conclusions accordingly, it can be concluded that locally low temperatures and acidic conditions are the main suspected reasons for protein misfolding. results based on the study findings the low temperature, 0°c, and acidic condition change the structure more strongly than other mentioned conditions. the low temperature and acidic conditions seem to have the most misfolding effect on insulin s...

estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. a...

background: protein aggregation is one of the important, common and troubling problems in biotechnology, pharmaceutical industries and amyloid-related disorders. methods: in the present study, the inhibitory effects of some carbohydrates (alginate, β-cyclodextrin and trehalose) on the formation of nano-globular aggregates from normal (hsa) and glycated (ghsa) human serum albumin were studied; w...

protein aggregation is a serious problem for both biotechnology and cell biology. diseases such as prion misfolding, alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutati...

the aggregation of protein is the most prevalent and the most disturbing kind of instability and this challenge exists in almost every stage of the development of protein drug. the presence of insoluble aggregations in protein drugs will make the supply of the product a tough job. this study identifies the inhibition of the folded interferon beta 1-b’s aggregation with the assistance of some ex...

Protein aggregation is phenomenon wherein protein loses its native structure and aggregates due to the adaption of non-native conformation. Amyloid aggregation formed by the accumulation of various proteins causes many diseases in humans and other organisms. Antioxidants can prevent proteins aggregation. Pulicaria undulata  extract along with phenolic compounds can increase protein stability an...

objective(s):alzheimer's disease (ad) is the most common age-related neurodegenerative disorder. one of the hallmarks of ad is an abnormal accumulation of fibril forms of tau protein which is known as a microtubule associated protein. in this regard, inhibition of tau aggregation has been documented to be a potent therapeutic approach in ad and tauopathies. unfortunately, the available syn...

Objective(s):Alzheimer's disease (AD) is the most common age-related neurodegenerative disorder. One of the hallmarks of AD is an abnormal accumulation of fibril forms of tau protein which is known as a microtubule associated protein. In this regard, inhibition of tau aggregation has been documented to be a potent therapeutic approach in AD and tauopathies. Unfortunately, the available syntheti...

A major problem in the formulation of therapeutic proteins is the irreversible protein aggregation. Recombinant human interferon alpha2b (rhIFN2b) has poor stability and undergoes physical degradation. The aim of this study was to investigate the effect of solution conditions on the heat-induced aggregation of rhIFNα2b. The protein was incubated for 1 h at 40°C–70°C and for up to 240 h at 50C...

A major problem in the formulation of therapeutic proteins is the irreversible protein aggregation. Recombinant human interferon alpha2b (rhIFN2b) has poor stability and undergoes physical degradation. The aim of this study was to investigate the effect of solution conditions on the heat-induced aggregation of rhIFNα2b. The protein was incubated for 1 h at 40°C–70°C and for up to 240 h at 50C...