Poly(vinyl alcohol) freeze casts with nano-additives as potential thermal insulators.

Freeze-casting consists of freezing a liquid suspension (aqueous or other), followed by sublimation of the solidified state to the gas state under reduced pressure, and subsequent sintering of the remaining scaffold to consolidate and densify the struts and walls. The structure is very porous with the pores being a replica of the solvent crystals. The technique is rather versatile and the use of a liquid solvent (water most of the time) as a pore forming agent is a strong asset. Freeze-casting has also been developed as a near net shape forming route yielding dense ceramics. In this work we report on porous composite materials synthesized via the ice templating method. Poly(vinyl alcohol) (PVA) is used as matrix and nano-silica (SiO2), nanoclay (NC) and microfibrillated cellulose (MFC) are used as fillers to improve the mechanical stability of the PVA scaffold. We show our results on the porosity and mechanical stability and consider these porous nanocomposites as potential insulation materials with low thermal conductivity and superior mechanical properties.

An adaptable two-lens high-resolution objective for single-site resolved imaging of atoms in optical lattices.

In this paper, we present a high-resolution, simple, and versatile imaging system for single-site resolved imaging of atoms in optical lattices. The system, which relies on an adaptable infinite conjugate two-lens design, has a numerical aperture of 0.52, which can in the ideal case be further extended to 0.57. It is optimized for imaging on the sodium D2-line but allows us to tune the objective's diffraction limited performance between 400 nm and 1000 nm by changing the distance between the two lenses. Furthermore, the objective is designed to be integrated into a typical atomic physics vacuum apparatus where the operating distance can be large (>20 mm) and diffraction limited performance still needs to be achieved when imaging through thick vacuum windows (6 mm to 10 mm). Imaging gold nanoparticles, using a wavelength of 589 nm which corresponds to the D2-line of sodium atoms, we measure diffraction limited performance and a resolution corresponding to an Airy radius of less than 0.7 µm, enabling potential single-site resolution in the commonly used 532 nm optical lattice spacing.

National beef tenderness survey - 2006: Assessment of Warner-Bratzler shear and sensory panel ratings for beef from US retail and foodservice establishments.

Beef from retail and foodservice establishments in 11 US cities was evaluated using Warner-Bratzler shear (WBS) and consumer evaluation panels. Postmortem aging times ranged from 3 to 83d for retail and 7 to 136d for foodservice with mean aging times of 22.6d and 30.1d, respectively. For retail, the three cuts from the round - top round, bottom round, and eye of round - had the highest (P<0.05) WBS values compared to cuts from the chuck, rib, and loin. Top loin steaks had the lowest (P<0.05) WBS value compared to ribeye and top sirloin foodservice steaks. Retail bone-in top loin, top loin, ribeye, T-bone, and porterhouse received the highest (P<0.05) ratings by consumers for overall like and like tenderness. Quality grade had little or no effect on foodservice sensory evaluations. Improvements in round tenderness are needed to increase consumer acceptability.

Retail cutting characteristics for US Choice and US Select beef subprimals.

US Choice (Ch) and US Select (Se) beef subprimals from the rib, chuck, plate, loin, and round were obtained to conduct retail cutting tests. Subprimals were merchandised into bone-in or boneless retail cuts and associated components by experienced retail meat merchandisers. These Se subprimals had less (P<0.05) trimmable fat than their Ch counterparts: ball tip, top sirloin, outside round, inside round, and ribeye. Se inside rounds, outside rounds, eye of rounds, boneless striploins, and ball tips had greater (P<0.05) purge losses than the same cuts from Ch. The only subprimals where grade impacted total saleable yield were the top (inside) rounds (Ch=80.13%, Se=87.34%; P=0.004) and outside rounds cut into roasts, steaks, and cubed steaks (Ch=87.61%, Se=90.28%; P=0.05). Methods to increase retail yields from beef subprimals should consider minimizing purge and increasing cutting efficiencies in addition to reducing fat trim.

