In this work, a series of boronated amidines based on the -dodecaborate anion and amino acids containing an amino group in the side chain of the general formula [BHNHC(NH(CH)CH(NH)COOH)CH], where n = 2, 3, 4, were synthesized. These derivatives contain conserved α-amino and α-carboxyl groups recognized by the binding centers of the large neutral amino acid transporter (LAT) system, which serves as a target for the clinically applied BNCT agent para-boronophenylalanine (BPA). The paper describes several approaches to synthesizing the target compounds, their acute toxicity studies, and tumor uptake studies in vivo in two tumor models.
View Article and Find Full Text PDFMagnonics, which harnesses the unique properties of spin waves, offers promising advancements in data processing due to its broad frequency range, nonlinear dynamics, and scalability for on-chip integration. Effective information encoding in magnonic systems requires precise spatial and temporal control of spin waves. Here, we demonstrate the rapid optical control of spin-wave transport in hybrid magnonic-plasmonic structures.
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December 2024
New derivatives of the -decaborate anion [BH-O(CH)O(CH)C(O)-L-OCH] (An) (: L = Trp; : L = His; : L = Met; : L = Ala(2-oxopyrrolidin-3-yl) (Pld) were synthesized and isolated as tetraphenylphosphonium salts (PhP)An. Anions ; ; , and contain a pendant functional group from the L-tryptophan methyl ester, L-histidine methyl ester, L-methionine methyl ester, or methyl 2-amino-3-(2-oxopyrrolidin-3-yl)propanoate (-Trp-OCH, -His-OCH, -Met-OCH, or -Pld-OCH) residue, respectively, bonded with the boron cluster anion through the oxybis[(ethane-2,1-diyl)oxy] spacer. This pacer is formed as a result of the nucleophilic opening of the attached dioxane molecule in the [BHO(CH)O] starting derivative.
View Article and Find Full Text PDFDNA polymerases from the hyperthermophilic Archaea have attracted considerable attention as PCR enzymes due to their high thermal stability and proofreading 3' → 5' exonuclease activity. This study is the first to report data concerning the purification and biochemical characteristics of the Tst DNA polymerase from . Both the wild type Tst(wt) DNA polymerase and its chimeric form containing the P36H substitution-which reduces the enzyme's affinity for the U-containing template and dUTP-and the DNA-binding domain Sso7d from were obtained and analyzed.
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