Exploring the Mechanism of Viral Peptide-Induced Membrane Fusion

  • Gourab Prasad Pattnaik
  • Geetanjali Meher
  • Hirak ChakrabortyEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1112)


Membrane fusion is essential in several cellular processes in the existence of eukaryotic cells such as cellular trafficking, compartmentalization, intercellular communication, sexual reproduction, cell division, and endo- and exocytosis. Membrane fusion proceeds in model membranes as well as biological membranes through the rearrangement of lipids. The stalk hypothesis provides a picture of the general nature of lipid rearrangement based on mechanical properties and phase behavior of water-lipid mesomorphic systems. In spite of extensive research on exploring the mechanism of membrane fusion, a clear molecular understanding of intermediate and pore formation is lacking. In addition, the mechanism by which proteins and peptides reduce the activation energy for stalk and pore formation is not yet clear though there are several propositions on how they catalyze membrane fusion. In this review, we have discussed about various putative functions of fusion peptides by which they reduce activation barrier and thus promote membrane fusion. A careful analysis of the discussed effects of fusion peptides on membranes might open up new possibilities for better understanding of the membrane fusion mechanism.


Membrane fusion Bending energy Void space Membrane curvature Depth-dependent membrane ordering Fusion peptide 



This work was supported by research grants from the University Grants Commission, New Delhi (File No. F.4-5(138-FRP)/2014(BSR)), and Science and Engineering Research Board, Department of Science and Technology (SERB-DST), New Delhi (File No. ECR/2015/000195). H. C. and G. M. thank the University Grants Commission for UGC-Assistant Professor position and UGC-BSR Research Fellowship, respectively. G. P. P. thanks SERB-DST for his project assistantship. We thank the Department of Science and Technology, New Delhi, and UGC for providing instrument facility to the School of Chemistry, Sambalpur University, under the FIST and DRS programs, respectively. We gratefully acknowledge the critical comments and discussions by Dr. S. N. Sahu and the members of Chakraborty group.


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Copyright information

© Springer Nature Singapore Pte Ltd. 2018

Authors and Affiliations

  • Gourab Prasad Pattnaik
    • 1
  • Geetanjali Meher
    • 1
  • Hirak Chakraborty
    • 1
    Email author
  1. 1.School of ChemistrySambalpur UniversityBurlaIndia

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