The antimicrobial peptide Temporin-L induces vesicle formation and reduces the virulence in .

The evolution of methicillin-resistant () has required the development of new antimicrobial agents and new approaches to prevent and overcome drug resistance. AntiMicrobial Peptides (AMPs) represent promising alternatives due to their rapid bactericidal activity and their broad-spectrum of action against a wide range of microorganisms. The amphibian Temporins constitute a well-known family of AMPs with high antibacterial properties against both Gram-positive and Gram-negative bacteria.

Molecular recognition of R1-type core lipooligosaccharide by DC-SIGN.

Due to their ability to recognize carbohydrate structures, lectins emerged as potential receptors for bacterial lipopolysaccharides (LPS). Despite growing interest in investigating the association between host receptor lectins and exogenous glycan ligands, the molecular mechanisms underlying bacterial recognition by human lectins are still not fully understood. We contributed to fill this gap by unveiling the molecular basis of the interaction between the lipooligosaccharide of and the dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin (DC-SIGN).

Release of a novel peptide from ferritin nanocages: A new tool for therapeutic applications.

The development of new drug delivery systems for targeted chemotherapy release in cancer cells represents a very promising tool. In this contest, protein-based nanocages have considerable potential as drug delivery devices. Notably, ferritin has emerged as an excellent candidate due to its unique architecture, surface properties and high biocompatibility.

Towards nanostructured red-ox active bio-interfaces: Bioinspired antibacterial hybrid melanin-CeO nanoparticles for radical homeostasis.

Redox-active nano-biointerfaces are gaining weight in the field of regenerative medicine since they can act as enzymes in regulating physiological processes and enabling cell homeostasis, as well as the defense against pathogen aggression. In particular, cerium oxide nanoparticles (CeO NPs) stand as intriguing enzyme-mimicking nanoplatforms, owing to the reversible Ce/Ce surface oxidation state. Moreover, surface functionalization leads to higher catalytic activity and selectivity, as well as more tunable enzyme-mimicking performances.

Molecular recognition of sialoglycans by streptococcal Siglec-like adhesins: toward the shape of specific inhibitors.

and , commensal bacteria present in the oral cavity of healthy individuals, upon entry into the bloodstream can become pathogenic, causing infective endocarditis (IE). Sialic acid-binding serine-rich repeat adhesins on the microbial surface represent an important factor of successful infection to cause IE. They contain Siglec-like binding regions (SLBRs) that variously recognize different repertoires of -glycans, with some strains displaying high selectivity and others broader specificity.

Molecular Simplification of Natural Products: Synthesis, Antibacterial Activity, and Molecular Docking Studies of Berberine Open Models.

Berberine, the main bioactive component of many medicinal plants belonging to various genera such as , , and is a multifunctional compound. Among the numerous interesting biological properties of berberine is broad antimicrobial activity including a range of Gram-positive and Gram-negative bacteria. With the aim of identifying berberine analogues possibly endowed with higher lead-likeness and easier synthetic access, the molecular simplification approach was applied to the secondary metabolite and a series of analogues were prepared and screened for their antimicrobial activity against Gram-positive and Gram-negative bacterial test species.

The antimicrobial peptide Temporin L impairs E. coli cell division by interacting with FtsZ and the divisome complex.

Background: The comprehension of the mechanism of action of antimicrobial peptides is fundamental for the design of new antibiotics. Studies performed looking at the interaction of peptides with bacterial cells offer a faithful picture of what really happens in nature.

Methods: In this work we focused on the interaction of the peptide Temporin L with E.

Structure of the Lipopolysaccharide from the sp. ORS285 Mutant Strain.

The importance of the outer membrane and of its main constituent, lipopolysaccharide, in the symbiosis between rhizobia and leguminous host plants has been well studied. Here, the first complete structural characterization of the entire lipopolysaccharide from an O-chain-deficient ORS285 mutant is achieved by a combination of chemical analysis, NMR spectroscopy, MALDI MS and MS/MS. The lipid A structure is shown to be consistent with previously reported lipid A, that is, a heterogeneous blend of penta- to hepta-acylated species carrying a nonstoichiometric hopanoid unit and possessing very-long-chain fatty acids ranging from 26:0(25-OH) to 32:0(31-OH).

Chemistry of lipid A: at the heart of innate immunity.

In many Gram-negative bacteria, lipopolysaccharide (LPS) and its lipid A moiety are pivotal for bacterial survival. Depending on its structure, lipid A carries the toxic properties of the LPS and acts as a potent elicitor of the host innate immune system via the Toll-like receptor 4/myeloid differentiation factor 2 (TLR4/MD-2) receptor complex. It often causes a wide variety of biological effects ranging from a remarkable enhancement of the resistance to the infection to an uncontrolled and massive immune response resulting in sepsis and septic shock.