Peptide–affinity tag conjugates are non-drug peptide conjugates in which a peptide is covalently linked to a small-molecule tag
that enables selective capture, enrichment, immobilization, or detection in research workflows.
These constructs are widely used in pull-down assays, interaction studies, surface immobilization, and assay development where reproducible binding and low background are important.
[1], [2]
Bio-Synthesis builds chemically defined peptide–affinity tag conjugates using site-defined attachment (N-/C-terminus, single-Cys, or handle-enabled options; project-dependent), with purification and fit-for-purpose analytical confirmation to support research-stage and preclinical programs.
The most common platform is biotinylation (biotin–streptavidin/avidin systems), but alternative tags—such as desthiobiotin (reversible capture),
digoxigenin (DIG) (antibody-based detection), or hapten tags like DNP—may be selected based on assay format and downstream handling needs.
[1], [3]
Successful affinity tagging typically depends on site-defined attachment (e.g., N-terminus, C-terminus, a single engineered Cys, or a dedicated handle; project-dependent)
and appropriate spacer design (e.g., PEG spacers) to reduce steric interference and preserve peptide binding/structure.
[4]
peptide affinity tag conjugation
biotinylated peptides
desthiobiotin (reversible capture)
DIG / hapten tags
site-defined attachment
ISO 9001:2015 / ISO 13485:2016
Figure: Representative peptide + linker/PEG spacer + affinity tag architecture (biotin shown as an example).
Related: Non-drug peptide–ligand conjugates ·
Peptide–fluorophore conjugates