lysozyme is a bactericidal enzyme whose structure and functions change in diabetes. chemical chaperones are small molecules including polyamines (e.g. spermine), amino acids (e.g. l-lysine) and polyols (e.g. glycerol). they can improve protein conformation in several stressful conditions such as glycation. in this study, the authors aimed to observe the effect of l-lysine as a chemical chaperon...

Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagentK(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperoneability of modified system by UV-Vis and fluorescence spectroscopy and theor...

What is a chaperone in the context of pharmacology? The term chaperone is borrowed from the name of a class of proteins that function in living cells [1]. Protein molecules are usually only marginally stable under physiological conditions, so some percent of them are often unfolded or misfolded. Such molecules can aggregate with one another, or with properly functioning proteins, with deleterio...

I. Protein folding in the cell. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 494 II. Molecular and chemical chaperones . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 494 A. Heat shock response and heat shock proteins . . . . . . . . . . . . . . . . . ...

Mutations in connexin 26 (Cx26) cause hearing disorders of a varying degree. Herein, to identify compounds capable restoring the function mutated Cx26, novel miniaturized microarray-based screening system was developed perform an optical assay Cx26 functionality. These molecules were identified through viability using HeLa cells expressing wild-type (WT) which exhibited sensitivity toward HSP90...

Protein aggregation and precipitation is associated with many debilitating diseases including Alzheimer's, Parkinson's, and light-chain amyloidosis. β-Casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity to protect protein form aggregation. Hofmeister salts (lyotropice series) are a class of ions which have an effect on the solubility and also the stab...

RATIONALE Doxorubicin is an effective chemotherapeutic agent for cancer, but its use is often limited by cardiotoxicity. Doxorubicin causes endoplasmic reticulum (ER) dilation in cardiomyocytes, and we have demonstrated that ER stress plays important roles in the pathophysiology of heart failure. OBJECTIVE We evaluated the role of ER stress in doxorubicin-induced cardiotoxicity and examined w...

Chemical arrays were employed to screen ligands for HtpG, the prokaryotic homologue of Hsp (heat-shock protein) 90. We found that colistins and the closely related polymyxin B interact physically with HtpG. They bind to the N-terminal domain of HtpG specifically without affecting its ATPase activity. The interaction caused inhibition of chaperone function of HtpG that suppresses thermal aggrega...

diminishing protein aggregation by chaperone is very important factor in medicine and industry. in this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by woodward reagentk(wrk) and examined on lysozyme as a target protein at ph 7.2 and outlined the mechanism for chaperoneability of modified system by uv-vis and fluorescence spectroscopy and theor...