Comparative Analysis of the Molecular Adjuvants and Their Binding Efficiency with CR1

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• 作者：B. Saranya ; Shweta Saxena ; K. M. Saravanan…
• 关键词：Molecular adjuvants ; Vaccine development ; Structural analysis ; Docking studies ; Hydrophobic interactions
• 刊名：Interdisciplinary Sciences: Computational Life Sciences
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：8
• 期：1
• 页码：35-40
• 全文大小：477 KB
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• 作者单位：B. Saranya (1)
  Shweta Saxena (2)
  K. M. Saravanan (1)
  H. Shakila (2)
  
  1. Centre of Excellence in Bioinformatics, School of Biotechnology, Madurai Kamaraj University, Madurai, Tamilnadu, 625 021, India
  2. Department of Molecular Microbiology, School of Biotechnology, Madurai Kamaraj University, Madurai, Tamilnadu, 625 021, India
  
• 刊物主题：Computer Appl. in Life Sciences; Computational Biology/Bioinformatics; Statistics for Life Sciences, Medicine, Health Sciences; Theoretical and Computational Chemistry; Theoretical, Mathematical and Computational Physics; Computational Science and Engineering;
• 出版者：International Association of Scientists in the Interdisciplinary Areas
• ISSN：1867-1462

文摘

There are so many obstacles in developing a vaccine or vaccine technology for diseases like cancer and human immunodeficiency virus infection. While developing vaccines that target specific infection, molecular adjuvants are indispensable. These molecular adjuvants act as a vaccine delivery vehicle to the immune system to increase the effectiveness of the specific antigens. In the present work, a computational study has been done on molecular adjuvants like IgGFc, GMCSF and C3d to find out how efficiently they are binding to CR1. Sequence, structure and mutational analysis are performed on the molecular adjuvants to understand the features important for their binding with the receptor. Results obtained from our study indicate that the adjuvant IgGFc complexed with the receptor CR1 has the best binding efficiency, which can be used further to develop better vaccine technologies. Keywords Molecular adjuvants Vaccine development Structural analysis Docking studies Hydrophobic interactions