Optimization of Solid-Phase Synthesis of the 1-40 Beta-Amyloid and Preparation of Antibodies Revealing It under Immunoblotting Conditions

被引：1

作者：

Volkova, T. D. ^{[1
]}

Koroev, D. O. ^{[1
]}

Kamynina, A. V. ^{[1
]}

Filatova, M. P. ^{[1
]}

Avetisyan, A. V. ^{[2
]}

Volpina, O. M. ^{[1
]}

机构：

[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

[2] Moscow MV Lomonosov State Univ, Belozersky Res Inst Physicochem Biol, Moscow 119234, Russia

来源：

RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY | 2020年 / 46卷 / 02期

基金：

俄罗斯基础研究基金会;

关键词：

beta-amyloid; synthetic peptides; antipeptide antibodies; oligomers; ALZHEIMERS-DISEASE; PRECURSOR PROTEIN; PEPTIDE; TOXICITY;

D O I：

10.1134/S1068162020020181

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：

The solid-phase synthesis and purification of the 1-40 sequence of the human beta-amyloid were optimized, resulting in a preparation of a product with a high yield and homogeneity more than 95%. The synthetic peptide is capable of forming oligomers. This fact was confirmed by electrophoresis in the polyacrylamide gel with a subsequent immunoblotting and fluorescence spectrophotometry using the thioflavin T dye. An available method for a production of the highly specific anti-beta-amyloid antibodies with a high titer was developed. These antibodies recognized both monomeric and oligomeric forms of the 1-40 peptide of beta-amyloid under the immunoblotting conditions.

引用

页码：217 / 222

页数：6

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