Abstract
Self-assembled peptide nanostructures with actively folded secondary structures have potential to mimic the function of proteins. We here show that α-helix-stabilized self-assembled peptide nanostructures (αSSPNs), whose sizes are comparable to those of proteins, have potential to be developed as protein-protein interaction (PPI) inhibitors along with several unprecedented properties. Using p53-MDM2 PPI as a model system, the molecular recognition and modulation of PPIs by αSSPN grafted with a p53 α-helix (p53 αSSPN) were investigated. The competition assay showed that the p53 αSSPN can inhibit the p53-MDM2 interaction. Interestingly, the p53 αSSPN was far more resistant to degradation by the protease chymotrypsin than the monomeric p53 peptide and had high thermal stability. These results suggest that the αSSPN scaffold holds great potential to be developed as a novel class of PPI inhibitors.
| Original language | English |
|---|---|
| Pages (from-to) | 2684-2689 |
| Number of pages | 6 |
| Journal | Biomacromolecules |
| Volume | 14 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 2013 Aug 12 |
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All Science Journal Classification (ASJC) codes
- Bioengineering
- Biomaterials
- Polymers and Plastics
- Materials Chemistry
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Helix stabilized, thermostable, and protease-resistant self-assembled peptide nanostructures as potential inhibitors of protein-protein interactions. / Jeong, Woo Jin; Lee, Myeong Sup; Lim, Yong-beom.
In: Biomacromolecules, Vol. 14, No. 8, 12.08.2013, p. 2684-2689.Research output: Contribution to journal › Article
TY - JOUR
T1 - Helix stabilized, thermostable, and protease-resistant self-assembled peptide nanostructures as potential inhibitors of protein-protein interactions
AU - Jeong, Woo Jin
AU - Lee, Myeong Sup
AU - Lim, Yong-beom
PY - 2013/8/12
Y1 - 2013/8/12
N2 - Self-assembled peptide nanostructures with actively folded secondary structures have potential to mimic the function of proteins. We here show that α-helix-stabilized self-assembled peptide nanostructures (αSSPNs), whose sizes are comparable to those of proteins, have potential to be developed as protein-protein interaction (PPI) inhibitors along with several unprecedented properties. Using p53-MDM2 PPI as a model system, the molecular recognition and modulation of PPIs by αSSPN grafted with a p53 α-helix (p53 αSSPN) were investigated. The competition assay showed that the p53 αSSPN can inhibit the p53-MDM2 interaction. Interestingly, the p53 αSSPN was far more resistant to degradation by the protease chymotrypsin than the monomeric p53 peptide and had high thermal stability. These results suggest that the αSSPN scaffold holds great potential to be developed as a novel class of PPI inhibitors.
AB - Self-assembled peptide nanostructures with actively folded secondary structures have potential to mimic the function of proteins. We here show that α-helix-stabilized self-assembled peptide nanostructures (αSSPNs), whose sizes are comparable to those of proteins, have potential to be developed as protein-protein interaction (PPI) inhibitors along with several unprecedented properties. Using p53-MDM2 PPI as a model system, the molecular recognition and modulation of PPIs by αSSPN grafted with a p53 α-helix (p53 αSSPN) were investigated. The competition assay showed that the p53 αSSPN can inhibit the p53-MDM2 interaction. Interestingly, the p53 αSSPN was far more resistant to degradation by the protease chymotrypsin than the monomeric p53 peptide and had high thermal stability. These results suggest that the αSSPN scaffold holds great potential to be developed as a novel class of PPI inhibitors.
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U2 - 10.1021/bm400532y
DO - 10.1021/bm400532y
M3 - Article
VL - 14
SP - 2684
EP - 2689
JO - Biomacromolecules
JF - Biomacromolecules
SN - 1525-7797
IS - 8
ER -