Syd Biotechnologies specialises in the development and screening of mRNA display libraries. These libraries, comprising a diverse array of peptide sequences, cDNAs, and antibodies, are engineered with essential features including T7 RNA polymerase promoter sites, ribosome binding sequences, actinomycin/puromycin binding regions, and RNA stability elements. 

The workflow begins with in vitro transcription, during which mRNA is synthesised and covalently linked to puromycin. This linkage facilitates the stable association between the mRNA and the corresponding translated protein. Translation is performed in vitro using E. coli or eukaryotic cell lysates, in the presence of tRNA, buffers, and elevated concentrations of Mg²⁺. 

Following translation, the resulting polypeptide–mRNA–puromycin complexes are purified and exposed to the target molecule. Through multiple rounds of enrichment, target–peptide–mRNA–ribosome quaternary complexes are selectively isolated. RNA from these complexes is then extracted, reverse transcribed, and cloned into a vector for sequencing. The amino acid sequences of the binding ligands are subsequently identified through translation. 

Utilising this ribosome display platform, Syd Biotechnologies is capable of screening ultra-diverse libraries—reaching up to 10¹⁴ to 10¹⁵ variants—greatly enhancing the probability of discovering high-affinity binders for a wide variety of biological targets.

Service Highlights 

  We generate and screen highly diverse libraries with complexities exceeding 10¹⁴–10¹⁵ variants. 

  Antibody libraries derived from immunised animals are constructed and screened for target-specific binders. 

  Peptide libraries of varying lengths—including mini-proteins and small peptides—are developed and evaluated. 

  We offer cDNA library preparation tailored for mRNA display platforms. 

  Custom libraries incorporating non-standard amino acids and cyclised peptides are also available. 

  Selected clones are validated using techniques such as FACS, ELISA, and Biacore for binding specificity and affinity.