Viruses, attachment probabilities

Indeed, the polymeric interface seems to be highly diffuse and hydrophilic because copolymers of N-vinylpyrrolidone and N- (2-hydroxyethyl) acrylamide are readily soluble in water [53]. Besides, aminopropyl-glass adsorbs the acryloyl chloride copolymer so that only 10% of its active functions become amidated. The rest is located on the loops and tails of the attached macromolecules [51]. Thus the steric repulsion of the bonded phase is a probable reason for the high inertness of the packing towards viruses. 

Carbohydrates attract water molecules, which is probably why they are to be found on the outside of cell membranes, but compatibility with water is only a minor part of what they do. Some carbohydrates are vital for passing subtle messages between cells. Sometimes the carbohydrates are attached to proteins which are also to be found on the surfaces of cells and these carbohydrates are there to protect the proteins from attack by enzymes. Essential though they are, carbohydrates can be exploited to attack cells and they are the route by which viruses and toxins gain access. 

Fusion reactions of viruses are mediated by short peptides that fall into two main groups one dependent on a shift to low pH and the other pH-independent [108]. Initial interests here have focused on peptides involved in pH-dependent fusion because of their potential for application in environmentally sensitive, and therefore controllable, model systems. Of the pH-dependent viruses (influenza virus, the vesicular stomatitis virus, the Semliki forest virus and mouse mammary tumor virus [108]), influenza hemagglutinin (HA) is probably the most studied [4]. HA alone is enough to facilitate the fusion of the influenza virus with the host membrane [102,107]. Through the involvement of at least three subunits, it mediates both the initial attachment of the virus to receptors that contain sialic acid [94] and its fusion with the endosomal membrane [57,58]. 

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