The field of medical diagnostics and therapeutics is being revolutionized by nanotechnology, from targeted drug delivery to cancer immunotherapy. Inorganic nanoparticles are widely used, albeit problems with agglutination, cytotoxicity, free radical generation, and instability in some biological environments limits their utility. Conjugation of biomolecules such as peptides to the surface of nanoparticles can mitigate such problems, as well as confer specialized theranostic (therapeutic and/or diagnostic) properties, useful across biomedical applications such as vaccines, drug delivery, and in vivo imaging. Coating with amino acids, rather than peptides, offers further a highly cost-effective approach (due to their ease of purification and availability), but is currently an underutilized way to decrease toxicity and enhance stability. Amino acid molecules are small (<200 Da) and have both positive and negative charge groups (zwitterionic) facilitating charge-specific molecule binding. Additionally, amino acids exert by themselves some useful biological functions, with antibacterial and viability enhancing properties (for eukaryotic cells). Overall particle size, nanoparticle core, and the specific amino acid used to functionalize their surface influence their biodistribution, and their effects on host immunity. In this review, we provide for the first time an overview of this emerging field, and identify gaps in knowledge for future research.

The rising incidence of drug resistant diseases has led to an increasing need for developing novel and efficient antimicrobial products that can counter these infections. We report for the first time, the exceptional antibacterial activity of N-doped carbon nanosheets (CNS). The antibacterial activity and mechanism of action of CNS was examined for gram negative E. coli. Based on the cell viability tests, nucleic acid quantitation, time and concentration dependent antibacterial activity tests and SEM and TEM micrographs, performed under similar concentration and incubation conditions, the CNS dispersion shows the highest antibacterial activity, sequentially followed by GO, rGO and CCM, with a loss of cell viability by 92.1 AE 1.7%. We envision that the physical stress and piercing action caused by sharp "knifeedges" as well as the presence of heteroatoms in CNS result in the rupturing of the bacterial cell wall, eventually causing cell death. The high I D /I G ratio (0.99) of CNS is closely related to the formation of structural and edge plane defects, especially in the case of N-doped carbonaceous materials, which is one of the key factors in enhancing the antibacterial activity of the material.

A new synthetic peptide is presented. A Glu residue binds through H-bonding to a guanine-base and a Trp residue intercalates with K+ resulting in stabilization of a human telomeric G-quadruplex with high selectivity over a complementary c-rich strand and double-stranded DNA.

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Airway inflammatory disorders are prevalent diseases in need of better management and new therapeutics. Immunotherapies offer a solution to the problem of corticosteroid resistance. Areas covered: The current review focuses on lipopolysaccharide (Gram-negative bacterial endotoxin)-mediated inflammation in the lung and the animal models used to study related diseases. Endotoxin-induced lung pathology is usually initiated by antigen presenting cells (APC). We will discuss different subsets of APC including lung dendritic cells and macrophages, and their role in responding to endotoxin and environmental challenges. Expert commentary: The pharmacotherapeutic considerations to combat airway inflammation should cost-effectively improve quality of life with sustainable and safe strategies. Selectively targeting APCs in the lung offer the potential for a promising new strategy for the better management and treatment of inflammatory lung disease.

Schematic representation of (HTPu–var-1-G4) located at the 3′ end, formation of G-quadruplex, model of the G-quadruplex structure, base stacking between G-quadruplex planes, G-quadruplex structure-peptide complex and twisting of G-quadruplex planes upon peptide binding.

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