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Front Cover: Targeting an Interaction Between Two Disordered Domains by Using a Designed Peptide (Chem. Eur. J. 45/2020)
Author(s) -
Mayer Guy,
Shpilt Zohar,
Bressler Shachar,
Marcu Orly,
SchuelerFurman Ora,
Tshuva Edit Y.,
Friedler Assaf
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202002213
Subject(s) - peptide , linker , folding (dsp implementation) , chemistry , biophysics , domain (mathematical analysis) , loop (graph theory) , crystallography , biology , biochemistry , computer science , mathematics , engineering , mathematical analysis , combinatorics , electrical engineering , operating system
p53 linkTer is a designed peptide , derived from combining the disordered termini of the p53 linker domain while omitting the connecting loop. The peptide bound the disordered RT loop in iASPP with the same affinity as the parent peptide, without pre‐folding to a defined conformation, and inhibited the interaction between the disordered domains of iASPP and p53, as well as cancer cell death. Omitting the secondary structure from the parent peptide changed its coupled folding and binding mechanism to just binding, suggesting that disorder may be advantageous for interactions. More information can be found in the Full Paper by A. Friedler et al. on page 10240.