Current Protein and Peptide Science - Volume 21, Issue 6, 2020

GRASP55 was first found as Golgi cisternae stacking protein. Due to the crucial role of Golgi in vesicular trafficking and protein modification, GRASP55 was found to function in these two aspects. Further investigation revealed that GRASP55 also participates in the unconventional secretory pathway under stress. Moreover, GRASP55 is involved in autophagy initiation and autophagosome maturation, as well as cell activity.

Hemoglobin and myoglobin have been considered for a long time the paradigmatic model systems for protein function, to the point of being defined the “hydrogen atom[s] of biology”. Given this privileged position and the huge amount of quantitative information available on these proteins, the red blood cell might appear as the model system and“hydrogen atom” of system biology. Indeed, since the red cell's main function is O2 transport by hemoglobin, the gap between the protein and the cell may appear quite small. Yet, a surprisingly large amount of detailed biochemical information is required for the modelization of the respiratory properties of the erythrocyte. This problem is compounded if modelization aims at uncovering or explaining evolutionarily selected functional properties of hemoglobin. The foremost difficulty lies in the fact that hemoglobins having different intrinsic properties and relatively ancient evolutionary divergence may behave similarly in the complex milieu of blood, whereas very similar hemoglobins sharing a substantial sequence similarity may present important functional differences because of the mutation of a few key residues. Thus, the functional properties of hemoglobin and blood may reflect more closely the recent environmental challenges than the remote evolutionary history of the animal. We summarize in this review the case of hemoglobins from mammals, in an attempt to provide a reasoned summary of their complexity that, we hope, may be of help to scientists interested in the quantitative exploration of the evolutionary physiology of respiration. Indeed the basis of a meaningful modelization of the red cell requires a large amount of information collected in painstaking and often forgotten studies of the biochemical properties of hemoglobin carried out over more than a century.

Protein folding is a natural phenomenon through which a linear polypeptide possessing necessary information attains three-dimension functionally active conformation. This is a complex and multistep process and therefore, the presence of several intermediary structures could be speculated as a result of protein folding. In in vivo, this folding process is governed by the assistance of other proteins called molecular chaperones and heat shock proteins. Due to the mechanism of protein folding, these intermediary structures remain major challenge for modern biology. Mutation in gene encoding amino acid can cause adverse environmental conditions which may result in misfolding of the linear polypeptide followed by the formation of aggregates and amyloidosis. Aggregation contributes to the pathophysiology of several maladies including diabetes mellitus, Huntington’s and Alzheimer’s disease. The propensity of native structure to form aggregated and fibrillar assemblies is a hallmark of amyloidosis. During aggregation of a protein, transition from α helix to β sheet is observed, and mainly β sheeted structure is visualised in a mature fibril. Heme proteins are very crucial for major life activities like transport of oxygen and carbon dioxide, synthesis of ATP, role in electron transport chain, and detoxification of free radicals formed during biochemical reactions. Any structural variation in the heme proteins may lead to a fatal response. Hence characterization of the folding intermediates becomes crucial. The characterization has been deciphered with the help of strong denaturants like acetonitrile and TFE. Moreover, possible role of elimination of these aggregates and prevention of protein denaturation is also discussed. Current review deals with the basic process and mechanism of the protein folding in general and the ultimate outcomes of the protein misfolding. Since Native conformation of heme proteins is essential for some vital activities as listed above, we have discussed possible prevention of denaturation and aggregation of heme proteins such as Hb, cyt c, catalase & peroxidase.

The peptides containing β-and γ-amino acids as building blocks display well-defined secondary structures with unique morphologies. The ability of such peptides to self-assemble into complex structures of controlled geometries has been exploited in biomedical applications. Herein, we have provided an updated overview about the peptides containing β-and γ-amino acids considering the significance and advancement in the area of development of peptide-based biomaterials having diverse applications.

Proteins are the most critical executive molecules by responding to the instructions stored in the genetic materials in any form of life. More frequently, proteins do their jobs by acting as a roleplayer that interacts with other protein(s), which is more evident when the function of a protein is examined in the real context of a cell. Identifying the interactions between (or amongst) proteins is very crucial for the biochemistry investigation of an individual protein and for the attempts aiming to draw a holo-picture for the interacting members at the scale of proteomics (or protein-protein interactions mapping). Here, we introduced the currently available reporting systems that can be used to probe the interaction between candidate protein pairs based on the fragment complementation of some particular proteins. Emphasis was put on the principles and details of experimental design. These systems are dihydrofolate reductase (DHFR), β-lactamase, tobacco etch virus (TEV) protease, luciferase, β- galactosidase, GAL4, horseradish peroxidase (HRP), focal adhesion kinase (FAK), green fluorescent protein (GFP), and ubiquitin.

Oxidative stress is the off-balance of antioxidants and free radicals. All kinds of diseases and disorders give rise to oxidative damage including autoimmune diseases. An autoimmune disorder is a pathological condition characterized by the breakdown of self-tolerance of the immune system in the body. Immunological processes against tissues and organs lead to enhanced oxidative stress and, in turn, misbalance of oxidative stress aggravates the pathobiology of the disease. Highly reactive nature of free radicals, for example hydroxyl and superoxide ions, alters DNA, protein, and lipids in the body which augment the pathologic processes of diseases. The damaged biomolecules are responsible for systemic complications and secondary disease co-morbidities. In this review, we discuss the role of oxidative stress in some incapacitating autoimmune diseases like Rheumatoid arthritis, Systemic Lupus Erythematosus, Type 1 Diabetes, and Multiple Sclerosis. Oxidative stress plays a central and course defining role in these diseases and it has become a necessity to study the pathological mechanism involved in oxidative stress to better understand and offer treatment holistically. Presently there are no clinically available parameters for measurement and treatment of pathological oxidative stress, therefore it requires intensive research. Probably, in the future, the discovery of easily detectable markers of oxidative stress can aid in the diagnosis, prognosis, and treatment of progressively destructive autoimmune diseases.

All life forms typically possess homochirality, with rare exceptions. In the case of peptides and proteins, only L-amino acids are known to be encoded by genes. Nevertheless, D-amino acids have been identified in a variety of peptides, synthesized by animal cells. They include neuroexcitatory and neuroprotective peptides, cardioexcitatory peptides, hyperglycemic hormones, opioid peptides, antimicrobial peptides, natriuretic and defensin-like peptides, and fibrinopeptides. This article is a review of their occurrence, structure and bioactivity. It further explores the pharmacology and potential medical applications of some of the peptides.