Overview
mRNA Display Linkers for Peptide–mRNA Fusion Workflows
Puromycin is an aminonucleoside antibiotic that structurally mimics aminoacyl-transfer RNA (tRNA). During protein synthesis, puromycin can enter the ribosomal A-site, form a peptide bond with the growing peptide chain and terminate further elongation.
This unique peptide-acceptor behavior is what makes puromycin valuable for mRNA display. When puromycin is attached to an RNA, DNA, hybrid or branched/bDNA oligonucleotide linker, the puromycin moiety can capture the nascent peptide emerging from the ribosome.
The resulting peptide–mRNA fusion physically connects the translated peptide with the encoding nucleic acid sequence. This genotype–phenotype linkage enables in vitro selection, peptide discovery, binder screening, protein engineering and directed evolution workflows.
Bio-Synthesis supports custom puromycin linker designs across RNA, DNA, DNA/RNA hybrid and branched/bDNA oligonucleotide architectures, including PEG-spacer linkers, affinity-tagged linkers, fluorescent linker constructs and application-specific mRNA display oligo formats.
How Puromycin Creates Peptide–mRNA Fusion Molecules
mRNA → ribosome → puromycin linker → peptide–mRNA fusion
mRNA
Template Translation
The mRNA library is translated in vitro to produce nascent peptide products.
Link
Puromycin Linker
A puromycin-bearing linker positions the acceptor near the ribosome.
Pep
Peptide Transfer
Puromycin accepts the nascent peptide chain from the ribosome.
Fuse
Selection-Ready Fusion
The peptide remains linked to the encoding mRNA for library selection.