PubMed · 5988109
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M G Shtol'ts, L K Shtamm, N P Bedniagina, A K Shtol'ts. 1966. [Erythromycin polymorphism].. https://pubmed.ncbi.nlm.nih.gov/5988109/
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Understanding the mechanism for sucrose-induced protein stabilization is important in many diverse fields, ranging from biochemistry and environmental physiology to pharmaceutical science. Timasheff and Lee [Lee, J. C. & Timasheff, S. N. (1981) J. Biol. Chem. 256, 7193-7201] have established that thermodynamic stabilization of proteins by sucrose is due to preferential exclusion of the sugar from the protein's surface, which increases protein chemical potential. The current study measures the preferential exclusion of 1 M sucrose from a protein drug, recombinant interleukin 1 receptor antagonist (rhIL-1ra). It is proposed that the degree of preferential exclusion and increase in chemical potential are directly proportional to the protein surface area and that, hence, the system will favor the protein state with the smallest surface area. This mechanism explains the observed sucrose-induced restriction of rhIL-1ra conformational fluctuations, which were studied by hydrogen-deuterium exchange and cysteine reactivity measurements. Furthermore, infrared spectroscopy of rhlL-1ra suggested that a more ordered native conformation is induced by sucrose. Electron paramagnetic resonance spectroscopy demonstrated that in the presence of sucrose, spin-labeled cysteine 116 becomes more buried in the protein's interior and that the hydrodynamic diameter of the protein is reduced. The preferential exclusion of sucrose from the protein and the resulting shift in the equilibrium between protein states toward the most compact conformation account for sucrose-induced effects on rhIL-1ra.
A 1000 base pair (bp) model supercoiled DNA is simulated using spherical screened Coulomb interactions between subunits on one hand and equivalent hard-cylinder interactions on the other. The amplitudes, or effective charges, of the spherical screened Coulomb electrostatic potentials are chosen so that the electrostatic potential surrounding the middle of a linear array of 2001 subunits (31.8 A diameter) closely matches the solution of the nonlinear Poisson-Boltzmann equation for a cylinder with 12 A radius and the full linear charge density of DNA at all distances beyond the 24 A hard-core diameter. This superposition of spherical screened Coulomb potentials is practically identical to the particular solution of the cylindrical linearized Poisson-Boltzmann equation that matches the solution of the nonlinear Poisson-Boltzmann equation at large distances. The interaction energy between subunits is reckoned from the effective charges according to the standard DLVO expression. The equivalent hard-cylinder diameter is chosen following Stigter's protocol for matching second virial coefficients, but for the full linear charge density of DNA. The electrostatic persistence length of the model with screened Coulomb interactions is extremely sensitive to the (arbitrarily) chosen subunit length at the higher salt concentrations. The persistence length of the hard-cylinder model is adjusted to match that of the screened Coulomb model for each ionic condition. Simulations for a superhelix density sigma = -0.05 using a spherical screened Coulomb interaction plus a 24 A hard-cylinder core (SCPHC) potential indicate that the radius of gyration of this 1000 bp DNA actually undergoes a slight increase as the NaCl concentration is raised from 0.01 to 1.0M. Thus, merely softening the potential from hard-cylinder to screened Coulomb form does not produce a large decrease in radius of gyration with increasing NaCl concentration for DNAs of this size. Radii of gyration, static structure factors, and diffusion coefficients obtained using the equivalent hard-cylinder (EHC) potential agree well with those obtained using the SCPHC potential in 1.0M NaCl, but in 0.1M NaCl the agreement is not as good, and in 0.01M NaCl the agreement is definitely unsatisfactory. These conclusions differ in significant respects from those obtained in previous studies.
The pulsating bubble surfactometer has been commonly used to measure the minimum surface tension of lung surfactant. The complexity of the original transinterface pressure tracings and its possible physiological meanings remain undefined. In the present study, we compared surface properties between calf lung surfactant extract (CLSE) and Tween 20, a nonionic surfactant, with the pulsating bubble surfactometer. A synchronized change between transinterface pressure (P) and bubble radius (R) was observed when CLSE was tested. Mathematical analysis and computer simulation indicate that this is due to the extremely potent surface tension lowering and adjusting abilities, which allows the surface tension to decrease towards zero at the end of compression and increase towards a high surface tension during re-expansion. In contrast, a time delay between P and R was observed when Tween 20 was assessed. Surface tension adjusting ability was shown only at concentrations below or around the critical micelle concentration (cmc) of Tween 20. Surface tension became unchangeable when concentrations were further increased, suggesting amphipathic molecules were saturated on the interface. The synchronization of transinterface pressure, alveolar radius and surface tension may play an important role in maintaining the pulmonary compliance in vivo. This unique feature, observed at concentrations several orders above the cmc of phospholipids, suggests that the structure of lung surfactant at the air-liquid interface differs from that of Tween 20, a monolayer of free amphipathic molecules.