peptidetransfer

Peptidetransfer is a biochemical process in which a peptide moiety is moved from a donor molecule to an acceptor, resulting in the formation of a new covalent linkage or modification of the acceptor. The term can describe natural enzymatic reactions as well as engineered or chemical ligation steps used in research and biotechnology.

In biology, the most prominent example is the peptidyl transferase reaction that occurs during protein synthesis in the ribosome. Here, the growing peptide on a peptidyl-tRNA in the P site is transferred to the aminoacyl-tRNA in the A site, forming a new peptide bond and extending the polypeptide chain. This reaction is catalyzed by the ribosome’s peptidyl transferase center, which is largely formed by ribosomal RNA and assisted by ribosomal proteins. The efficiency and fidelity of this transfer underlie accurate translation of the genetic code.

Peptidetransfer also features in other biological contexts. Enzymes such as sortases catalyze transpeptidation to covalently join peptides or proteins at specific motifs, a reaction exploited in protein engineering and biotechnology. In bacterial cell wall synthesis, transpeptidases cross-link peptide side chains, strengthening the peptidoglycan matrix through peptide transfer reactions. Additionally, certain chemical or enzymatic ligation methods in the laboratory mimic transpeptidation to assemble proteins, peptides, or peptide–drug conjugates.

Understanding peptidetransfer is important for biochemistry, medicine, and biotechnology, influencing areas from fundamental biology and antibiotic action to protein engineering and synthetic biology.