Directed Branched Polymer near an Attractive Line

We study the adsorption-desorption phase transition of directed branched polymer in $d+1$ dimensions in contact with a line by mapping it to a $d$ dimensional hard core lattice gas at negative activity. We solve the model exactly in 1+1 dimensions, and calculate the crossover exponent related to fraction of monomers adsorbed at the critical point of surface transition, and we also determine the density profile of the polymer in different phases. We also obtain the value of crossover exponent in 2+1 dimensions and give the scaling function of the sticking fraction for 1+1 and 2+1 dimensional directed branched polymer.Comment: 19 pages, 4 figures, accepted for publication in J. Phys. A:Math. Ge

Conformation and dynamics of a diluted chain in the presence of an adsorbing wall: A simulation with the bond fluctuation model

The bond fluctuation model has been used to simulate the adsorption process of a single long polymer chain on an adsorbing surface. Simulations start at high temperature with the chain in an equilibrium coil structure. The inter- and intra chain energy potential were selected in such a way that on cooling the polymer chain vitrifies without any indication of chain ordering or chain folding. The structure attained on cooling is analysed for arrange of values of the interaction potential between the surface and the polymer segments. Adsorption is measured by the fraction of polymer segments situated on the adsorbingwallwhilst crystalline ordering is characterized by the pair correlation function g(r), the bond order parameter P2(r) and the bond correlation functionM(j). Isothermal adsorption is followed as well as a function of temperature. The work shows that adsorbing surface nucleates crystalline order by suppressing one dimension in the segmental mobility of the polymer chain, along with factors as thermal treatment and inter and intra-potentials.RSS gratefully acknowledges the support of the Spanish Ministerio de Economia y Competitividad (MINECO) and FEDER funds under the project MAT2012-38359-C03-01.Sabater I Serra, R.; Torregrosa Cabanilles, C.; Meseguer Dueñas, JM.; Gómez Ribelles, JL.; Molina Mateo, J. (2014). Conformation and dynamics of a diluted chain in the presence of an adsorbing wall: A simulation with the bond fluctuation model. Journal of Non-Crystalline Solids. 402:7-15. https://doi.org/10.1016/j.jnoncrysol.2014.05.009S71540

Biochemical mechanisms implemented by human acute myeloid leukemia cells to suppress host immune surveillance

Acute myeloid leukaemia (AML) is a blood/bone marrow cancer originating from myeloid cell precusors capable of self-renewing. AML cells implement biochemical mechanisms which allow them not only to survive, but also to successfully escape immune surveillance. ln this work, we discuss crucial molecular mechanisms used by human AML cells in order to evade immune attack

Application of isothermal titration calorimetry in evaluation of protein–nanoparticle interactions

Nanoparticles (NPs) offer a number of advantages over small organic molecules for controlling protein behaviour inside the cell. Protein binding to the surface of NPs depends on their surface characteristics, composition and method of preparation (Mandal et al. in J Hazard Mater 248–249:238–245, 2013). It is important to understand the binding affinities, stoichiometries and thermodynamical parameters of NP–protein interactions in order to see which interaction will have toxic and hazardous consequences and thus to prevent it. On the other side, because proteins are on the brink of stability, they may experience interactions with some types of NPs that are strong enough to cause denaturation or significantly change their conformations with concomitant loss of their biological function. Structural changes in the protein may cause exposure of new antigenic sites, “cryptic” peptide epitopes, potentially triggering an immune response which can promote autoimmune disease (Treuel et al. in ACS Nano 8(1):503–513, 2014). Mechanistic details of protein structural changes at NP surface have still remained elusive. Understanding the formation and persistence of the protein corona is critical issue; however, there are no many analytical methods which could provide detailed information about the NP–protein interaction characteristics and about protein structural changes caused by interactions with nanoparticles. The article reviews recent studies in NP–protein interactions research and application of isothermal titration calorimetry (ITC) in this research. The study of protein structural changes upon adsorption on nanoparticle surface and application of ITC in these studies is emphasized. The data illustrate that ITC is a versatile tool for evaluation of interactions between NPs and proteins. When coupled with other analytical methods, it is important analytical tool for monitoring conformational changes in proteins

Surface thermodynamic homeostasis of salivary conditioning films through polar–apolar layering

Salivary conditioning films (SCFs) form on all surfaces exposed to the oral cavity and control diverse oral surface phenomena. Oral chemotherapeutics and dietary components present perturbations to SCFs. Here we determine the surface energetics of SCFs through contact angle measurements with various liquids on SCFs following perturbations with a variety of chemotherapeutics as well as after renewed SCF formation. Sixteen-hour SCFs on polished enamel surfaces were treated with a variety of chemotherapeutics, including toothpastes and mouthrinses. After treatment with chemotherapeutics, a SCF was applied again for 3 h. Contact angles with four different liquids on untreated and treated SCF-coated enamel surfaces were measured and surface free energies were calculated. Perturbations either caused the SCF to become more polar or more apolar, but in all cases, renewed SCF formation compensated these changes. Thus, a polar SCF attracts different salivary proteins or adsorbs proteins in a different conformation to create a more apolar SCF surface after renewed SCF formation and vice versa for apolar SCFs. This polar–apolar layering in SCF formation presents a powerful mechanism in the oral cavity to maintain surface thermodynamic homeostasis—defining oral surface properties within a narrow, biological range and influencing chemotherapeutic strategies. Surface chemical changes brought about by dietary or chemotherapeutic perturbations to SCFs make it more polar or apolar, but new SCFs are rapidly formed compensating for changes in surface energetics