Peptide Drugs Braced for Rigors of Oral Route
May 21, 2020 | Biotechnology
Reading time: 3 minutes
Fresh from Genetic Engineering and Biotechnology News (GEN), here is a new Biotech article for you:
As far as our digestive system is concerned, peptides are foodstuffs to be broken down, not therapeutics to be kept intact until they enter the bloodstream. Peptide drugs, then, must run a gauntlet of countless degradative enzymes. Few have what it takes to stand the punishment. To give peptide drugs a sturdier backbone, researchers at the Ecole Polytechnique Fédérale de Lausanne (EPFL) have been developing double-bridged peptides, that is, peptides that are cyclized by two chemical bridges.
More rigid and stable than linear peptides, the double-bridged peptides better resist digestive enzymes. Still, the cyclized structures haven’t been rolling toward pill form. The ones that have been evaluated thus far have given into enzymatic pressure. Undeterred, the EPFL researchers decided to explore the double-bridged peptide space more widely—so widely, in fact, that the researchers realized that they needed a new search method.
Led by Christian Heinis, the EPFL team developed a phage display method to screen large libraries of genetically encoded double-bridged peptides. The method, which identifies among billions of double-bridged peptides those that bind a disease target of interest and survive enzymes of the gastrointestinal tract, was described in a paper (“De novo development of proteolytically resistant therapeutic peptides for oral administration”) that appeared May 11 in the journal Nature Biomedical Engineering.... Read more at the GEN Blog.
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