FTPP incorporates a CKGGRAKDC peptide sequence that binds selectively to prohibitin, a protein expressed on the luminal surface of vascular endothelial cells supplying white adipose tissue at higher density than in many other vascular beds. This homing domain directs the conjugated proapoptotic payload specifically to prohibitin-expressing endothelium, providing a model system for studying tissue-selective vascular targeting strategies based on differential surface receptor expression rather than systemic drug distribution.

The (KLAKLAK)2 domain is a synthetic cationic amphipathic peptide that, upon cellular internalisation following prohibitin-mediated binding, disrupts mitochondrial membrane integrity, triggering the intrinsic apoptotic pathway in the targeted endothelial cell. Because this proapoptotic domain only reaches functionally relevant intracellular concentrations following prohibitin-dependent uptake, the overall mechanism is studied as a model for spatially restricted apoptosis induction, with cell death confined largely to cells expressing the target receptor at sufficient density.

Competitive binding assays using free prohibitin-binding peptide (without the proapoptotic payload) to block FTPP uptake, alongside biodistribution studies tracking labeled FTPP localisation across different vascular beds, are standard methods for confirming the homing domain's binding specificity. Comparative studies using a scrambled or non-binding control peptide sequence conjugated to the same proapoptotic domain are also used to confirm that observed effects depend on the specific prohibitin-targeting sequence rather than nonspecific peptide uptake or toxicity.