<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bavikar, Sudhir N.</style></author><author><style face="normal" font="default" size="100%">Salunke, Deepak B.</style></author><author><style face="normal" font="default" size="100%">Hazra, Braja G.</style></author><author><style face="normal" font="default" size="100%">Pore, Vandana S.</style></author><author><style face="normal" font="default" size="100%">Dodd, Robert H.</style></author><author><style face="normal" font="default" size="100%">Thierry, Josiane</style></author><author><style face="normal" font="default" size="100%">Shirazi, Fazal</style></author><author><style face="normal" font="default" size="100%">Deshpande, Mukund V.</style></author><author><style face="normal" font="default" size="100%">Kadreppa, Sreenath</style></author><author><style face="normal" font="default" size="100%">Chattopadhyay, Samit</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synthesis of chimeric tetrapeptide-linked cholic acid derivatives: impending synergistic agents</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Antimicrobial activity</style></keyword><keyword><style  face="normal" font="default" size="100%">Cholic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytotoxicity</style></keyword><keyword><style  face="normal" font="default" size="100%">Synergism</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetrapeptide</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">20</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">5512-5517</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Tetrapeptides derived from glycine and beta-alanine were hooked at the C-3 beta position of the modified cholic acid to realize novel linear tetrapeptide-linked cholic acid derivatives. All the synthesized compounds were tested against a wide variety of microorganisms (Gram-negative bacteria, Gram-positive bacteria and fungi) and their cytotoxicity was evaluated against human embryonic kidney (HEK293) and human mammary adenocarcinoma (MCF-7) cell lines. While relatively inactive by themselves, these compounds interact synergistically with antibiotics such as fluconazole and erythromycin to inhibit growth of fungi and bacteria, respectively, at 1-24 mu g/mL. The synergistic effect shown by our novel compounds is due to their inherent amphiphilicity. The fractional inhibitory concentrations reported are comparable to those reported for Polymyxin B derivatives. (c) 2008 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">20</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.486</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Swaroop, Pandrangi Siva</style></author><author><style face="normal" font="default" size="100%">Tripathy, Sibanarayan</style></author><author><style face="normal" font="default" size="100%">Jachak, Gorakhnath R.</style></author><author><style face="normal" font="default" size="100%">Reddy, D. Srinivasa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Efforts towards the synthesis of microsporin B: ready access to both the enantiomers of the key amino acid fragment</style></title><secondary-title><style face="normal" font="default" size="100%">Tetrahedron Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cross metathesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzymatic resolution</style></keyword><keyword><style  face="normal" font="default" size="100%">HDAC inhibitor</style></keyword><keyword><style  face="normal" font="default" size="100%">Microsporin</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetrapeptide</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">34</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">55</style></volume><pages><style face="normal" font="default" size="100%">4777-4779</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Both the isomers methyl-(2S,8R)-2-((tert-butoxycarbonyl)amino)-8-hydroxydecanoate and methyl-(2S,8S)-2-((tert-butoxycarbonyl)amino)-8-hydroxydecanoate of an unusual amino acid residue and the key fragment of microsporin B are prepared. The key steps include cross metathesis and enzymatic kinetic resolution. In addition, a linear tetrapeptide with desired components towards total synthesis is also reported. (C) 2014 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">34</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;2.68&lt;/p&gt;</style></custom4></record></records></xml>