino acid sequence in the peptide chain: some sequences have a large number of consecutive hydrophobic amino acids, such as W, F, V, I, L, M, Y. When these hydrophobic amino acids are repeated in large or consecutive sequence, The entire peptide chain is usually poorly soluble. In order to enhance the polarity and hydrophilicity of the peptide, we also recommend that the client extend the sequence without affecting the experimental results, or increase the number of hydrophobic amino acids to reduce the solubility. Sex.
3. Replacing the residue of the hydrophobic amino acid in the sequence: the effect of increasing the solubility can be achieved by substituting the soluble amino acid for the hydrophobic amino acid in the sequence. We usually use Gly, Ala to replace hydrophobic amino acids, generally get better dissolution, which is a conservative but effective way to enhance the solubility of the peptide.
The professional technical team, excellent equipment and sophisticated synthetic purification process make our national peptide organisms fully equipped with the conditions and capabilities to provide various insoluble peptides. Reducing the customer's experimental cycle, improving the customer's experimental efficiency, and helping customers' scientific research projects achieve better results is always the purpose and goal of our company's services.
success case:
Insoluble sequence Biotin-GGGGGGGG
HPLC analysis:
MS analysis:
In general, the solubility of a polypeptide is usually closely related to the amino acid sequence of the entire peptide chain. Usually, when an overall acidic polypeptide is difficult to dissolve, an appropriate amount of an alkaline solution may be added, and when the alkaline polypeptide is difficult to dissolve, an appropriate amount may be added. Acidic solution, when the sequence contains a large number of hydrophobic amino acids or neutral amino acids, it is difficult to dissolve directly in water. Usually, a small amount of organic solvent is added first. After dissolution, it is diluted with distilled water. Commonly used organic solvents are acetonitrile, DMSO, DMF, C. Alcohol, isopropanol, etc. It should be noted that when the peptide chain contains Met or Cys, it cannot be dissolved in DMSO, which is likely to cause the S contained in the peptide chain to be oxidized. In addition, in order to help customers design peptides to achieve good experimental results, we usually give some effective advice to customers on the physical properties, chemical properties and molecular structure of peptide chains.
For customer orders, we usually give the following suggestions to increase the solubility of poorly soluble peptides:
1. Modification of the C-terminus and N-terminus of the peptide chain: For acidic peptides, we recommend C-terminal acetylation modification. For basic peptides, we recommend N-terminal amination modification.
2. Modifying the amino acid sequence in the peptide chain: some sequences have a large number of consecutive hydrophobic amino acids, such as W, F, V, I, L, M, Y. When these hydrophobic amino acids are repeated in large or consecutive sequence, The entire peptide chain is usually poorly soluble. In order to enhance the polarity and hydrophilicity of the peptide, we also recommend that the client extend the sequence without affecting the experimental results, or increase the number of hydrophobic amino acids to reduce the solubility. Sex.
3. Replacing the residue of the hydrophobic amino acid in the sequence: the effect of increasing the solubility can be achieved by substituting the soluble amino acid for the hydrophobic amino acid in the sequence. We usually use Gly, Ala to replace hydrophobic amino acids, generally get better dissolution, which is a conservative but effective way to enhance the solubility of the peptide.
The professional technical team, excellent equipment and sophisticated synthetic purification process make our national peptide organisms fully equipped with the conditions and capabilities to provide various insoluble peptides. Reducing the customer's experimental cycle, improving the customer's experimental efficiency, and helping customers' scientific research projects achieve better results is always the purpose and goal of our company's services.
success case:
Insoluble sequence Biotin-GGGGGGGG
HPLC analysis:
MS analysis:
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