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Synergistic effects and promising anticancer activities encourage the combination of non-steroidal anti-inflammatory drugs with metallodrugs. Here, we discuss the interactions of an organometallic complex consisting of an acetylsalicylic acid (ASA) moiety attached to a PtII center via an alkenol linker in a Zeise's salt-type coordination (ASA-buten-PtCl3) with model peptides angiotensin 1 (AT), substance P (Sub P), and ubiquitin (UQ). Top-down mass spectrometry experiments show that the amino acid involved in the initial binding to the metal complex controls the coordination sphere of PtII in the adducts. The strong trans labilizing effect of the coordinating sulfur atom in Met causes fast release of the organic moiety and leads to the formation of dimers and oligomers in the case of Sub P. In contrast, interactions with nitrogen donors in AT result in stable adducts containing the intact ASA-buten-PtII complex. UQ forms two sets of PtII adducts, only one of them retains the ASA moiety, which is presumably the result of an unexpected binding geometry. Importantly, UQ is additionally acetylated at various Ser and Lys residues by the ASA-buten-PtCl3 complex. Control experiments with ASA are negative. This is the first example of concomitant platination and acetylation of a peptide with an ASA metal complex.As the twenty-first-Century Maritime Silk Road tourism program aims on development of new tourist routes with special interest on the polar regions of the Arctic and the Antarctic, as well as the Tibetan Plateau, management of climate risks in travels and their reduction is an important issue for achievement of its goals at national and local levels. Acclimatization is crucial for adventurous tourists, and especially for those traveling to extremely cold and highly elevated environments, when climate and weather in tourist destination differ significantly from those at home. The Acclimatization Thermal Strain Index for Tourism (ATSIT) is designed and used to measure numerically the physiological expenses a traveler pays during the acclimatization process. The purpose of the present study is to examine acclimatization consequences for travels from Beijing, capital of China, to destinations at the Arctic, the Antarctic, and the Tibetan Plateau, collectively referred to as the 3Polar regions, during the main seasons of winter and summer, and back. The results show that acclimatizing to cold involves greater physiological strain than adjustment to heat. Acclimatization load in winter is low for all travels from Beijing and back home. ATSIT projections detect the most harmful degree of discomfort for summer travels from Beijing. The greatest acclimatization impact comes when changing locales from hot and humid to cold and dry climatic conditions, which might cause high and very high physiological strain. selleck compound Moreover, as many destinations in the 3Polar regions, mostly in the Tibetan Plateau, are located in mountains, a special acclimatization plan is required to weaken the threat of mountain sickness. The results will be helpful for warning stakeholders and the decision makers in the tourism sector of economies, and are expected to be translated into action for the development of proper intervention procedures in health control, to minimize population loss.A proposed treatment using dual-peptide ligand masks, that are functional extensions to existing analogous mammalian immune system structures, to bind to cancer cell surface proteins and stop mutating cancers that could evade presently used engineered immune cell therapies. One treatment injects the dual-peptide ligand masks into the blood stream of patients, and another treatment injects the dual-peptide ligand masks into localized cancers to bind to cancer cell surface proteins. The mammalian immune system has long used analogous, but more complex structures called pentraxins to physically link various types of pathogens to immune cells for neutralization. This treatment approach offers potential advantages in increased binding adaptability to mutations in the surface proteins of cancer cells, and potentially lower treatment cost compared to engineered immune cell treatments against cancer, especially against mutating cancer cells, even compared to extremely specific and costly monoclonal antibody treatments or engineered T cell treatments.Herpes simplex virus (HSV)-1 and HSV-2 are ubiquitous human pathogens that infect keratinized epithelial surfaces and establish lifelong latent infection in sensory neurons of the peripheral nervous system. HSV-1 causes oral cold sores, and HSV-2 causes genital lesions characterized by recurrence at the site of the initial infection. In multicellular organisms, cell death plays a pivotal role in host defense by eliminating pathogen-infected cells. Apoptosis and necrosis are readily distinguished types of cell death. Apoptosis, the main form of programmed cell death, depends on the activity of certain caspases, a family of cysteine proteases. Necroptosis, a regulated form of necrosis that is unleashed when caspase activity is compromised, requires the activation of receptor-interacting protein (RIP) kinase 3 (RIPK3) through its interaction with other RIP homotypic interaction motif (RHIM)-containing proteins such as RIPK1. To ensure lifelong infection in the host, HSV carries out sophisticated molecular strategies to evade host cell death responses during viral infection. HSV-1 is a well-characterized pathogen that encodes potent viral inhibitors that modulate both caspase activation in the apoptosis pathway and RIPK3 activation in the necroptosis pathway in a dramatic, species-specific fashion. The viral UL39-encoded viral protein ICP6, the large subunit of the virus-encoded ribonucleotide reductase, functions as a suppressor of both caspase-8 and RHIM-dependent RIPK3 activities in the natural human host. In contrast, ICP6 RHIM-mediated recruitment of RIPK3 in the nonnatural mouse host drives the direct activation of necroptosis. This chapter provides an overview of the current state of the knowledge on molecular interactions between HSV-1 viral proteins and host cell death pathways and highlights how HSV-1 manipulates cell death signals for the benefit of viral propagation.