Chemical proteomics relies primarily on click-chemistry-based protein labeling and biotin-streptavidin enrichment, but these techniques have inherent limitations. Enrichment of intracellular proteins using a totally synthetic host-guest complex is described, overcoming the problem associated with the classical approach. We achieve this by affinity-based protein labeling with a target-specific probe molecule conjugated to a high-affinity guest (suberanilohydroxamic acid-ammonium-adamantane; SAHA-Ad) and then enriching the labeled species using a cucurbit[7]uril bead. This method shows high specificity for labeled molecules in a MDA-MB-231 breast cancer cell lysate. Moreover, this method shows promise for labeling proteins in live cells.

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A series of novel dendrimers with pyrrolidine as surface group has been achieved in high yields by terminal-group modification on chalcone dendrimers through the application of 1,3-dipolar cycloaddition reaction. In 1,3-dipolar cycloaddition, azomethine ylides (AMY) with alkenes afforded five-membered N-methyl pyrrolidine. The formation of N-methyl pyrrolidine in the dendritic structure would be an important candidate in the field of biology and pharmacology.Design and synthesis of dendritic architectures have been active areas of research because of their countless applications in the field of biology and material sciences. 1-4 Dendrimers are highly branched, regularly ordered monodisperse three-dimensional architecture. The combination of discrete numbers of functionalities and high local densities of active groups in dendrimers has attracted a lot of attention from those active in medicinal chemistry. 5,6 In this way, introduction of heterocyclic unit into dendritic structure would be an important candidate for medicinal applications.Pyrrolidine, an important nucleus in the five-membered heterocyclic ring systems, is one of the main building blocks for the syntheses of many natural products and pharmaceuticals. 7-12 The 1,3-dipolar cycloaddition reaction of azomethine ylides (AMY) with alkenes is a powerful method for the synthesis of pyrrolidines with high stereoselectivity. 13,14 Pyrrolidine and its derivatives have gained much attention during recent years due to their interesting biological and medicinal properties. Pyrrolidine derivatives find applications as organocatalytic and semiconducting agents. 15-17 Pyrrolidine derivatives play a crucial role in pharmacological applications such as preventing and treating rheumatoid arthritis, asthma, allergies, rhinitis, and related diseases as they inhibit the production of intracellular phospholipase A2 and prostaglandin E2. 18 Furthermore, pyrrolidines are important building blocks in organic synthesis. [19][20][21] Methodology plays a pivotal role for the synthesis of dendrimers in modern chemistry. Recently, cycloaddition reactions are being involved for the synthesis of such dendrimers. 22,23 In this association, 1,3-dipolar cycloaddition is one of the most powerful method to introduce five-membered heterocycles in to the dendritic architectures. 24,25 Recently, our research group has reported the synthesis of novel dendrimers with chalcone and carbohydrate moiety at the surface using 'click' methodology. 26,27 In connection with this, we report herein the synthesis of some novel pyrrolidine dendrimers 1-4 ( Figure 1) through 1,3-dipolar cycloaddition reaction using previously reported chalcone dendrimers 5-8. 28 In order to synthesize the pyrrolidine dendrimer 1, the dendritic chalcone 5 underwent 1,3-dipolar cycloaddition reaction with 3.1 equivalents of sarcosine and 6.0 equivalents of paraformaldehyde in toluene under refluxing condition for 12 hours to give the pyrrolidine dendrimer 1 in 91% yield (Scheme 1). The 1 H NMR spectrum of 1 displayed three s...

Chemical proteomics relies primarily on click‐chemistry‐based protein labeling and biotin‐streptavidin enrichment, but these techniques have inherent limitations. Enrichment of intracellular proteins using a totally synthetic host–guest complex is described, overcoming the problem associated with the classical approach. We achieve this by affinity‐based protein labeling with a target‐specific probe molecule conjugated to a high‐affinity guest (suberanilohydroxamic acid–ammonium‐adamantane; SAHA‐Ad) and then enriching the labeled species using a cucurbit[7]uril bead. This method shows high specificity for labeled molecules in a MDA‐MB‐231 breast cancer cell lysate. Moreover, this method shows promise for labeling proteins in live cells.

Antibacterial activity against Shigella dysenteriae, Staphylococcus aureus and Serratia marcescen was studied with S-BINOL based triazole dendrimers 1, 2 and 3 with m-terphenyl surface units. Supported by molecular docking studies, the activity dendrimer 2 was comparable to that of streptomycin.