PMID- 25818122
OWN - NLM
STAT- MEDLINE
DCOM- 20151104
LR  - 20181113
IS  - 1559-4106 (Electronic)
IS  - 1934-8630 (Print)
IS  - 1559-4106 (Linking)
VI  - 10
IP  - 2
DP  - 2015 Jun 27
TI  - Parameterization of an interfacial force field for accurate representation of 
      peptide adsorption free energy on high-density polyethylene.
PG  - 021002
LID - 10.1116/1.4916361 [doi]
LID - 021002
AB  - Interfacial force field (IFF) parameters for use with the CHARMM force field have 
      been developed for interactions between peptides and high-density polyethylene 
      (HDPE). Parameterization of the IFF was performed to achieve agreement between 
      experimental and calculated adsorption free energies of small TGTG-X-GTGT 
      host-guest peptides (T = threonine, G = glycine, and X = variable amino-acid 
      residue) on HDPE, with +/-0.5 kcal/mol agreement. This IFF parameter set consists 
      of tuned nonbonded parameters (i.e., partial charges and Lennard-Jones 
      parameters) for use with an in-house-modified CHARMM molecular dynamic program 
      that enables the use of an independent set of force field parameters to control 
      molecular behavior at a solid-liquid interface. The R correlation coefficient 
      between the simulated and experimental peptide adsorption free energies increased 
      from 0.00 for the standard CHARMM force field parameters to 0.88 for the tuned 
      IFF parameters. Subsequent studies are planned to apply the tuned IFF parameter 
      set for the simulation of protein adsorption behavior on an HDPE surface for 
      comparison with experimental values of adsorbed protein orientation and 
      conformation.
FAU - Abramyan, Tigran M
AU  - Abramyan TM
AD  - Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson 
      University, Clemson, South Carolina 29634.
FAU - Snyder, James A
AU  - Snyder JA
AD  - Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson 
      University, Clemson, South Carolina 29634.
FAU - Yancey, Jeremy A
AU  - Yancey JA
AD  - Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson 
      University, Clemson, South Carolina 29634.
FAU - Thyparambil, Aby A
AU  - Thyparambil AA
AD  - Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson 
      University, Clemson, South Carolina 29634.
FAU - Wei, Yang
AU  - Wei Y
AD  - Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson 
      University, Clemson, South Carolina 29634.
FAU - Stuart, Steven J
AU  - Stuart SJ
AD  - Department of Chemistry, 369 Hunter Laboratories, Clemson University, Clemson, 
      South Carolina 29634.
FAU - Latour, Robert A
AU  - Latour RA
AD  - Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson 
      University, Clemson, South Carolina 29634.
LA  - eng
GR  - P20 GM103444/GM/NIGMS NIH HHS/United States
GR  - 5P20RR021949/RR/NCRR NIH HHS/United States
GR  - P20 RR021949/RR/NCRR NIH HHS/United States
GR  - EB002027/EB/NIBIB NIH HHS/United States
GR  - P41 EB002027/EB/NIBIB NIH HHS/United States
GR  - 8P20GM103444/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20150627
PL  - United States
TA  - Biointerphases
JT  - Biointerphases
JID - 101275679
RN  - 0 (Peptides)
RN  - 9002-88-4 (Polyethylene)
SB  - IM
MH  - *Adsorption
MH  - Molecular Dynamics Simulation
MH  - Peptides/*chemistry
MH  - Polyethylene/*chemistry
MH  - Protein Binding
MH  - *Surface Tension
PMC - PMC4376758
EDAT- 2015/03/31 06:00
MHDA- 2015/11/05 06:00
PMCR- 2016/03/27
CRDT- 2015/03/31 06:00
PHST- 2015/03/31 06:00 [entrez]
PHST- 2015/03/31 06:00 [pubmed]
PHST- 2015/11/05 06:00 [medline]
PHST- 2016/03/27 00:00 [pmc-release]
AID - 1.4916361 [pii]
AID - 311502BIP [pii]
AID - 10.1116/1.4916361 [doi]
PST - epublish
SO  - Biointerphases. 2015 Jun 27;10(2):021002. doi: 10.1116/1.4916361.