A novel form of a drug to treat osteoporosis

A novel form of a drug used to treat osteoporosis that comes with the potential for fewer side effects may provide a new option for patients.

Osteoporosis is a bone disease that occurs when the body loses too much bone, makes too little bone, or both. As a result, bones become weak and may break from a fall or, in severe cases, from sneezing or minor bumps.

The disease makes bones so porous. Now, Purdue University innovators developed a novel form of a drug used to treat osteoporosis. They have developed a stabilized form of human calcitonin, a peptide drug already used for people with osteoporosis.

Scientists created a prodrug form of the peptide hormone to increase its effectiveness as an osteoporosis treatment.

In humans, calcitonin is the hormone liable for normal calcium homeostasis. When recommended to osteoporosis patients, calcitonin inhibits bone resorption, resulting in increased bone mass.

Tragically, human calcitonin goes through fibrillation in an aqueous solution, prompting decreased viability when utilized as a therapeutic. As a substitute, osteoporosis patients have been prescribed salmon calcitonin. It doesn’t fibrillate as quickly; however, it experiences low intensity and the potential for a few unfriendly results.

Elizabeth Topp, a Purdue professor of physical and industrial pharmacy, said, “The technology can help make these calcitonin drugs safer and more effective. Our approach will increase the therapeutic potential of human calcitonin, promising a more effective option to replace salmon calcitonin for osteoporosis and related disorders.”

Purdue researchers phosphorylated specific amino acid residues to decrease the fibrillation propensity and increase the therapeutic benefit of human calcitonin.

Topp said, “Many promising new peptide drugs tend to form fibrils. This technology provides a way to stabilize them reversibly so that the stabilizing modification comes off when the drug is given to the patient.”

Journal Reference:
  1. Harshil K. Renawala et al. Fibrillation of Human Calcitonin and Its Analogs: Effects of Phosphorylation and Disulfide Reduction. DOI: 10.1016/j.bpj.2020.11.009

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