The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28).
Metal ions play a critical role in human islet amyloid polypeptide (hIAPP) aggregation, which is believed to be closely associated with β-cell death in type II diabetes. In this work, the effect of Al3+ on the aggregation of hIAPP (11-28) was studied by several different experimental approaches. Atomic force microscopy measurements showed that Al3+ could remarkably inhibit hIAPP(11-28) fibrillogenesis, while Zn2+ had a slight promotion effect on peptide aggregation, which was also confirmed by Thioflavin T fluorescence observation. Furthermore, X-ray photoelectron spectroscopy measurement indicated that Al ions might form chemical bonds with neighboring atoms and destroy the secondary structures of the protein. Our studies could deepen the understanding of the role of metal ions in the aggregation of amyloid peptides.
School of Science, Ningbo University, Ningbo 315211, China.
Lanlan
L
Su
School of Science, Ningbo University, Ningbo 315211, China.
Cheng
C
Lu
School of Science, Ningbo University, Ningbo 315211, China.
Peng
P
Yan
School of Science, Ningbo University, Ningbo 315211, China.
Nan
N
Zhang
Ningbo Institute of Material Technology and Engineering, Chinese Academy of Sciences, Ningbo 315201, China.
Sheng
S
Cai
Ningbo Institute of Material Technology and Engineering, Chinese Academy of Sciences, Ningbo 315201, China.
Gongjun
G
Zhang
School of Science, Ningbo University, Ningbo 315211, China.
Xingfei
X
Zhou
Laboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China.
Bin Li
D000535:Aluminum / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007477:Ions / Q000494:pharmacology; D058228:Islet Amyloid Polypeptide / Q000737:chemistry* / Q000235:genetics; D018625:Microscopy, Atomic Force; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D056951:Photoelectron Spectroscopy; D066329:Protein Aggregates / Q000187:drug effects*; D066263:Protein Aggregation, Pathological; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D015032:Zinc / Q000494:pharmacology
D000682:Amyloid; D007477:Ions; D058228:Islet Amyloid Polypeptide; D010446:Peptide Fragments; D066329:Protein Aggregates; D000535:Aluminum; D015032:Zinc
Thioflavin T fluorescence; X-ray photoelectron spectroscopy; atomic force microscopy; hIAPP peptides; metal ions