Gp41-1 split intein (Gp41-1)

The Gp41-1 split intein is a highly efficient protein splicing element derived from a cyanophage, consisting of N-terminal (IntN) and C-terminal (IntC) fragments. These fragments possess a high affinity for one another and, upon association, catalyze a self-excision process known as protein trans-splicing, which covalently links two flanking protein sequences (exteins) with a native peptide bond (PMID: 23933386, PMID: 21534051). In biotechnology and medicine, Gp41-1 is primarily utilized as a tool for protein engineering and gene therapy rather than serving as a traditional therapeutic target. It is frequently employed to circumvent the packaging limits of viral vectors, such as Adeno-associated virus (AAV), by splitting large therapeutic proteins into two halves that reconstitute functionally within the target cell (PMID: 31586043). While it is not a target for small molecule drugs, its kinetics and specificity make it a cornerstone of synthetic biology for the conditional activation of enzymes, transcription factors, and chimeric antigen receptors (CARs).

Other names

Gp41-1 N-inteinGp41-1 C-inteinGp41-1 protein splicing elementN-terminal intein fragmentC-terminal intein fragment

The Gp41-1 split intein fragments (IntN and IntC) undergo rapid and spontaneous association to form a functional catalytic domain that facilitates protein trans-splicing, resulting in the excision of the intein and the ligation of flanking extein sequences via a peptide bond (PMID: 23933386).