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Title: All-atom molecular dynamics of virus capsids as drug targets

Abstract

Virus capsids are protein shells that package the viral genome. Although their morphology and biological functions can vary markedly, capsids often play critical roles in regulating viral infection pathways. A detailed knowledge of virus capsids, including their dynamic structure, interactions with cellular factors, and the specific roles that they play in the replication cycle, is imperative for the development of antiviral therapeutics. The following Perspective introduces an emerging area of computational biology that focuses on the dynamics of virus capsids and capsid–protein assemblies, with particular emphasis on the effects of small-molecule drug binding on capsid structure, stability, and allosteric pathways. When performed at chemical detail, molecular dynamics simulations can reveal subtle changes in virus capsids induced by drug molecules a fraction of their size. Finally, the current challenges of performing all-atom capsid–drug simulations are discussed, along with an outlook on the applicability of virus capsid simulations to reveal novel drug targets.

Authors:
 [1];  [1];  [1];  [1];  [1]
  1. Univ. of Illinois at Urbana-Champaign, Urbana, IL (United States)
Publication Date:
Research Org.:
Univ. of Illinois at Urbana-Champaign, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1250973
Alternate Identifier(s):
OSTI ID: 1344922
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Journal Article: Published Article
Journal Name:
Journal of Physical Chemistry Letters
Additional Journal Information:
Journal Volume: 7; Journal Issue: 10; Journal ID: ISSN 1948-7185
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Perilla, Juan R., Hadden, Jodi A., Goh, Boon Chong, Mayne, Christopher G., and Schulten, Klaus. All-atom molecular dynamics of virus capsids as drug targets. United States: N. p., 2016. Web. doi:10.1021/acs.jpclett.6b00517.
Perilla, Juan R., Hadden, Jodi A., Goh, Boon Chong, Mayne, Christopher G., & Schulten, Klaus. All-atom molecular dynamics of virus capsids as drug targets. United States. doi:10.1021/acs.jpclett.6b00517.
Perilla, Juan R., Hadden, Jodi A., Goh, Boon Chong, Mayne, Christopher G., and Schulten, Klaus. Fri . "All-atom molecular dynamics of virus capsids as drug targets". United States. doi:10.1021/acs.jpclett.6b00517.
@article{osti_1250973,
title = {All-atom molecular dynamics of virus capsids as drug targets},
author = {Perilla, Juan R. and Hadden, Jodi A. and Goh, Boon Chong and Mayne, Christopher G. and Schulten, Klaus},
abstractNote = {Virus capsids are protein shells that package the viral genome. Although their morphology and biological functions can vary markedly, capsids often play critical roles in regulating viral infection pathways. A detailed knowledge of virus capsids, including their dynamic structure, interactions with cellular factors, and the specific roles that they play in the replication cycle, is imperative for the development of antiviral therapeutics. The following Perspective introduces an emerging area of computational biology that focuses on the dynamics of virus capsids and capsid–protein assemblies, with particular emphasis on the effects of small-molecule drug binding on capsid structure, stability, and allosteric pathways. When performed at chemical detail, molecular dynamics simulations can reveal subtle changes in virus capsids induced by drug molecules a fraction of their size. Finally, the current challenges of performing all-atom capsid–drug simulations are discussed, along with an outlook on the applicability of virus capsid simulations to reveal novel drug targets.},
doi = {10.1021/acs.jpclett.6b00517},
journal = {Journal of Physical Chemistry Letters},
number = 10,
volume = 7,
place = {United States},
year = {Fri Apr 29 00:00:00 EDT 2016},
month = {Fri Apr 29 00:00:00 EDT 2016}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1021/acs.jpclett.6b00517

Citation Metrics:
Cited by: 14 works
Citation information provided by
Web of Science

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