SPPS is the peptide synthesize based on the solid support which is also known as resin, linkers are modified on the resin to provide the reactive group for the first amino acid. Peptide is synthesized through the amide bond between the amide group and carboxyl group from another in the condition of pre-activated species or in situ activation. To avoid the undesired reactions, protecting groups are involved to temporary mask reactive groups on both N α-position and side chain of the amino acid. Fmoc is one of commonly used N α-position protecting group, which advantages are quiet obvious. For instance, the deprotection condition with 20–50% piperidine in DMF is truly mild; and the protection scheme with the side chain of different amino acid is orthogonal. Moreover the progress of each deprotection reaction can be followed by real time spectrophotometric monitoring the release of the cleaved Fmoc-group at 300-320 nm. After the desired peptide is synthesized, the resin bound peptide is deprotected and detached from the solid support via TFA cleavage since Fmoc-strategy uses acid liable linkers.
Articles in this section
- Why it is difficult to synthesize peptide with FITC without the Ahx linker?
- I also noticed that one of the peptides was pinkish and others yellow.Could you please let me know the reasons?
- What’s the condition you suggest to store the peptide powder and the solution? Also, how long can they be store at room temperature?
- How to read my peptide QC report? Especially the HPLC and MS report?
- I would like to know what quality control measure you employ i.e., how do I determine that the product you sent me is what I wanted?
- How many continuous "R" can we synthesize in a peptide?
- Do you provide peptoid service?
- Can you cyclize my peptide by disulphide bond (cysteine bridge) while my peptide sequence contains 3 cysteines?
- What is your recommended peptide purity for in vivo application?
- For the peptide synthesis, can you send me the synthesis protocol that was used including the procedure that was used for making the disulfide bonds?