Irreversible denaturation of proteins through aluminum-induced formation of backbone ring structures.
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.
Shanghai Institute of Applied Physics, Chinese Academy of Sciences, P. O. Box 800-204, Shanghai 201800 (China). bosong@sinap.ac.cn.
Bo
B
Song
Qian
Q
Sun
Haikuo
H
Li
Baosheng
B
Ge
Ji Sheng
JS
Pan
Andrew Thye Shen
AT
Wee
Yong
Y
Zhang
Shaohua
S
Huang
Ruhong
R
Zhou
Xingyu
X
Gao
Fang
F
Huang
Haiping
H
Fang
D000535:Aluminum / Q000737:chemistry*; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory
D011506:Proteins; D000535:Aluminum
aluminum; aluminum-related diseases; peptides; protein denaturation