Evaluation of the Biological Properties and the Enzymatic Stability of Glycosylated Luteinizing Hormone-Releasing Hormone Analogs.

Glycosylation of LHRH analogs significantly increased their enzymatic stability, with compounds 1 and 6 showing half-lives extended from 3 minutes to up to 103 minutes in kidney membrane enzymes. These glycopeptides also demonstrated significant antiproliferative effects on LHRH receptor-positive prostate cancer cells and stimulated hormone release in rat pituitary cells.

The study involved chemically attaching carbohydrate units (lactose, glucose, galactose) to LHRH peptides and testing their stability against enzymatic degradation in human plasma, rat kidney membranes, and liver homogenates. The antiproliferative activity was assessed on prostate cancer cells, and hormone release was measured in dispersed rat pituitary cells.

Improving the stability of LHRH peptides can enhance their therapeutic potential by prolonging their activity in the body and increasing their effectiveness against hormone-sensitive cancers and hormone regulation.

The study was conducted primarily in vitro and in rat cells, so further in vivo and clinical studies are needed to confirm therapeutic benefits and safety in humans.