Frog foams and natural protein surfactants

Foams and surfactants are relatively rare in biology because of their potential to harm cell membranes and other delicate tissues. However, in recent work we have identified and characterized a number of natural surfactant proteins found in the foam nests of tropical frogs and other unusual sources. These proteins, and their associated foams, are relatively stable and bio-compatible, but with intriguing molecular structures that reveal a new class of surfactant activity. Here we review the structures and functional mechanisms of some of these proteins as revealed by experiments involving a range of biophysical and biochemical techniques, with additional mechanistic support coming from more recent site-directed mutagenesis studies

Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2

C60 fullerene is not soluble in water and dispersion usually requires organic solvents, sonication or vigorous mechanical mixing. However, we show here that mixing of pristine C60 in water with natural surfactant proteins latherin and ranaspumin-2 (Rsn-2) at low concentrations yields stable aqueous dispersions with spectroscopic properties similar to those previously obtained by more vigorous methods. Particle sizes are significantly smaller than those achieved by mechanical dispersion alone, and concentrations are compatible with clusters approximating 1:1 protein:C60 stoichiometry. These proteins can also be adsorbed onto more intractable carbon nanotubes. This promises to be a convenient way to interface a range of hydrophobic nanoparticles and related materials with biological macromolecules, with potential to exploit the versatility of recombinant protein engineering in the development of nano-bio interface devices. It also has potential consequences for toxicological aspects of these and similar nanoparticles

Hydrophobic Ligand Binding by Zn-α_2-glycoprotein, a Soluble Fat-depleting Factor Related to Major Histocompatibility Complex Proteins

Zn-alpha2-glycoprotein (ZAG) is a member of the major histocompatibility complex (MHC) class I family of proteins and is identical in amino acid sequence to a tumor-derived lipid-mobilizing factor associated with cachexia in cancer patients. ZAG is present in plasma and other body fluids, and its natural function, like leptin's, probably lies in lipid store homeostasis. X-ray crystallography has revealed an open groove between the helices of ZAG's alpha1 and alpha2 domains, containing an unidentified small ligand in a position similar to that of peptides in MHC proteins (Sanchez, L. M., Chirino, A. J., and Bjorkman, P. J. (1999) Science 283, 1914-1919). Here we show, using serum-derived and bacterial recombinant protein, that ZAG binds the fluorophore-tagged fatty acid 11-(dansylamino)undecanoic acid (DAUDA) and, by competition, natural fatty acids such as arachidonic, linolenic, eicosapentaenoic, and docosahexaenoic acids. Other MHC class I-related proteins (FcRn, HFE, HLA-Cw*0702) showed no such evidence of binding. Fluorescence and isothermal calorimetry analysis showed that ZAG binds DAUDA with Kd in the micromolar range, and differential scanning calorimetry showed that ligand binding increases the thermal stability of the protein. Addition of fatty acids to ZAG alters its intrinsic (tryptophan) fluorescence emission spectrum, providing a strong indication that ligand binds in the expected position close to a cluster of exposed tryptophan side chains in the groove. This study therefore shows that ZAG binds small hydrophobic ligands, that the natural ligand may be a polyunsaturated fatty acid, and provides a fluorescence-based method for investigating ZAG-ligand interactions

Resonance assignments for latherin, a natural surfactant protein from horse sweat

Latherin is an intrinsically surfactant protein of ~23 kDa found in the sweat and saliva of horses. Its function is probably to enhance the translocation of sweat water from the skin to the surface of the pelt for evaporative cooling. Its role in saliva may be to enhance the wetting, softening and maceration of the dry, fibrous food for which equines are adapted. Latherin is unusual in its relatively high content of aliphatic amino acids (~25 % leucines) that might contribute to its surfactant properties. Latherin is related to the palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNCs) of mammals, at least one of which is now known to exhibit similar surfactant activity to latherin. No structures of any PLUNC protein are currently available. 15N,13C-labelled recombinant latherin was produced in Escherichia coli, and essentially all of the resonances were assigned despite the signal overlap due to the preponderance of leucines. The most notable exceptions include a number of residues located in an apparently dynamic loop region between residues 145 and 154. The assignments have been deposited with BMRB accession number 19067

