Correction: Sulatskaya et al. Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T. 2018, , 2762.

In the original publication [...

Polymer Particles Bearing Recombinant LEL CD81 as Trapping Systems for Hepatitis C Virus.

Hepatitis C is one of the most common social diseases in the world. The improvements in both the early diagnostics of the hepatitis C and the treatment of acute viremia caused by hepatitis C virus are undoubtedly an urgent task. In present work, we offered the micro- and nanotraps for the capturing of HCV.

Towards the Development of a 3-D Biochip for the Detection of Hepatitis C Virus.

The early diagnostics of hepatitis C virus (HCV) infections is currently one of the most highly demanded medical tasks. This study is devoted to the development of biochips (microarrays) that can be applied for the detection of HCV. The analytical platforms of suggested devices were based on macroporous poly(glycidyl methacrylate--di(ethylene glycol) dimethacrylate) monolithic material.

Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T.

The persistence of high concentrations of beta-2-microglobulin (β2M) in the blood of patients with acute renal failure leads to the development of the dialysis-related amyloidosis. This disease manifests in the deposition of amyloid fibrils formed from the various forms of β2M in the tissues and biological fluids of patients. In this paper, the amyloid fibrils formed from the full-length β2M (β2m) and its variants that lack the 6 and 10 N-terminal amino acids of the protein polypeptide chain (ΔN6β2m and ΔN10β2m, respectively) were probed by using the fluorescent dye thioflavin T (ThT).

Fluorescent characterization of amyloid deposits in the kidneys of mdx mice.

Amyloidosis is a group of diseases that occurs when amyloid proteins are deposited in tissues and organs. The traditional way of identifying amyloid in tissue sections is staining with Congo red. However, this method has a number of limitations including background staining (background fluorescence), low fluorescence intensity and false-positive staining.

Monitoring of actin unfolding by room temperature tryptophan phosphorescence.

Slow intramolecular mobility of native and inactivated actin from rabbit skeletal muscle during the process of protein unfolding induced by GdnHCl was studied using tryptophan room temperature phosphorescence (RTP). By this method, the conclusion was confirmed that an essentially unfolded intermediate preceded the formation of inactivated actin [Turoverov et al. Biochemistry (2002) 41, 1014-1019].

Expression of recombinant GFP-actin fusion protein in the methylotrophic yeast Pichia pastoris.

The integrative vector pPIC3 for the yeast Pichia pastoris and a cDNA fragment encoding a fusion protein consisting of green fluorescent protein (GFP) and actin 5C of the fruit fly Drosophila melanogaster were used to construct a pPIC3-GFP-actin 5C expression plasmid. The P. pastoris host strain GS115 was transformed with the pPIC3-GFP-actin 5C carrying HIS4 as a selective marker.

The place of inactivated actin and its kinetic predecessor in actin folding-unfolding.

The kinetics of actin unfolding induced by guanidine hydrochloride of different concentrations was studied. The parametric representation of the kinetic dependencies of tryptophan fluorescence intensity changes recorded at two wavelengths allowed us to detect and characterize a new essentially unfolded kinetic intermediate. Its characteristics suggested that this intermediate state is a premolten globule.

Kinetics of actin unfolding induced by guanidine hydrochloride.

The kinetics of actin unfolding induced by guanidine hydrochloride has been studied. On the basis of obtained experimental data a new kinetic pathway of actin unfolding was proposed. We have shown that the transition from native to inactivated actin induced by guanidine hydrochloride (GdnHCl) passes through essential unfolding of the protein.

Human alpha-fetoprotein as a Zn(2+)-binding protein. Tight cation binding is not accompanied by global changes in protein structure and stability.

The binding of zinc to human alpha-fetoprotein (AFP) isolated from human umbilical cord serum was studied by fluorimetric Zn(2+)-titration. We found that the total number of strong binding sites for zinc on this protein was 5: AFP has one very strong (dissociation constant, K(d)<10(-8) M) and at least four lower affinity zinc binding sites (K(d)<10(-5) M). Fourier transform infrared (FTIR) analysis revealed that aspartate and histidine residues could be involved in the strong coordination of zinc.