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Saporin is a Type I ribosome-inactivating protein (RIP) derived from the seeds of the soapwort plant (*Saponaria officinalis*). As an RNA N-glycosidase, saporin specifically and irreversibly removes a single adenine residue from the highly conserved sarcin/ricin loop of the 28S ribosomal RNA. This modification prevents the binding of elongation factors, effectively halting protein synthesis and triggering cell death via apoptosis. Unlike Type II RIPs such as ricin, saporin lacks a cell-binding B-chain, rendering it unable to enter cells independently and making it relatively non-toxic to cells lacking a specific internalizing mechanism. This property has led to its widespread use as a cytotoxic payload in the development of immunotoxins and antibody-drug conjugates (ADCs), where it is chemically linked or genetically fused to targeting moieties like monoclonal antibodies or peptides to selectively eliminate specific cell populations in oncology and neuroscience research.
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