Current Pharmaceutical Biotechnology - Volume 11, Issue 2, 2010

A functional protein must be in its specific three dimensional native structure. All information to reach to the native state is ciphered in its amino acid sequence. However the milieu of a cell as well as stress factors presents challenges for folding to native state [1-3]. Several stress factors i.e. temperature elevation, pH, salinity and oxygen concentration alteration, ageing may influence cells and protein folding. Fortunately, hea Read More

Molecular chaperones and the heat shock response guard and modulate protein conformation, protect proteins from misfolding and aggregation, and maintain signalling and organellar networks. Overnutrition and the metabolic syndrome represent a pro-aging condition, and dietary restriction is the most robust environmental intervention that induces longevity from yeast to mammals. In recent years a considerable effort has Read More

Small heat shock proteins (sHsps) are molecular chaperones ubiquitously distributed in numerous species, from bacteria to humans. A conserved C-terminal “α-crystallin” domain organized in a β-sheet sandwich and oligomeric structure are common features of sHsps. sHsps protect cells against many kinds of stresses including heat shock, oxidative and osmotic stress. sHsps recognize unfolded proteins, prevent their irrev Read More

The most characteristic feature of neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis and Huntington's disease, is the occurrence of extra- or intracellular fibrillar aggregates containing misfolded proteins with beta-sheet conformation. These aggregates are composed of distinct proteins in each neurodegenerative disease. However, mutations in genes en Read More

Cell-penetrating peptides (CPP), also called protein transduction domains (PTD), membrane-permeable peptides (MPP), or Trojan horse peptides, have been used in many different research areas. The delivery of heat shock proteins (Hsp) using CPP has been applied in models for apoptosis, necrosis, oxidative stress, neurodegenerative diseases, stroke, cystic fibrosis, smooth muscle relaxation, myocardial injury, scar formati Read More

Screening for protein interaction partners of ion channels helps to elucidate signaling cascades to cellular targets and processes for a better understanding of the origin of diseases. Most important are the cytosolic segments of membrane- bound voltage- and ligand-gated ion channels or from ion channel regulators, which may connect to specific signaling complexes. So far, not much is known about those interactions. Mo Read More

The homeostasis of the protein synthesis and degradation is crucial for cell survival. Most age-related neurodegenerative diseases are characterized by accumulation of aberrant protein aggregates in affected brain regions. The principal routes of intracellular protein metabolism are the ubiquitin proteasome system (UPS) and the autophagy-lysosome pathway (ALP). They collaborate to degrade wasted proteins and in Read More

Protein misfolding and aggregation in the brain have been implicated as a common molecular pathogenesis of various neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and the polyglutamine (polyQ) diseases. The polyQ diseases are a group of nine hereditary neurodegenerative diseases, including Huntington's disease (HD) and various types of spinocerebellar ataxia (S Read More

Intra- and extracellular protein misfolding and aggregation is likely to contribute to a number of age-related central nervous system diseases (“proteinopathies”). Therefore, molecular chaperones, such as heat shock proteins (HSPs), that regulate protein folding, misfolding and adaption to cellular stress are emerging as therapeutic targets. Here we review the current knowledge of HSP-modulating drugs and discuss the op Read More

Heat shock proteins (Hsps) protect protein substrates against conformational damage to promote the function of the proteins, prevent aggregation and prevent formation of toxic inclusion bodies. Protein aggregates and fibrils have been associated with neurodegenerative diseases and with inclusion bodies. High-level expression of recombinant protein for biotechnological purposes often leads to insoluble inclusion bodies. Th Read More

We report a significant increase of a curcumin (1,7-bis[4-hydroxy-3-methoxyphenyl]-1,6-heptadiene-3,5-dione) fluorescence brightness when deposited on plasmonic platforms (self assembled silver nanostructures formed on the surface of silver semitransparent film). The enhancement of fluorescence intensity is accompanied by a strong decrease in fluorescence lifetime. Simultaneously, the increased photostability of cur Read More

This has reference to the recent review article entitled “Momordica balsamina; a medicinal and neutraceutical plant for health care management” which appeared in Current Pharmaceutical Biotechnology1. The article discussed medicinal aspect i.e. anti-HIV, anti-inflammatory, hypoglycaemic, anti-bacterial, anti-plasmodial anti-diarrheal, anti-oxidant and hepatoprotective properties of M. balsamina. It is a timely article, which d Read More

Full text available