Protein and Peptide Letters - Volume 24, Issue 4, 2017

Enzymes and structural proteins dominated thinking about protein structure and function for most of the twentieth century. In recent decades, however, we have begun to appreciate the significant physiological and pathological roles of nonglobular proteins. Amyloids first gained infamy from their implications in a score of human mortal diseases. However, they have recently been discovered to play vital physiological rol Read More

An increasing spectrum of diseases more than neurodegenerative diseases is characteristic of aggregation of specific proteins, while aggregation of a large number of non-specific proteins are associated with aging down to Escherichia coli. Triggered by disease-causing mutations and agingassociated damages, many well-folded cytosolic proteins become “completely insoluble” in vivo. As facilitated by our discovery in 2 Read More

The major len protein α B-crystallin (α B) is an intracellular chaperone. It belongs to the family of small heat shock proteins (sHsps) which plays a critical role in maintaining protein homeostasis and preventing protein aggregation, especially under stress conditions. Dysfunction of α B is closely related to cataract, and many neurodegenerative diseases including Alzheimer’s, Parkinson’s, and Creutzfeldt-Jakob disease. Due to the Read More

Alzheimer’s disease (AD) has become the most common neurodegenerative disease. The deposition of amyloid fibrils in the brain is one of the characteristics of AD. The fibrils are composed of amyloid-β peptide (Aβ). Aβ is produced through a series event of protease cleavage of a transmembrane protein called β-amyloid precursor protein (APP) which is commonly expressed in the brain. The production of Aβ and it Read More

Protein misfolding and aggregation is a key attribute of different neurodegenerative diseases. Misfolded and aggregated proteins are intrinsically disordered and rule out structure based drug design. The comprehensive characterization of misfolded proteins and associated aggregation pathway is prerequisite to develop therapeutics for neurodegenerative diseases caused due to the protein aggregation. Visible protein a Read More

Since cell adhesion is important for cell processes such as migration and proliferation, it is a crucial consideration in biomaterial design and development. Based on the fusion of mussel adhesive protein fp151 with laminin-1-originated functional peptides we designed fusion proteins (fLA4, fLG6 and fAG73) and explored their cell adhesion properties. In our study, cell adhesion analysis showed that protein fLG6 and fLA Read More

Mutations of tumor suppressor protein p53 are present in almost about 50% of all cancers. It has been reported that the p53 mutations cause aggregation and subsequent loss of p53 function, leading to cancer progression. Here in this study we focus on the inhibitory effects of cationic osmolyte molecules acetylcholine chloride, and choline on an aggregation prone 10 amino acid p53 mutant peptide WRPILTIITL, and the Read More

The conformational stability of the Cold shock protein A (CspA) from C. pseudotuberculosis (Cp), a nucleic acid binding protein in function of pH and salt concentration was examined by using differential scanning calorimetry and CD spectroscopy in combination with computational analysis to identify the specify amino acids undergoing change. Our approach identified a sodiumbinding site in CpCspA and at pH 8.0 a significant r Read More

2S albumin is a low-molecular-weight seed storage protein belonging to the prolamin superfamily. In the present work a small 2S albumin (WTA) protein of ~16 kDa has been purified from the seeds of Wrightia tinctoria. The WTA is a heterodimer protein with a small subunit of ~5 kDa and a larger subunit of ~11 kDa bridged together through disulphide bonds. The protein exhibits deoxyribonucleases activity against closed cir Read More