Star Of The East : \b Melody, Star Of The Sea

https://digitalcommons.library.umaine.edu/mmb-vp/2523/thumbnail.jp

A generalization of a theorem by Cheo and Yien concerning digital sums

For a non-negative integer n, let s(n) denote the digital sum of n. Cheo and Yien proved that for a positive integer x, the sum of the terms of the sequence{s(n):n=0,1,2,…,(x−1)}is (4.5)xlogx+0(x). In this paper we let k be a positive integer and determine that the sum of the sequence{s(kn):n=0,1,2,…,(x−1)}is also (4.5)xlogx+0(x). The constant implicit in the big-oh notation is dependent on k

The structure of latherin, a surfactant allergen protein from horse sweat and saliva

Latherin is a highly surface-active allergen protein found in the sweat and saliva of horses and other equids. Its surfactant activity is intrinsic to the protein in its native form, and is manifest without associated lipids or glycosylation. Latherin probably functions as a wetting agent in evaporative cooling in horses, but it may also assist in mastication of fibrous food as well as inhibition of microbial biofilms. It is a member of the PLUNC family of proteins abundant in the oral cavity and saliva of mammals, one of which has also been shown to be a surfactant and capable of disrupting microbial biofilms. How these proteins work as surfactants while remaining soluble and cell membrane-compatible is not known. Nor have their structures previously been reported. We have used protein nuclear magnetic resonance spectroscopy to determine the conformation and dynamics of latherin in aqueous solution. The protein is a monomer in solution with a slightly curved cylindrical structure exhibiting a ‘super-roll’ motif comprising a four-stranded anti-parallel β-sheet and two opposing α-helices which twist along the long axis of the cylinder. One end of the molecule has prominent, flexible loops that contain a number of apolar amino acid side chains. This, together with previous biophysical observations, leads us to a plausible mechanism for surfactant activity in which the molecule is first localized to the non-polar interface via these loops, and then unfolds and flattens to expose its hydrophobic interior to the air or non-polar surface. Intrinsically surface-active proteins are relatively rare in nature, and this is the first structure of such a protein from mammals to be reported. Both its conformation and proposed method of action are different from other, non-mammalian surfactant proteins investigated so far

Sprint-based exercise and cognitive function in adolescents.

Moderate intensity exercise has been shown to enhance cognition in an adolescent population, yet the effect of high-intensity sprint-based exercise remains unknown and was therefore examined in the present study. Following ethical approval and familiarisation, 44 adolescents (12.6 ± 0.6 y) completed an exercise (E) and resting (R) trial in a counter-balanced, randomised crossover design. The exercise trial comprised of 10 × 10 s running sprints, interspersed by 50 s active recovery (walking). A battery of cognitive function tests (Stroop, Digit Symbol Substitution (DSST) and Corsi blocks tests) were completed 30 min pre-exercise, immediately post-exercise and 45 min post-exercise. Data were analysed using mixed effect models with repeated measures. Response times on the simple level of the Stroop test were significantly quicker 45 min following sprint-based exercise (R: 818 ± 33 ms, E: 772 ± 26 ms; p = 0.027) and response times on the complex level of the Stroop test were quicker immediately following the sprint-based exercise (R: 1095 ± 36 ms, E: 1043 ± 37 ms; p = 0.038), while accuracy was maintained. Sprint-based exercise had no immediate or delayed effects on the number of items recalled on the Corsi blocks test (p = 0.289) or substitutions made during the DSST (p = 0.689). The effect of high intensity sprint-based exercise on adolescents' cognitive function was dependant on the component of cognitive function examined. Executive function was enhanced following exercise, demonstrated by improved response times on the Stroop test, whilst visuo-spatial memory and general psycho-motor speed were unaffected. These data support the inclusion of high-intensity sprint-based exercise for adolescents during the school day to enhance cognition

Detrimental Tears

For our museum we chose to design it as a walkthrough of a ship used during the Transatlantic trade. Through research we were able to understand how slaves on the ship were treated. We were able to understand that slaves were confined to small spaces while linked together with others during voyages. With this we were able to gather ideas on the layout of our museum. First we chose to put a set of metal chains in the museum to give a sense of how slaves had to be transported. As you walk through you will see what it was like for a slave to be living on the ship. In part of the museum we will have small boxes where someone can sit down and get a feel of how slaves were confined to space while aboard the ship. While sitting there will be a pair of headphones to put on so you will be able to hear the sound of the ocean and other voices.https://csuepress.columbusstate.edu/historyfrombelow/1010/thumbnail.jp