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Design and synthesis of BRC analogous peptides and their interactions with a key p53 peptide
Author(s) -
Zhao Dongxin,
Lu Kui,
Liu Guangbin,
Ma Li,
Zhu Hanjing,
He Juan
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13256
Subject(s) - mutant , peptide , chemistry , mutation , circular dichroism , gene , biochemistry , biology , stereochemistry
Mutations in breast cancer susceptibility gene 2 ( BRCA2 ) can lead to chromosomal instability and result in breast cancer, which is strongly associated with p53 mutations. Here, based on the crystal structure of BRC 4 and p53, the spatial structure of BRC 2 and p53 (171–192) was simulated, providing structural basis for the site‐specific mutation of BRC 2. The BRC analogous peptides and p53 (171–192) were synthesized, and the interaction between the mutant peptide and p53 (171–192) was studied using circular diachronic spectroscopy and fluorescence spectroscopy. The results show that the mutations of amino acid residues constituting the BRC 2 α‐helix significantly affect the structure and interaction of BRC analogs and p53 (171–192), which provides support for understanding the structure of the BRC repeat motifs and its interaction pattern with p53.