Current Protein and Peptide Science - Volume 23, Issue 1, 2022

Previously, the application of proteins was uncommon as therapeutically active molecules. Some of the first applications of proteins as drugs have been insulin and vaccines for overcoming a physiological deficiency and the prevention of diseases, respectively. Nowadays, proteins have many applications, not only as drugs but also as drug delivery systems to be administered by different routes. Due to their nature, the behavio Read More

Antimicrobial Peptides (AMPs) are small, ribosomally synthesized proteins found in nearly all forms of life. In plants, AMPs play a central role in plant defense due to their distinct physicochemical properties. Due to their broad-spectrum antimicrobial activity and rapid killing action, plant AMPs have become important candidates for the development of new drugs to control plant and animal pathogens that are resistant to multip Read More

Over the past two decades, the advances in the next generation sequencing (NGS) platforms have led to the identification of numerous genes/QTLs at high-resolution for their potential use in crop improvement. The genomic resources generated through these high-throughput sequencing techniques have been efficiently used in screening of particular gene of interest particularly for numerous types of plant stresses and qu Read More

Background: COVID-19 is a global threat as a result of the incessant spread of SARS-CoV- 2, necessitating the rapid availability of effective antiviral medications to protect our society. For SARSCoV- 2, a group of peptides has already been indicated, although their effectiveness has yet to be shown. SARS-CoV-2 is an enveloped virus with hydrophobic fusion protein and spike glycoproteins. Methods: Here, we have compiled a li Read More

Background: An extensive study of the folding and stability of proteins and their complexes has revealed a number of problems and questions that need to be answered. One of them is the effect of chaperones on the process of fibrillation of various proteins and peptides. Methods: We studied the effect of molecular chaperones, such as GroEL and α-crystallin, on the fibrillogenesis of the Aβ(1-42) peptide using electron microsc Read More

Background: The importance of aromaticity vs. hydrophobicity of the central hydrophobic core (CHC, residues 17-20) in governing fibril formation in Aβ(1-42) has been the focus of an ongoing debate in the literature. Introduction: Mutations in the CHC (especially at Phe19 and Phe20) have been used to examine the relative impact of hydrophobicity and aromaticity on the degree of aggregation of Aβ(1-42). However, the results h Read More