N-terminal [Glu]₃ moiety of γ-glutamyl peptides contributes largely to the activation of human calcium-sensing receptor, a <i>kokumi</i> receptor

γ-glutamyl peptides have been suggested to impart kokumi properties to foods by activating human calcium-sensing receptor (hCaSR). In this study, the relationship between γ-glutamyl peptide structure and hCaSR activity was systematically analyzed using γ-[Glu](n=0-4)-α-[Glu](n=0-3)-Tyr. Our results suggest that N-terminal [Glu]3 moiety is very important for hCaSR activities of γ-glutamyl peptides.</p

RaptGen-Assisted Generation of an RNA/DNA Hybrid Aptamer against SARS-CoV‑2 Spike Protein

Optimization of aptamers in length and chemistry is crucial for industrial applications. Here, we developed aptamers against the SARS-CoV-2 spike protein and achieved optimization with a deep-learning-based algorithm, RaptGen. We conducted a primer-less SELEX against the receptor binding domain (RBD) of the spike with an RNA/DNA hybrid library, and the resulting sequences were subjected to RaptGen analysis. Based on the sequence profiling by RaptGen, a short truncation aptamer of 26 nucleotides was obtained and further optimized by a chemical modification of relevant nucleotides. The resulting aptamer is bound to RBD not only of SARS-CoV-2 wildtype but also of its variants, SARS-CoV-1, and Middle East respiratory syndrome coronavirus (MERS-CoV). We concluded that the RaptGen-assisted discovery is efficient for developing optimized aptamers

MOESM1 of Six-helix bundle completion in the distal C-terminal heptad repeat region of gp41 is required for efficient human immunodeficiency virus type 1 infection

Additional file 1: Fig. S1. Interaction of the C34 (647+A) peptide with N36. A. CD spectrographic analysis of the complexes formed between N36 and C34 or its mutant C34 (647+A). Left panel, the secondary structure of complexes formed by C34 and N36 (dark blue) or C34 (647+A) and N36 (orange). Right panel, the stability of complexes formed by C34 with N36 (dark gray) and its mutants (light gray), as measured by thermal denaturation analysis

Additional file 1: of A method of producing genetically manipulated mouse mammary gland

Table S1. Electroporation parameters obtained by NEPA21 electroporator (NEPAGENE) for gene transduction into MaSC-enriched cells. Figure S1. Isolation of basal/MaSC fraction from female mice aged 8–10 weeks. a Singlet sorting. b Further singlet sorting. c Lin(−) 7-AAD(−) sorting, excluding hematopoietic, endothelial, and stromal cells (Lin(+)), and dead cells (7-AAD(+)). d Sorting of basal/MaSC fraction by CD49f and CD24. Figure S2. Dox-dependent expression of TRE3G-EGFP gene-introduced MECs under MMF culture. Red fluorescence shows mCherry marker driven by PCAG. Scale bar = 500 μm. (DOCX 1884 kb