Abstract

The enzymatically labile peptidcs LHRH and TRH were conjugated to various lipidic peptides. The conjugates and free peptides were incubated with Caco-2 cell homogenates and their respective degradation profiles were studied following incubation. Conjugation to lipidic peptides increased the half-life of LHRH and TRH. The Caco-2 cell homogenates were capable of cleaving the conjugated lipidic peptide, to release the parent LHRH or TRH. The released LHRH or TRH subsequently demonstrated a longer half-life than when present alone in the incubation mixture, suggesting that the cleaved lipidic peptide is capable of inhibiting enzymes.

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