Drug Targets & Biological Macromolecules

protease

A protease is an enzyme that works like molecular scissors, cutting other proteins by snipping the bonds that hold their building blocks together. Proteins are chains of amino acids linked by peptide bonds, and a protease severs one of these bonds at a precise spot. This controlled cutting lets the body activate, recycle, or shut down proteins on demand.

Each protease recognizes a particular sequence or shape around the bond it cuts, then uses its active site to break that peptide bond, usually with the help of water or a reactive amino acid. Some proteases trim a protein to switch it on, others dismantle proteins for recycling, and still others are hijacked by viruses to assemble their own machinery. This variety makes proteases targets across many diseases.

Because viruses and parasites often depend on their own proteases to mature, blocking those enzymes can stop an infection in its tracks. Protease inhibitors must fit the cutting pocket tightly enough to outcompete the natural substrate. The caveat is that human proteases resemble pathogen ones, so achieving selectivity, and avoiding interference with normal physiology, is a central design challenge.

HIV protease inhibitors block the viral enzyme that cuts long protein precursors into the pieces a new virus needs, leaving the virus unable to mature.

Stopping the viral scissors prevents assembly of infectious virus.

Proteases are grouped by the chemistry they use to cut, such as serine, cysteine, aspartic, and metalloproteases, which guides how inhibitors are designed.

Also called
peptidase肽酶肽酶