Structural changes induced in proteins by therapeutic ultrasounds

被引：52

作者：

Marchioni, C. ^{[1
]}

Riccardi, E. ^{[1
]}

Spinelli, S. ^{[1
]}

Dell'Unto, F. ^{[1
]}

Grimaldi, P. ^{[1
]}

Bedini, A. ^{[2
]}

Giliberti, C. ^{[2
]}

Giuliani, L. ^{[2
]}

Palomba, R. ^{[2
]}

Castellano, A. Congiu ^{[1
]}

机构：

[1] Univ Roma La Sapienza, Dipartimento Fis, I-00185 Rome, Italy

[2] ISPESL, Rome, Italy

来源：

ULTRASONICS | 2009年 / 49卷 / 6-7期

关键词：

Ultrasound; Spectroscopy; FTIR; Circular dichroism; Proteins; Structure; SECONDARY-STRUCTURE; CAVITATION; SPECTRA; PULSE;

D O I：

10.1016/j.ultras.2009.02.003

中图分类号：

O42 [声学];

学科分类号：

070206 ; 082403 ;

摘要：

The structural effect induced by therapeutic ultrasound on proteins in aqueous solution has been investigated with FTIR spectroscopy, UV-VIS spectroscopy, circular dichroism and light scattering. Six proteins (cytochrome, lysozyme, myoglobin, bovine serum albumin, trypsinogen, and alpha-chymotrypsinogen A) with different molecular weight and secondary structure have been studied. The experiment has been performed using an ultrasound source at resonant frequency of 1 MHz and sonication times of 10, 20, 30, 40, 50, and 60 min. A different behaviour of proteins under sonication depends on the dominant secondary structure type (alpha-helix or beta-sheets) and on the grade of the ordered structure. The results suggest that the free radicals, produced by water sonolysis, have an important role in the changes of structural order. (C) 2009 Elsevier B. V. All rights reserved.

引用

页码：569 / 576

页数：8

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