Neglected N-Truncated Amyloid-β Peptide and Its Mixed Cu-Zn Complexes

被引：1
作者：
Fraczyk, Tomasz [1 ]
Cieplak, Piotr [2 ]
机构：
[1] Polish Acad Sci, Inst Biochem & Biophys, Pawinskiego 5a St, PL-02106 Warsaw, Poland
[2] Sanford Burnham Prebys Med Discovery Inst, La Jolla, CA 92037 USA
来源：
PROTEIN JOURNAL | 2022年 / 41卷 / 03期
关键词：
Alzheimer's disease; Amyloid-beta; Mixed complex; Copper complex; Zinc complex; ZINC-BINDING SITE; A-BETA; ALZHEIMER-DISEASE; FIBRIL STRUCTURE; II BINDING; PROTEIN; AMYLOID-BETA(1-42); AGGREGATION; INSIGHTS; TARGETS;
D O I：
10.1007/s10930-022-10056-7
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Amyloid-beta (A beta) peptides are involved in Alzheimer's disease (AD) development. The interactions of these peptides with copper and zinc ions also seem to be crucial for this pathology. Although Cu(II) and Zn(II) ions binding by A beta peptides has been scrupulously investigated, surprisingly, this phenomenon has not been so thoroughly elucidated for N-truncated A beta(4-x)-probably the most common version of this biomolecule. This negligence also applies to mixed Cu-Zn complexes. From the structural in silico analysis presented in this work, it appears that there are two possible mixed Cu-Zn(A beta(4-x)) complexes with different stoichiometries and, consequently, distinct properties. The Cu-Zn(A beta(4-x)) complex with 1:1:1 stoichiometry may have a neuroprotective superoxide dismutase-like activity. On the other hand, another mixed 2:1:2 Cu-Zn(A beta(4-x)) complex is perhaps a seed for toxic oligomers. Hence, this work proposes a novel research direction for our better understanding of AD development.
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页码：361 / 368
页数：8
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