No abstract

COVID‐19 is caused by the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2), which infects host cells by binding its viral spike protein receptor‐binding domain (RBD) to the angiotensin converting enzyme 2 (ACE2) on host cells. Blocking the SARS‐CoV‐2‐RBD/ACE2 interaction is, therefore, a potential strategy to inhibit viral infections. Using a novel biopanning strategy, a small anti‐ACE2 peptide is discovered, which shows high affinity and specificity to human ACE2. It blocks not only the SARS‐CoV‐2‐RBD/ACE2 interaction but also the SARS‐CoV‐1‐RBD/ACE2 interaction. Moreover, it inhibits SARS‐CoV‐2 infection in Vero‐E6 cells. The peptide shows negligible cytotoxicity in Vero‐E6 cells and Huh7 cells. In vivo short‐term lung toxicity study also demonstrates a good safety of the peptide after intratracheal administration. The anti‐ACE2 peptide can be potentially used as a prophylactic or therapeutic agent for SARS‐CoV‐2 or other ACE2‐mediated viruses. The strategy used in this study also provides a fast‐track platform to discover other antiviral peptides, which will prepare the world for future pandemics.

Blockade of the interaction between programmed cell death ligand-1 (PD-L1) and its receptor PD-1 has shown great success in cancer immunotherapy. Peptides possess unique characteristics that give them significant advantages as immune checkpoint inhibitors. However, unfavorable physicochemical properties and proteolytic stability profiles limit the translation of bioactive peptides as therapeutic agents. Studies have revealed that cyclization improves the biological activity and stability of linear peptides. In this study, we report the use of macrocyclization scanning for the discovery of cyclic anti-PD-L1 peptides with improved bioactivity. The cyclic peptides demonstrated up to a 34-fold improvement in the PD-1/PD-L1 blocking activity and significant in vivo anti-tumor activity. Our results demonstrate that macrocyclization scanning is an effective way to improve the serum stability and bioactivity of the anti-PD-L1 linear peptide. This strategy can be employed in the optimization of other bioactive peptides, particularly those for protein–protein interaction modulation.

The antimicrobial activity of 2-naphtholic and phenolic azo compounds was determined against seven microbial species, Staphylococcus aureus (ATCC 25923), Streptococcus pyrogenes (clinical), and Enterococcus faecalis (ATCC 29212), Salmonella typhi (clinical), Pseudomonas aeruginosa (ATCC 27853), Escherichia coli (ATCC 251922), and Candida albicans (ATCC 10231), using the high-throughput spot culture growth inhibition assay (HT-SPOTi). The minimum inhibitory concentrations (MIC) were determined for the active azo dyes. All the azo compounds (A1–B4) were screened for anthelmintic activity against adult Ghanaian earthworms, Hyperiodrilus spp. As part of the systematic investigation for biological activity, all the azo compounds exhibited good antimicrobial activity against the seven human pathogenic microorganisms. All the compounds exhibited anthelminthic activity against adult Ghanaian earthworms, Hyperiodrilus spp.

A simple, rapid, accurate, and less expensive spectrophotometric method has been developed for the quantitation of 5-hydroxymethyl furfural (5-HMF) levels in canned malt drinks and fruit juice drinks sampled in the Kumasi Metropolis, Ghana. The quantitation is based on the selective maximum absorption of ultraviolet radiation by 5-HMF at the wavelength (λmax) of 284 nm using acetonitrile : water (50 : 50 v/v) as the solvent system. The method was established to be specific, precise, and accurate over a concentration range of 0.001 mg/ml–0.02 mg/ml. 5-HMF levels in fruit juice samples (A1–A10) were between 0.132 mg/ml and 0.438 mg/ml, and these levels were shown to be comparable (t = 2.200;p=0.0553) to the contents in the canned malt samples (M1–M10) which were between 0.3140 mg/ml and 0.7170 mg/ml. The study failed to show any dependence of 5-HMF levels on the composition of the product as well as the manufacturing process adopted. The length of storage did also not significantly affect the 5-HMF levels in the products.

SARS‐CoV‐2 infects human cells by binding its spike protein to the human ACE2 receptor. Using a peptide biopanning strategy, the authors have discovered small anti‐ACE2 peptides that can effectively block the SARS‐CoV‐2/ACE2 interaction. The anti‐ACE2 peptides can be potentially used as prophylactic or therapeutic agents for SARS‐CoV‐2 and other ACE2‐mediated viruses. This is reported by Kun Cheng and co‐workers in article number 2100087.