Terminology AP is a sudden inflammation of the pancreas. It can have severe complications and high mortality despite treatment. While mild cases are often successfully treated with conservative measures and aggressive intravenous fluid rehydration, severe cases may require admission to the intensive care unit or even surgery to deal with complications of the disease process. Peer 17-AAG solubility review The role of SSM is mainly deleterious and also anti inflammatory and antimicrobial, what in literature has support about the protective effect of SSM in AP. The study is designed reasonably and the methods and the results seem mostly proper to show interesting protective effect of SSM on AP. Footnotes Supported by National Research Foundation of Korea grant funded by the Korea government MEST, No.

2010-0029498 P- Reviewers Sumi S, Kumar A S- Editor Jiang L L- Editor A E- Editor Xiong L
Fusogenic viral envelope glycoproteins are multimeric proteins that facilitate the fusion of viral and target cell lipid membranes during the initiation of infection. The membrane fusion process is energetically favorable and essentially irreversible, but has a considerable kinetic energy barrier [1]. These proteins allow rapid membrane fusion by drawing the opposing membranes together and either stabilizing or providing the activation energy to surmount the transition state [1], [2]. In this way, they behave in many aspects like a fusion catalyst. Because they effect a macromolecular process that involves large scale conformational changes in the substrate membranes and the proteins themselves, these proteins possess multiple interacting surfaces that could be targeted by inhibitors [3].

There are several distinct types of viral fusion proteins, including the class I, primarily alpha helical proteins (such as HIV TM and influenza HA), the class II, primarily beta sheet proteins (such as the flavivirus E and alphavirus E1), and mixed helix/sheet proteins (including herpes virus gB and rhabdovirus G) [3], [4]. To date, most progress with viral fusion protein inhibitors has focused on class I alpha helical proteins. The HIV TM protein provides an excellent example of targeting distinct, interacting surfaces for inhibition. The HIV TM functions as a homotrimer with each monomer contributing two alpha helical regions that interact to form a post-fusion six-helix bundle.

Inhibition of the formation of this six-helix bundle can be accomplished by exogenous peptides mimicking either of the two reciprocally interacting helices [5]�C[7]. Only a few examples of viral entry inhibitors with activity against the primarily beta sheet envelope proteins (E) from flaviviruses have been described [8]�C[10]. However, few of these have taken advantage of the available GSK-3 crystal structures of flavivirus E proteins, including both pre-fusion and post-fusion forms [11]�C[22].