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Irreversible Denaturation of Proteins through Aluminum‐Induced Formation of Backbone Ring Structures
Author(s) -
Song Bo,
Sun Qian,
Li Haikuo,
Ge Baosheng,
Pan Ji Sheng,
Wee Andrew Thye Shen,
Zhang Yong,
Huang Shaohua,
Zhou Ruhong,
Gao Xingyu,
Huang Fang,
Fang Haiping
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201307955
Subject(s) - chemistry , ring (chemistry) , amide , circular dichroism , denaturation (fissile materials) , crystallography , peptide , peptide bond , ab initio , x ray photoelectron spectroscopy , ion , nuclear magnetic resonance , organic chemistry , biochemistry , nuclear chemistry , physics
A combination of ab initio calculations, circular dichroism, nuclear magnetic resonance, and X‐ray photoelectron spectroscopy has shown that aluminum ions can induce the formation of backbone ring structures in a wide range of peptides, including neurodegenerative disease related motifs. These ring structures greatly destabilize the protein and result in irreversible denaturation. This behavior benefits from the ability of aluminum ions to form chemical bonds simultaneously with the amide nitrogen and carbonyl oxygen atoms on the peptide backbone.