B →Vℓ+ℓ− in the Standard Model from light-cone sum rules

We present $B_q\to\rho$, $B_q\to\omega$, $B_q\to K^*$, $B_s\to K^*$ and $B_s\to \phi$ form factors from light-cone sum rules (LCSR) at $\mathcal{O}(\alpha_s)$ for twist-2 and 3 and $\mathcal{O}(\alpha_s^0)$ for twist-4 with updated hadronic input parameters. Three asymptotic light-cone distribution amplitudes of twist-$4$ (and $5$) are determined, necessary for the form factors to obey the equations of motion. It is argued that the latter constrain the uncertainty of tensor-to-vector form factor ratios thereby improving the prediction of zeros of helicity amplitudes of major importance for $B\to K^*\ell\ell$ angular observables. We provide easy-to-use fits to the LCSR results, including the full error correlation matrix, in all modes at low $q^2$ as well as combined fits to LCSR and lattice results covering the entire kinematic range for $B_q\to K^*$, $B_s\to K^*$ and $B_s\to \phi$. The error correlation matrix avoids the problem of overestimating the uncertainty in phenomenological applications. Using the new form factors and recent computations of non-factorisable contributions we provide Standard Model predictions for $B\to K^*\gamma$ as well as $B\to K^*\ell^+\ell^-$ and $B_s\to\phi\mu^+\mu^-$ at low dilepton invariant mass. Employing our $B \to (\rho,\omega)$ form factor results we extract the CKM element $|V_\mathrm{ub}|$ from the semileptonic decays $B\to(\rho,\omega) \ell\nu$ and find good agreement with other exclusive determinations.Comment: 64 pages, 7 figures, 15 tables. v3: Minor clarifications, numerics unchanged. Matches version published in JHE

Intrinsic Determinants of Aβ12–24 pH-Dependent Self-Assembly Revealed by Combined Computational and Experimental Studies

The propensity of amyloid- (A) peptide to self-assemble into highly ordered amyloid structures lies at the core of their accumulation in the brain during Alzheimer's disease. By using all-atom explicit solvent replica exchange molecular dynamics simulations, we elucidated at the atomic level the intrinsic determinants of the pH-dependent dimerization of the central hydrophobic segment A and related these with the propensity to form amyloid fibrils measured by experimental tools such as atomic force microscopy and fluorescence. The process of A dimerization was evaluated in terms of free energy landscape, side-chain two-dimensional contact probability maps, -sheet registries, potential mean force as a function of inter-chain distances, secondary structure development and radial solvation distributions. We showed that dimerization is a key event in A amyloid formation; it is highly prompted in the order of pH 5.02.98.4 and determines further amyloid growth. The dimerization is governed by a dynamic interplay of hydrophobic, electrostatic and solvation interactions permitting some variability of -sheets at each pH. These results provide atomistic insight into the complex process of molecular recognition detrimental for amyloid growth and pave the way for better understanding of the molecular basis of amyloid diseases

QCD and strongly coupled gauge theories : challenges and perspectives

We highlight the progress, current status, and open challenges of QCD-driven physics, in theory and in experiment. We discuss how the strong interaction is intimately connected to a broad sweep of physical problems, in settings ranging from astrophysics and cosmology to strongly coupled, complex systems in particle and condensed-matter physics, as well as to searches for physics beyond the Standard Model. We also discuss how success in describing the strong interaction impacts other fields, and, in turn, how such subjects can impact studies of the strong interaction. In the course of the work we offer a perspective on the many research streams which flow into and out of QCD, as well as a vision for future developments.Peer reviewe

Iron Behaving Badly: Inappropriate Iron Chelation as a Major Contributor to the Aetiology of Vascular and Other Progressive Inflammatory and Degenerative Diseases

The production of peroxide and superoxide is an inevitable consequence of aerobic metabolism, and while these particular "reactive oxygen species" (ROSs) can exhibit a number of biological effects, they are not of themselves excessively reactive and thus they are not especially damaging at physiological concentrations. However, their reactions with poorly liganded iron species can lead to the catalytic production of the very reactive and dangerous hydroxyl radical, which is exceptionally damaging, and a major cause of chronic inflammation. We review the considerable and wide-ranging evidence for the involvement of this combination of (su)peroxide and poorly liganded iron in a large number of physiological and indeed pathological processes and inflammatory disorders, especially those involving the progressive degradation of cellular and organismal performance. These diseases share a great many similarities and thus might be considered to have a common cause (i.e. iron-catalysed free radical and especially hydroxyl radical generation). The studies reviewed include those focused on a series of cardiovascular, metabolic and neurological diseases, where iron can be found at the sites of plaques and lesions, as well as studies showing the significance of iron to aging and longevity. The effective chelation of iron by natural or synthetic ligands is thus of major physiological (and potentially therapeutic) importance. As systems properties, we need to recognise that physiological observables have multiple molecular causes, and studying them in isolation leads to inconsistent patterns of apparent causality when it is the simultaneous combination of multiple factors that is responsible. This explains, for instance, the decidedly mixed effects of antioxidants that have been observed, etc...Comment: 159 pages, including 9 Figs and 2184 reference