Morphofunctional correlations in the experimental study of myocardiopathies under the stress of forced restraint. Note 2: The influence of adrenal imbalance

Tests were performed with 70 rats to determine the effects of restraint on the functions and structure of the myocardium under varying conditions of adrenal imbalance. Results showed that in rats with adrenal imbalance, fasting and restraint produced the same biochemical alterations as in the controls. The morphologic alteractions, as well as their electric expression, were more varied and evident in the animals with adrenal imbalance. Persistence of the microscopic and electrocardiographic alterations after 72 hours restraint in the animals subjected to unilateral adrenalectomy suggests chronic evolution of the myocardial lesions. This proves the necessity of intact adrenals for a good adaptability to stress

Fractal intermediates in the self-assembly of silicatein filaments

Silicateins are proteins with catalytic, structure-directing activity that are responsible for silica biosynthesis in certain sponges; they are the constituents of macroscopic protein filaments that are found occluded within the silica needles made by Tethya aurantia. Self-assembly of the silicatein monomers and oligomers is shown to form fibrous structures by a mechanism that is fundamentally different from any previously described filament-assembly process. This assembly proceeds through the formation of diffusion-limited, fractally patterned aggregates on the path to filament formation. The driving force for this self-assembly is suggested to be entropic, mediated by the interaction of hydrophobic patches on the surfaces of the silicatein subunits that are not found on highly homologous congeners that do not form filaments. Our results are consistent with a model in which silicatein monomers associate into oligomers that are stabilized by intermolecular disulfide bonds. These oligomeric units assemble into a fractal network that subsequently condenses and organizes into a filamentous structure. These results represent a potentially general mechanism for protein fiber self-assembly

Switchable peptide surfactants with designed metal binding capacity

By modifying a well-studied peptide sequence, we have designed two biosurfactants with the ability to reversibly and precisely control the stability of foams. Foam stabilization occurs when the peptide forms a cohesive interfacial film cross-linked by metal ions, while foam destabilization occurs when peptide-metal binding is disrupted. The parent sequence is an amphipathic peptide that adsorbs at fluid interfaces, but forms neither cohesive interfacial films nor stable foams at the concentrations tested. Two modified peptide sequences were designed in which internal sites were substituted with metal-binding histidine residues. The first derivative, AM1, contains two histidines and can undergo intermolecular cross-linking by metal at the air-water interface. AM1 forms cohesive interfacial films and stable foams in the presence of Zn(II), Co(II), or Ni(II), but not in the absence of metal ions. The second derivative, AFD4, has four histidine substitutions, and can undergo both intra- and intermolecular cross-linking by metal ions. AFD4 forms stronger interfacial films and more stable foams than AM1 in the presence of the same metal ions, and also undergoes helical structuring in solution in the presence of added metal ions. For both peptides, film formation and foam stabilization can be reversed by acidification of the bulk solution, or addition of a metal chelator

Characterization of peptide-guided polymer assembly at the air/water interface

An organo-soluble, peptide-polymer conjugate that combines poly(n-butyl acrylate) with a beta-sheet-forming peptide is spread at the water surface to investigate peptide-guided self-assembly in a two-dimensional environment. Single layers of the conjugate are studied to gain information on the packing, orientation, and structure of the conjugate molecules using standard monolayer techniques: isotherms, grazing incidence X-ray diffraction (GIXD), and infrared reflection absorption spectroscopy (IRRAS). At all conditions studied, the stabilizing beta-sheet network consists of antiparallel beta-sheets oriented parallel to the air/water interface. The incorporation of temporary switch defects in the peptide segment enables beta-sheet assembly to be triggered at different packing densities. Stable monolayers, with low compressibilities similar to peptide monolayers, form when beta-sheet assembly occurs in monolayers that contain closely packed conjugate molecules. Langmuir-Schaefer transfer of the switched monolayer seeded with 1/1000 part stearic acid results in a transferred monolayer containing ordered domains with 7 nm wide stripes, a width in agreement with the end-to-end distance of the conjugate molecule. In this interfacial system, high packing densities and a hydrophobic seed molecule play an important role in beta-sheet network and structure formation. Both effects likely direct the highly ordered beta-sheet structure because of beta-strand prealignment. Insights gained from self-assembly in this system can be applied to peptide aggregation mechanisms in more complex interfacial environments