The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

被引：12

作者：

Makshakova, Olga ^{[1
]}

Bogdanova, Liliya ^{[1
]}

Faizullin, Dzhigangir ^{[1
]}

Khaibrakhmanova, Diliara ^{[2
]}

Ziganshina, Sufia ^{[3
]}

Ermakova, Elena ^{[1
]}

Zuev, Yuriy ^{[1
]}

Sedov, Igor ^{[1
,2
]}

机构：

[1] Kazan Inst Biochem & Biophys, FRC Kazan Sci Ctr RAS, Kazan 420111, Russia

[2] Kazan Fed Univ, Chem Inst, Kazan 420111, Russia

[3] Zavoisky Phys Tech Inst, FRC Kazan Sci Ctr RAS, Phys 3Zavoisky, Kazan 420029, Russia

来源：

PHARMACEUTICS | 2023年 / 15卷 / 02期

关键词：

lysozyme; amyloid fibrils; disaggregation; polysaccharides; carrageenan; alginate; galactan; chitosan; infrared spectroscopy; atomic force microscopy; EGG-WHITE LYSOZYME; AGGREGATION; GLYCOSAMINOGLYCANS; CHITOSAN; NANOPARTICLES; INHIBITION; OLIGOMER; PEPTIDE; HEPARIN; MODEL;

D O I：

10.3390/pharmaceutics15020624

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The deposition of proteins in the form of insoluble amyloid fibril aggregates is linked to a range of diseases. The supramolecular architecture of such deposits is governed by the propagation of beta-strands in the direction of protofilament growth. In the present study, we analyze the structural changes of hen egg-white lysozyme fibrils upon their interactions with a range of polysaccharides, using AFM and FTIR spectroscopy. Linear anionic polysaccharides, such as kappa-carrageenan and sodium alginate, are shown to be capable to disaggregate protofilaments with eventual protein renaturation. The results help to understand the mechanism of amyloid disaggregation and create a platform for both the development of new therapeutic agents for amyloidose treatment, and the design of novel functional protein-polysaccharide complex-based nanomaterials.

引用

页数：17

共 82 条

[51] Inhibition of Glycosaminoglycan-Mediated Amyloid Formation by Islet Amyloid Polypeptide and proIAPP Processing Intermediates [J].