This record provides bibliographic details and links to the original research. An editorial study breakdown is not available.
What the researchers found
Rigidifying the macrocycle improved alpha helicity, target affinity, and proteolytic stability.
Why it matters
Enhancing the delivery and stability of peptides could lead to more effective cancer therapies. This research provides insights into designing better therapeutic peptides.
How the study worked
The study systematically compared various cyclization constraints and linker positions to assess their effects on peptide properties.
What this study cannot tell us
The study primarily focuses on in vitro conditions, which may not fully replicate in vivo environments.
Read the original research
Landscaping macrocyclic peptides: stapling hDM2-binding peptides for helicity, protein affinity, proteolytic stability and cell uptake.
RSC chemical biology, 3(7), 895-904
Citation
de Araujo, Aline D; Lim, Junxian; Wu, Kai-Chen; Hoang, Huy N; Nguyen, Huy T; Fairlie, David P. (2022). Landscaping macrocyclic peptides: stapling hDM2-binding peptides for helicity, protein affinity, proteolytic stability and cell uptake.. RSC chemical biology, 3(7), 895-904. https://doi.org/10.1039/d1cb00231g