Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge.

Using the framework of an investigation of the stimuli-responsive behavior of peptide assembly on a solid surface, this study on the behavior of a chemisorbed peptide on a gold surface was performed. The studied peptide is a dimeric form of the antimicrobial peptide Trichogin GAIV, which was also modified by substituting the glycine with lysine residues, while the N-terminus octanoyl group was replaced by a lipoic one that was able to bind to the gold surface. In this way, a chemically linked peptide assembly that is pH-responsive was obtained because of the protonation/deprotonation of the sidechains of the Lys residues.

Unveiling the self-assembly process of gellan-chitosan complexes through a combination of atomistic simulations and experiments.

Polyelectrolyte complexes (PECs), formed via the self-assembly of oppositely charged polysaccharides, are highly valued for their biocompatibility, biodegradability, and hydrophilicity, offering significant potential for biotechnological applications. However, the complex nature and lack of insight at a molecular level into polyelectrolytes conformation and aggregation often hinders the possibility of achieving an optimal control of PEC systems, limiting their practical applications. To address this problem, an in-depth investigation of PECs microscopic structural organization is required.

Words as social tools (WAT): A reprise.

The paper presents new evidence collected in the last five years supporting the Words As social Tools proposal on abstract concepts. We discuss findings revolving around three central tenets. First, we show that-like concrete concepts-also abstract concepts evoke sensorimotor experiences, even if to a lower extent, and that they are linked to inner experiences (e.

Advanced label-free electrochemical immunosensor for a minimally invasive detection of proteins in paintings.

In recent decades, scientific methodologies applied in theCultural Heritage field have been growing, due to their pivotal role in guiding informed decisions concerning conservation strategies and daily maintenance. To achieve this goal, minimally/non-invasive quantitative and qualitative analyses are needed. However, the non-invasive and selective identification of proteinaceous binders and coatings in artworks represent an open issue in Cultural Heritage science.

Immunological and homeostatic pathways of alpha -1 antitrypsin: a new therapeutic potential.

α -1 antitrypsin (A1AT) is a 52 kDa acute-phase glycoprotein belonging to the serine protease inhibitor superfamily (SERPIN). It is primarily synthesized by hepatocytes and to a lesser extent by monocytes, macrophages, intestinal epithelial cells, and bronchial epithelial cells. A1AT is encoded by SERPINA1 locus, also known as PI locus, highly polymorphic with at least 100 allelic variants described and responsible for different A1AT serum levels and function.