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1. Structural Characteristics of Heparin Binding to SARS-CoV-2 Spike Protein RBD of Omicron Sub-Lineages BA.2.12.1, BA.4 and BA.5

   https://doi.org/10.3390/v14122696  

   Shi, Deling; Bu, Changkai; He, Peng; Song, Yuefan; Dordick, Jonathan S.; Linhardt, Robert J.; Chi, Lianli; Zhang, Fuming (December 2022, Viruses)

   The now prevalent Omicron variant and its subvariants/sub-lineages have led to a significant increase in COVID-19 cases and raised serious concerns about increased risk of infectivity, immune evasion, and reinfection. Heparan sulfate (HS), located on the surface of host cells, plays an important role as a co-receptor for virus–host cell interaction. The ability of heparin and HS to compete for binding of the SARS-CoV-2 spike (S) protein to cell surface HS illustrates the therapeutic potential of agents targeting protein–glycan interactions. In the current study, phylogenetic tree of variants and mutations in S protein receptor-binding domain (RBD) of Omicron BA.2.12.1, BA.4 and BA.5 were described. The binding affinity of Omicron S protein RBD to heparin was further investigated by surface plasmon resonance (SPR). Solution competition studies on the inhibitory activity of heparin oligosaccharides and desulfated heparins at different sites on S protein RBD–heparin interactions revealed that different sub-lineages tend to bind heparin with different chain lengths and sulfation patterns. Furthermore, blind docking experiments showed the contribution of basic amino acid residues in RBD and sulfo groups and carboxyl groups on heparin to the interaction. Finally, pentosan polysulfate and mucopolysaccharide polysulfate were evaluated for inhibition on the interaction of heparin and S protein RBD of Omicron BA.2.12.1, BA.4/BA.5, and both showed much stronger inhibition than heparin. 

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2. Persistent Laplacian projected Omicron BA.4 and BA.5 to become new dominating variants

   Jiahui Chen; Yuchi Qiu; Rui Wang; Guo-Wei Wei (January 2022, Computers in biology and medicine)
3. Omicron BA.1 and BA.2 variants increase the interactions of SARS-CoV-2 spike glycoprotein with ACE2

   https://doi.org/10.1016/j.jmgm.2022.108286  

   Golcuk, Mert; Yildiz, Ahmet; Gur, Mert (December 2022, Journal of Molecular Graphics and Modelling)
4. Excitation and emission spectra of Ba+ ions in solid xenon

   https://doi.org/10.1063/10.0036205  

   Soderstrom, Joe; Fairbank, David; Yvaine, Mari; Stickrod, Jaret; Jeng, Shie-Chang; Hall, Kendy; Benitez_Medina, Julio Cesar; Taylor, Connor; Stanley, Jennifer; Iverson, Alec; et al (April 2025, Low Temperature Physics)

   Excitation and emission spectra at 12 K temperature are presented for the first time for Ba+ in solid xenon. This is only the third such atomic ion studied in a solid noble gas matrix. Two groups of emission peaks, each with similar excitation spectra, photobleaching behavior and temperature dependence, are identified that may be associated with transitions from a common excited state in a particular solid xenon matrix site. Favorable conditions are found for imaging of single Ba+ ions in solid xenon, including reasonably strong emission efficiency, acceptable photobleaching and a method for overcoming background emission from the surface of the cooled sapphire window. A comparison of the new excitation spectrum of Ba+ in solid xenon with unpublished results on spectroscopy of Ba+ in liquid xenon helps confirm the identification of the latter. 

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5. Electron-phonon coupling of the iron pnictide superconductor Ba(Fe0.92Co0.08)2As2

   https://doi.org/10.1364/LS.2023.LW5F.3  

   Bartenev, Alexander; Kolodka, Roman S; Eom, Ki-Tae; Kang, Jong-Hoon; Rua, Adrian; Theran, Larry; Verbel, Camilo; Hellstrom, Eric E; Eom, Chang-Beom; Rua, Armando; et al (October 2023, Optica Publishing Group)

   Femtosecond photoexcitation of Ba(Fe_0.92Co_0.08)₂As₂superconductors reveals distinct dynamics of laser fluence-dependent ultrafast processes. The modified two-temperature model shows the complex interplay between thermalization time constants, electron-phonon coupling parameters, and level of optical excitation. 

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