Innovative wholesale carcass fabrication and retail cutting to optimize beef value.

Innovations in beef carcass fabrication to improve subprimal yield, retail cut yield, and overall carcass value were evaluated. Alternating sides from 30 beef carcasses were assigned to either an innovative or conventional style of fabrication. The innovative method resulted in greater (P<0.001) total subprimal yield and less (P<0.001) lean trimmings from the forequarter; however, hindquarter total subprimal yield and lean trimmings were not affected (P>0.05) by fabrication style. Value was greater for the innovative forequarter (P<0.001) and hindquarter (P<0.01), and total value was increased by more than US $14 per beef carcass compared to the conventional style. Selected subprimals were evaluated in retail cutting tests. In general, the innovative retail subprimals had yields equal to or greater than the conventional subprimals. Innovative carcass fabrication may allow for greater marketing options for beef cuts to improve carcass value and to offer greater retail merchandizing opportunities.

High voltage electrical stimulation enhances muscle tenderness, increases aging response, and improves muscle color from cabrito carcasses.

Our study examined high and low voltage electrical stimulation and postmortem storage as strategies to improve tenderness and lean color in cabrito carcasses. Boer cross (n=60) kids were assigned to either high (550 V), low (20 V), or no electrical stimulation treatments. No differences in muscle temperature were observed between treatments at any time measured. Muscle pH declined fastest in high voltage treated carcasses. High voltage electrical stimulation slightly increased (P<0.05) b (∗) and a (∗) in the M. gluteus medius and tended to increase L (∗) and b (∗) (P=0.06 and 0.11, respectively) values in the M. longissimus thoracis. Electrical stimulation had no effect on myofibril fragmentation at 1-, 3-, or 14-d postmortem or sarcomere length. High voltage electrical stimulation increased (P<0.05) tenderness at 1- and 3-d postmortem, but not at 14-d postmortem. Aging for 3 d did not affect tenderness regardless of stimulation treatment, but aging time for 14 d improved (P<0.05) tenderness. These data indicate that high voltage electrical stimulation and 14 d aging were effective in improving the tenderness of meat from cabrito carcasses.

Identification of important amino acid residues of the Na+-Ca2+ exchanger inhibitory peptide, XIP.

The Na+-Ca2+ exchanger plays an important role in cardiac contractility by moving Ca2+ across the plasma membrane during excitation-contraction coupling. A 20 amino acid peptide, XIP, synthesized to mimic a region of the exchanger, inhibits exchange activity. We identify here amino acid residues important for inhibitory function. Effects of modified peptides on Na+-Ca2+ exchange activity were determined. Exchange activity was assessed as 45Ca2+ uptake into Na+-loaded cardiac sarcolemmal vesicles. We find that the entire length of XIP is important for maximal potency, though the major inhibitory components are between residues 5 and 16. Basic and aromatic residues are most important for the inhibitory function of XIP. Substitutions of arginine 12 and arginine 14 with alanine or glutamine dramatically decrease the potency of XIP, suggesting that these residues play a key role in possible charge-charge interactions. Substitutions of other basic residues with alanines or glutamines had less effect on the potency of XIP. All aromatic residues participate in binding with the exchanger, probably via hydrophobic interactions as indicated by tryptophan fluorescence. A tyrosine is required at position 6 for maximal inhibition and phenylalanine 5 and tyrosine 8 can only be replaced by other aromatic residues. Tyrosine 10 and tyrosine 13 can be replaced with other bulky residues. A specific conformation of XIP, with structural constrains provided by all parts of the molecule, is required for optimal inhibitory function.

Interaction of a neutral endopeptidase inhibitor with an ANP-C receptor ligand in anesthetized dogs.

