Advantages And Disadvantages Of Synthetic Peptides

Advantages And Disadvantages Of Synthetic Peptides

It’s good that synthetic peptides have both positive and negative aspects.

PROS

  • For a low-cost option, you may try synthetic peptides. Chemical syntheses should be used for 20 to 50 amino acids short peptides. Vendors are always accessible to assist you promptly. The time savings alone make it worthwhile compared to biologically cloning and expressing the gene. You may buy peptides online if you are a licensed professional.
  • Some post-translational modifications, such as the phosphorylation of Tyr or Ser, are conceivably feasible.
  • When producing peptides with such great purity and precision, there is no need to worry about the intricacy of the biological matrix.
  • An affinity tag is not required for purification since it might interfere with the peptide’s original function.

CONS

  • Proteins can only be made up to a particular size (between 20 and 50 amino acids).
  • Post-translational modifications, like glycosylation that is difficult to synthesize for biological function, might be problematic.
  • Disulfide bonds are challenging to create.
  • Using this method, a secondary or tertiary structure or the creation of large bioactive proteins may not be possible. The protein.

The many uses of Synthetic peptides

Antibody manufacturing may be tailored to meet specific needs.

Using synthetic peptides as antigens, custom antibodies may be created. When the peptide is linked to a carrier protein, it may activate a host humoral immune response and generate monoclonal and polyclonal antibodies. Instead of using the entire initial protein, this approach dramatically simplifies manipulating the epitope. However, the amino acid structure of the antigen is essential. The pattern most likely to elicit an immune response may be found using free internet tools.

Western blot analysis may benefit from peptide-based antibodies. One possibility is to employ a peptide containing phosphorylated amino acids to create an antibody that exclusively detects phosphorylated proteins. This antibody and a peptide containing the non-phosphorylated residues may be used to stain a Western blot for phosphorylated and non-phosphorylated proteins. This method is often used in cell signaling research to study the relationships between kinases and phosphatases. Even the P-32 cleaning will be taken care of for you!

Proteins interact with one another.

It is possible to learn about protein-protein interactions by studying peptides. Beads coated with streptavidin may be used to draw down proteins that bind to the biotinylated polypeptide. In epigenetics research, it is common practice to use peptides matching the histone tails with and sans post-translational modifications. SDS-PAGE may be utilized to look at any proteins linked to a particular molecule.

They can also help with NMR and fluorescence anisotropy due to their small size. The last application for peptides is as substrates for enzyme activities. According to a recent study, peptide libraries and purified enzymes may be used to locate direct substrates for the enzymes. It would have been challenging, if not impossible, to use biological systems to study connections between native and recombinant proteins.

Mass spectrometry

Using synthesized peptides as standards in mass spectrometry might be advantageous. There are numerous aspects to consider to quantify the peptides generated following digestion using mass spectrometry precisely.

You may, for example, use this method to determine the quantity of an isotopically labeled peptide in the protein that has undergone a specific post-translational alteration. An internal standard may now be used to measure native peptide quantities.

Because they produce the same MS/MS spectrum characteristics as native peptides but are compensated by the variance in molecular weight, synthetically tagged peptides may be helpful when searching for peaks in an MS/MS spectrum.

naveenboda1993

Leave a Reply

Your email address will not be published.