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Paper   IPM / Biological / 15408
School of Biological Sciences
  Title:   Identification of the Crucial Residues in the Early Insertion of Pardaxin into Different Phospholipid Bilayers
  Author(s): 
1 . Majid Jafari
2 . Faramarz Mehrnejad
3 . Raheleh Aghdami
4 . Naser Chaparzadeh
5 . Zahra Razaghi Moghadam Kashani
6 . Farahnoosh Doostdar
  Status:   Published
  Journal: Journal of Chemical Information and Modeling
  No.:  4
  Vol.:  57
  Year:  2017
  Pages:   929�??941 - DOI: 10.1021/acs.jcim.6b00693
  Supported by:  IPM
  Abstract:
Antimicrobial peptides (AMPs) are part of the innate host defense system, and they are produced by living organisms to defend themselves against infections. Pardaxin is a cationic AMP with antimicrobial and antitumor activities that has potential to be used as a novel antibiotic or for drug delivery in cancer therapy. This peptide acts on the membrane of target cells and can lead to lysis using different mechanisms of action. Here, we conducted 4.5 μs all-atom molecular dynamics (MD) simulations to determine the critical fragments and residues of Pardaxin for early insertion into different lipid bilayers. Our results revealed that the N-terminal domain of the peptide, particularly the Phe 2 and (/or) Phe 3 residues, has a crucial role in early insertion, independent of the type of lipid bilayers.

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