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The problem of localizing small (relative to wavelength) scatterers by diffractions to enhance their use in identifying small-scale details in a seismic image is extremely important in shallow exploration to identify interesting features such as fractures, caves, and faults. The conventional approach based on seismic reflection is limited in resolution by the Rayleigh criterion. In certain acquisition geometries, such as crosswell surveys aimed at obtaining high-resolution signals, the availability of suitable data sets for effective migration depends on the spatial extent of the available source and receiver data intervals. With the aim of overcoming the resolution limits of seismic reflection, we study the detectability, response, and location of meter- and possibly submeter-dimension carbonate concretions (septaria) in the Boom Clay Formation (potential host rocks for radioactive waste disposal) by diffraction analysis of high-frequency signals. We investigate diffraction wavefields by signal separation, focusing, and high-resolution coherency analysis using the multiple signal classification method and semblance. The investigation is performed for two different surveys in Belgium, a shallow and high-resolution reverse vertical seismic profile (RVSP) and a near-offset crosswell application at Kruibeke and ON-MOL-2 sites, respectively. The data analysis is supported by synthetic wavefield modeling. The multioffset RVSP provides the appropriate geometry to observe and investigate the septaria diffractions from depth and the surface. The crosswell approach, calibrated using synthetic data in the analysis of wavefield patterns in 2D, indicates promising imaging results with field data of a selected diffraction zone in the interwell area.

The crucial role of integrin in pathological processes such as tumor progression and metastasis formation has inspired intense efforts to design novel pharmaceutical agents modulating integrin functions in order to provide new tools for potential therapies. In the past decade, we have investigated the biological proprieties of the chimeric peptide RGDechi, containing a cyclic RGD motif linked to an echistatin C-terminal fragment, able to specifically recognize αvβ3 without cross reacting with αvβ5 and αIIbβ3 integrin. Additionally, we have demonstrated using two RGDechi-derived peptides, called RGDechi1-14 and ψRGDechi, that chemical modifications introduced in the C-terminal part of the peptide alter or abolish the binding to the αvβ3 integrin. Here, to shed light on the structural and dynamical determinants involved in the integrin recognition mechanism, we investigate the effects of the chemical modifications by exploring the conformational space sampled by RGDechi1-14 and ψRGDechi using an integrated natural-abundance NMR/MD approach. Our data demonstrate that the flexibility of the RGD-containing cycle is driven by the echistatin C-terminal region of the RGDechi peptide through a coupling mechanism between the N- and C-terminal regions.