scholarly journals Erratum: Corrigendum: A polyalanine peptide derived from polar fish with anti-infectious activities

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Marlon H. Cardoso ◽  
Suzana M. Ribeiro ◽  
Diego O. Nolasco ◽  
César de la Fuente-Núñez ◽  
Mário R. Felício ◽  
...  
Keyword(s):  
Polar Fish

Intracellular oxygen diffusion: the roles of myoglobin and lipid at cold body temperature.

1998 ◽  
Vol 201 (8) ◽  
pp. 1119-1128 ◽  
Author(s):  
B D Sidell
Keyword(s):  
Body Temperature ◽  
Fish Species ◽  
Oxygen Diffusion ◽  
Mechanical Performance ◽  
Muscle Cells ◽  
Cold Temperature ◽  
Oxygen Binding ◽  
Mitochondrial Density ◽  
Polar Fish ◽  
The Mean

Cold temperature can constrain the rate of oxygen movement through muscle cells of ectothermic animals because the kinetic energy of the solvent-solute system decreases and the viscosity of the aqueous cytoplasm increases during cooling within the physiological range of body temperatures. These factors affect the movement of both dissolved oxygen and oxymyoglobin, the two predominant routes of intracellular oxygen diffusion in vertebrate oxidative muscles. In addition, reductions in temperature have been shown to increase the affinity of myoglobin for oxygen and to slow the rate of Mb O2-dissociation, compromising the ability of this oxygen-binding protein to facilitate intracellular oxygen diffusion. Experiments with both seasonally cold-bodied fishes and polar fish species suggest that several factors combine to overcome these limitations in delivery of oxygen from the blood to the mitochondria. First, reductions in body temperature induce increases in mitochondrial density of oxidative muscle cells, reducing the mean diffusional pathlength for oxygen between capillaries and mitochondria. Second, cold body temperature in both temperate-zone and polar fishes is frequently correlated with a high content of neutral lipid in oxidative muscles, providing an enhanced diffusional pathway for oxygen through the tissue. Third, recent data indicate that myoglobins from fish species bind and release oxygen more rapidly at cold temperature than do those from mammals. Data from both oxidative skeletal muscle and cardiac muscle of fishes suggest that these factors in various combinations contribute to enhance the aerobically supported mechanical performance of the tissues at cold cellular temperatures.

The evolution of thermal adaptation in polar fish

Gene ◽  
2006 ◽  
Vol 385 ◽  
pp. 137-145 ◽  
Author(s):  
Cinzia Verde ◽  
Elio Parisi ◽  
Guido di Prisco
Keyword(s):  
Thermal Adaptation ◽  
Polar Fish

“Antifreeze” Glycoproteins from Polar Fish

ChemInform ◽  
2003 ◽  
Vol 34 (38) ◽  
Author(s):  
Margaret M. Harding ◽  
Pia I. Anderberg ◽  
A. D. J. Haymet
Keyword(s):  
Antifreeze Glycoproteins ◽  
Polar Fish

scholarly journals A polyalanine peptide derived from polar fish with anti-infectious activities

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Marlon H. Cardoso ◽  
Suzana M. Ribeiro ◽  
Diego O. Nolasco ◽  
César de la Fuente-Núñez ◽  
Mário R. Felício ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Bacterial Infections ◽  
Rational Design ◽  
Pathogenic Bacteria ◽  
Cd Spectroscopy ◽  
Design Strategies ◽  
Promising Alternative ◽  
Gram Negative ◽  
Bacterial Surface ◽  
Polar Fish

Abstract Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design strategies. Here we focused on the study of Pa-MAP 1.9, a rationally designed AMP derived from the polar fish Pleuronectes americanus. Pa-MAP 1.9 was active against Gram-negative planktonic bacteria and biofilms, without being cytotoxic to mammalian cells. By using AFM, leakage assays, CD spectroscopy and in silico tools, we found that Pa-MAP 1.9 may be acting both on intracellular targets and on the bacterial surface, also being more efficient at interacting with anionic LUVs mimicking Gram-negative bacterial surface, where this peptide adopts α-helical conformations, than cholesterol-enriched LUVs mimicking mammalian cells. Thus, as bacteria present varied physiological features that favor antibiotic-resistance, Pa-MAP 1.9 could be a promising candidate in the development of tools against infections caused by pathogenic bacteria.

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