Inhibition of important degradative pathways of atrial natriuretic peptide (ANP) in vivo could be a valuable therapeutic tool for regulating endogenous levels of ANP. The aim was to investigate the in vivo effects of both blockade of atrial natriuretic peptide clearance receptor and inhibition of neutral endopeptidase 24.11, an enzyme shown to be involved in ANP breakdown. Therefore, we infused a specific neutral endopeptidase inhibitor ((S)-thiorphan) and an ANP-C receptor ligand (AP 811) alone or in combination into anaesthetized beagle dogs. Compared with vehicle controls, coadministration of (S)-thiorphan and AP 811 (100 micrograms/kg/min and 10 micrograms/kg/min, resp.) had greater effects on endocrine and renal parameters than administration of either substance alone. Coadministration of both compounds increased urinary excretion of volume and sodium, cGMP and ANP. We found also increased plasma cGMP, plasma ANP and decreased plasma renin activity. No effects were observed with respect to blood pressure, left ventricular pressure or heart rate during the infusion period of 2 h. We conclude from these investigations, that blocking both degrading pathways of ANP with the ANP-C receptor ligand AP 811 and the neutral endopeptidase inhibitor (S)-thiorphan is more effective than inhibition of either system alone. Such a combination might therefore be a useful therapeutic tool in cardiovascular diseases.

Autoradiographic localization of [125I]-C-ANP compared to [125I]-ANP in rat tissue.

Whole-body autoradiography demonstrated the different distribution of [125I]-C-ANP and [125I]-ANP to rat tissues. Highest enrichment of radioactivity of both labelled peptides was found in the kidney. In some organs we found remarkable differences between [125I]-ANP and [125I]-C-ANP. In the kidney cortex, especially in the glomeruli, as well as in the endocardium, the zona glomerulosa and the medulla of the adrenal gland, where high levels of radioactivity after [125I]-ANP administration were detected, no or just few radioactivity was found after administration of [125I]-C-ANP. On the other hand in the kidney papilla and the outer subcortical medulla, characteristic blackening was found after [125I]-C-ANP administration. Those differences might be important for the understanding of pharmacological actions of ANP analogues.

Structural fluctuations of a helical polypeptide traversing a lipid bilayer.

Time-resolved fluorescence anisotropy (FA) measurements are reported for five helical bilayer-spanning henicosapeptides, each containing one tryptophan at sequence position 1, 6, 11, 16, or 21. The FA decay reflects two molecular processes in all cases: local internal fluctuations of the tryptophan side chain with a relaxation time of 200-500 ps, and motions of the whole polypeptide molecule with a relaxation time of 9-10 ns. The amplitudes of the fast fluctuation are largest at the helix ends and decrease toward the center of the helix. A similar observation was made for the helical polypeptides dissolved in organic solvents showing that the mobility gradient along the polypeptide sequence is an inherent property of the polypeptide helix and not due to the lipid bilayer. However, the amplitudes of the fast fluctuations can be modulated by the physical state of the lipid bilayer. With decreasing temperature, the internal mobility of the tryptophan in all positions decreases with an abrupt change at the lipid-phase transition. Concomitant molecular dynamics calculations indicate a correlation between the fast FA decay and conformational fluctuations within the helix. According to the simulation, the conformation of the polypeptide is on average predominantly helical, but actually the molecule can fluctuate between a variety of different substructures. The conformational fluctuations are largest at the helix ends and provide the free space required for rotation of the indole ring around the tryptophan side chain bonds.

Depth-dependent fluorescent quenching of a tryptophan residue located at defined positions on a rigid 21-peptide helix in liposomes.

Five lipophilic 21-peptide analogs of the potential-dependent pore-former, alamethicin, were synthesized bearing tryptophan residues at the position 1, 6, 11, 16 and 21 on a long, conformationally rigid, alpha-helix. The alpha-helical conformation was induced and stabilized using the sequential oligomers (Ala-Aib-Ala-Aib-Ala)n as analyzed by CD and NMR. The partitioning of the N-t-butoxycarbonyl 21-peptide methyl esters and the N-terminally deprotected alpha-helices was followed by fluorescence enhancement in phospholipid bilayer vesicles. Quenching experiments were performed by titrating with n-doxyl stearic acids bearing the nitroxide label at positions 5, 7, 10, 12 and 16. This well-defined system revealed that the N- and C-terminal tryptophan residues become situated in the hydrophilic region. Tryptophan at position 11 was found in the lipophilic core, whereas the tryptophan at positions 6 and 16 were localized at intermediate depths of the lipid membrane. Therefore, the helices span the lipid bilayer with their long axis normal to the membrane surface.

