Aggregation of biologically important peptides and proteins: inhibition or acceleration depending on protein and metal ion concentrations

被引:75
作者
Poulson, Benjamin Gabriel [1 ]
Szczepski, Kacper [1 ]
Lachowicz, Joanna Izabela [2 ]
Jaremko, Lukasz [1 ]
Emwas, Abdul-Hamid [3 ]
Jaremko, Mariusz [1 ]
机构
[1] KAUST, Div Biol & Environm Sci & Engn BESE, Thuwal 239556900, Saudi Arabia
[2] Univ Cagliari, Dept Med Sci & Publ Hlth, I-09042 Monserrato, Italy
[3] KAUST, Core Labs, Thuwal 239556900, Saudi Arabia
关键词
ALPHA-SYNUCLEIN AGGREGATION; ALZHEIMERS-DISEASE; A-BETA; STRUCTURAL-CHARACTERIZATION; TAU PHOSPHORYLATION; PARKINSONS-DISEASE; PRECURSOR PROTEIN; PANCREATIC-ISLETS; BINDING-SITES; IN-VITRO;
D O I
10.1039/c9ra09350h
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The process of aggregation of proteins and peptides is dependent on the concentration of proteins, and the rate of aggregation can be altered by the presence of metal ions, but this dependence is not always a straightforward relationship. In general, aggregation does not occur under normal physiological conditions, yet it can be induced in the presence of certain metal ions. However, the extent of the influence of metal ion interactions on protein aggregation has not yet been fully comprehended. A consensus has thus been difficult to reach because the acceleration/inhibition of the aggregation of proteins in the presence of metal ions depends on several factors such as pH and the concentration of the aggregated proteins involved as well as metal concentration level of metal ions. Metal ions, like Cu2+, Zn2+, Pb(2+)etc. may either accelerate or inhibit aggregation simply because the experimental conditions affect the behavior of biomolecules. It is clear that understanding the relationship between metal ion concentration and protein aggregation will prove useful for future scientific applications. This review focuses on the dependence of the aggregation of selected important biomolecules (peptides and proteins) on metal ion concentrations. We review proteins that are prone to aggregation, the result of which can cause serious neurodegenerative disorders. Furthering our understanding of the relationship between metal ion concentration and protein aggregation will prove useful for future scientific applications, such as finding therapies for neurodegenerative diseases.
引用
收藏
页码:215 / 227
页数:13
相关论文
共 141 条
[1]   α-Synuclein aggregation at low concentrations [J].
Afitska, Kseniia ;
Fucikova, Anna ;
Shvadchak, Volodymyr V. ;
Yushchenko, Dmytro A. .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2019, 1867 (7-8) :701-709
[2]   Towards the functional high-resolution coordination chemistry of blood plasma human serum albumin [J].
Al-Harthi, Samah ;
Lachowicz, Joanna Izabela ;
Nowakowski, Michal Eligiusz ;
Jaremko, Mariusz ;
Jaremko, Lukasz .
JOURNAL OF INORGANIC BIOCHEMISTRY, 2019, 198
[3]   Interaction of amylin species with transition metals and membranes [J].
Alghrably, Mawadda ;
Czaban, Iwona ;
Jaremko, Lukasz ;
Jaremko, Mariusz .
JOURNAL OF INORGANIC BIOCHEMISTRY, 2019, 191 :69-76
[4]  
[Anonymous], J NEUROINFECTIOUS DI
[5]  
[Anonymous], INORG CHEM
[6]  
[Anonymous], ALZHEIMERS DIS CELLU
[7]  
[Anonymous], CELLS BASEL
[8]   IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies [J].
Asthana, Shreyasi ;
Mallick, Bibekanand ;
Alexandrescu, Andrei T. ;
Jha, Suman .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2018, 1860 (09) :1765-1782
[9]   Physiological and pathological effects of amyloid-β species in neural stem cell biology [J].
Bernabeu-Zornoza, Adela ;
Coronel, Raquel ;
Palmer, Charlotte ;
Monteagudo, Maria ;
Zambrano, Alberto ;
Liste, Isabel .
NEURAL REGENERATION RESEARCH, 2019, 14 (12) :2035-2042
[10]   Interaction of α-synuclein with divalent metal ions reveals key differences:: A link between structure, binding specificity and fibrillation enhancement [J].
Binolfi, Andres ;
Rasia, Rodolfo M. ;
Bertoncini, Carlos W. ;
Ceolin, Marcelo ;
Zweckstetter, Markus ;
Griesinger, Christian ;
Jovin, Thomas M. ;
Fernandez, Claudio O. .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (30) :9893-9901