Academic Journal

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

التفاصيل البيبلوغرافية
العنوان: FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts
المؤلفون: Dmitrii Usoltsev, Vera Sitnikova, Andrey Kajava, Mayya Uspenskaya
المصدر: Biomolecules, Vol 10, Iss 4, p 606 (2020)
بيانات النشر: MDPI AG, 2020.
سنة النشر: 2020
المجموعة: LCC:Microbiology
مصطلحات موضوعية: protein denaturation, FTIR spectroscopy, second derivative method, secondary structure, neutral salts, aggregates, Microbiology, QR1-502
الوصف: The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH4)2SO4). The changes in the secondary structure were studied at 23 °C and 80 °C by using the second derivative deconvolution method of the IR spectra. Our results demonstrated that the ability of the salts to stabilize/destabilize these two proteins correlates with the Hofmeister series of ions. At the same time, some exceptions were also observed. The destabilization of the native structures of both α-helical albumin and β-structural trypsin upon interaction with neutral salts leads to the formation of intermolecular β-sheets typical for amyloid fibrils or amorphous aggregates. Thus, our quantitative FTIR-spectroscopy analysis allowed us to further clarify the mechanisms and complexity of the neutral salt actions on protein structures which may lead to strategies preventing unwelcome misfolding of proteins.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2218-273X
Relation: https://www.mdpi.com/2218-273X/10/4/606; https://doaj.org/toc/2218-273X
DOI: 10.3390/biom10040606
URL الوصول: https://doaj.org/article/87831b01f712422f996494be2db64986
رقم الانضمام: edsdoj.87831b01f712422f996494be2db64986
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2218273X
DOI:10.3390/biom10040606