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Peptide Modification


1. Amidation and Acetylation

If the peptide is from an internal sequence of a protein, terminal amidation (C-terminus) or acetylation (N-terminus) will remove its charge and help it imitate its natural structure (amide, CONH2). In addition, this modification makes the resulting peptide more stable towards enzymatic degradation resulting from exopeptidases.

2.Disulfide Bridge

Peptide cyclization can be achieved through creating disulfide bridges between cysteine residues on the peptide. This is a challenging practice for peptide containing multiple cysteine residues due to random formations of disulfide bridges between them.we have been able to provide customers up to four disulfide bridges in one peptide .                             


Phosphopeptides can assist in the investigation of the influences of phosphorylation on peptides and protein structure and in the understanding of regulatory processes mediated by protein kinases.  We has successfully synthesized numerous serine-, threonine-, and tyrosine-phosphopeptides. For peptides containing one or more of these hydroxy-amino acids, selective phosphorylation can be achieved by orthogonal protection or by Fmoc-protected phosphorylated amino acids. 

4.Biotin and FITC

For C-terminal labeling of biotin, a Lys residue is added to the C-terminus of the peptide. Biotin is then attached to the lysine side chain via amide bond. The positive charge of the lysine is then removed.

Fluorescein isothiocyanate (FITC) is an activated precursor used for fluorescein labeling. For efficient N-terminal labeling, a seven-atom aminohexanoyl spacer (NH2-CH2-CH2-CH2-CH2-CH2-COOH) is inserted between the fluorophore (fluoroscein) and the N-terminus of the peptide.

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