Voltage-dependent channel formation by rods of helical polypeptides.

The voltage-dependence of channel formation by alamethicin and it natural analogues can be described by a dipole flip-flop gating model, based on electric field-induced transbilayer orientational movements of single molecules. These field-induced changes in orientation result from the large permanent dipole moment of alamethicin, which adopts alpha-helical conformation in hydrophobic medium. It was, therefore, supposed that the only structural requirement for voltage-dependent formation of alamethicin-type channels might be a rigid lipophilic helical segment of minimum length. In order to test this hypothesis we synthesized a family of lipophilic polypeptides--Boc-(Ala-Aib-Ala-Aib-Ala)n-OMe, n = 1-4--which adopt alpha-helical conformation for n = 2-4 and studied their interaction with planar lipid bilayers. Surprisingly, despite their large difference in chain length, all four polypeptides showed quantitatively similar behavior. At low field strength of the membrane electric field these polypeptides induce a significant, almost voltage-independent increase of the bilayer conductivity. At high field strength, however, a strongly voltage-dependent conductance increase occurs similar to that observed with alamethicin. It results from the opening of a multitude of ion translocating channels within the membrane phase. The steady-state voltage-dependent conductance depends on the 8th-9th power of polypeptide concentration and involves the transfer of 4-5 formal elementary charges. From the power dependences on polypeptide concentration and applied voltage of the time constants in voltage-jump current-relaxation experiments, it is concluded that channels could be formed from preexisting dodecamer aggregates by the simultaneous reorientation of six formal elementary charges. Channels exhibit large conductance values of several nS, which become larger towards shorter polypeptide chain length. A mean channel diameter of 19 A is estimated corresponding roughly to the lumen diameter of a barrel comprised of 10 alpha-helical staves. Similar to experiments with the N-terminal Boc-derivative of alamethicin we did not observe the burst sequence of nonintegral conductance steps typical of natural (N-terminal Ac-Aib)-alamethicin. Saturation in current/voltage curves as well as current inactivation in voltage-jump current-relaxation experiments are found. This may be understood by assuming that channels are generated as dodecamers but, while reaching the steady state, reduce their size to that of an octamer or nonamer. We conclude that the overall behavior of these synthetic polypeptides is very similar to that of alamethicin.(ABSTRACT TRUNCATED AT 400 WORDS)

Molecular shape and dipole moment of alamethicin-like synthetic peptides.

The peptides Boc-(L-Ala-Aib-L-Ala-Aib-L-Ala)n-OMe, with n = 2 (P10) and n = 4 (P20), have been synthesized as purely hydrophobic models of the antibiotic alamethicin, which is known to be a voltage-dependent pore former in membranes and is apparently alpha-helical in lipophilic media. These peptides were investigated in 1-octanol, a solvent which resembles the membrane environment. From dielectric dispersion studies quantitative information on the molecular shape and dipole moments could be derived. Further independent data concerning conformation and extent of aggregation of the peptides were obtained by circular dichroism and ultracentrifuge measurements. The results suggest that the peptides assume the form of elongated particles having a significant amount of ordered secondary structure and carrying a dipole parallel to the long axis. Apparently the monomeric peptide molecules undergo, to some extent, a head-to-tail aggregation which is slightly enhanced at lower temperatures. Based on the high-frequency parts of the dielectric dispersion curves the lengths, diameters, and dipole moments of the monomer particles have been determined as 22.5A, 10A, 36 D (P10) and 28.5A, 12A, 64D (P20).