N-terminal Modifications


JPT is able to incorporate a wide range of N-terminal modifications into peptides. Examples of modifications routinely synthesized at JPT are shown below.

N-terminal acetylation removes the charge from the amino terminus of a peptide. In general, acetyl modification is recommended if a peptide is meant to imitate its natural structure in a protein. In addition, this modification stabilizes the resulting peptide towards enzymatic degradation resulting from exopeptidases.

Besides acylations, other N-terminal modifications are available (e.g. urea, carbamate, sulfonamide, alkylamine).

If tolerated by the peptides’ pharmacodynamics, radioligands are often attached to the N‑terminus of peptides. Examples include the attachment of DOTA, NOTA, NODAGA, etc..

Standard Acylations


N terminal modifications acylations
N terminal modifications acylations
N terminal modifications acylations
Non-Amide Modifications

N terminal modifications non amide
N terminal modifications non amide
N terminal modifications non amide
Radioligands

N terminal modifications radioligands
N terminal modifications radioligands
N terminal modifications radioligands
Dyes and Quenchers

n terminal modifications dyes quenchers
n terminal modifications dyes quenchers
n terminal modifications dyes quenchers
Select for an extended list of dyes and quenchers.

Affinity and Reactive Labeling
Please visit our Biotinylation and Tagged Peptides site for a list of affinity and reactive labeling options.