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Title: Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin

Abstract

Nonideal polymer mixtures of PEGs of different molecular weights partition differently into nanosize protein channels. Here, we assess the validity of the recently proposed theoretical approach of forced partitioning for three structurally different beta-barrel channels: voltage-dependent anion channel from outer mitochondrial membrane VDAC, bacterial porin OmpC (outer membrane protein C), and bacterial channel-forming toxin alpha-hemolysin. Our interpretation is based on the idea that relatively less-penetrating polymers push the more easily penetrating ones into nanosize channels in excess of their bath concentration. Comparison of the theory with experiments is excellent for VDAC. Polymer partitioning data for the other two channels are consistent with theory if additional assumptions regarding the energy penalty of pore penetration are included. In conclusion, the obtained results demonstrate that the general concept of "polymers pushing polymers" is helpful in understanding and quantification of concrete examples of size-dependent forced partitioning of polymers into protein nanopores.

Authors:
 [1];  [2];  [3];  [4];  [1];  [1]
  1. Univ. of Massachusetts, Amherst, MA (United States)
  2. Univ. of Massachusetts, Amherst, MA (United States); Univ. of Ljubljana, Ljubljana (Slovenia); J. Stefan Institute, Ljubljana (Slovenia)
  3. National Institutes of Health, Bethesda, MD (United States)
  4. Univ. of Massachusetts, Amherst, MA (United States); National Institutes of Health, Bethesda, MD (United States)
Publication Date:
Research Org.:
Univ. of Massachusetts, Amherst, MA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Materials Sciences & Engineering Division; USDOE
OSTI Identifier:
1274822
Alternate Identifier(s):
OSTI ID: 1439277
Grant/Contract Number:  
SC0008176
Resource Type:
Journal Article: Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 113; Journal Issue: 32; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; β-barrel pores; nanopore-based sensing; polymer confinement; polymer; transport; macromolecular crowding

Citation Formats

Aksoyoglu, M. Alphan, Podgornik, Rudolf, Bezrukov, Sergey M., Gurnev, Philip A., Muthukumar, Murugappan, and Parsegian, V. Adrian. Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin. United States: N. p., 2016. Web. doi:10.1073/pnas.1602716113.
Aksoyoglu, M. Alphan, Podgornik, Rudolf, Bezrukov, Sergey M., Gurnev, Philip A., Muthukumar, Murugappan, & Parsegian, V. Adrian. Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin. United States. doi:10.1073/pnas.1602716113.
Aksoyoglu, M. Alphan, Podgornik, Rudolf, Bezrukov, Sergey M., Gurnev, Philip A., Muthukumar, Murugappan, and Parsegian, V. Adrian. Wed . "Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin". United States. doi:10.1073/pnas.1602716113.
@article{osti_1274822,
title = {Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin},
author = {Aksoyoglu, M. Alphan and Podgornik, Rudolf and Bezrukov, Sergey M. and Gurnev, Philip A. and Muthukumar, Murugappan and Parsegian, V. Adrian},
abstractNote = {Nonideal polymer mixtures of PEGs of different molecular weights partition differently into nanosize protein channels. Here, we assess the validity of the recently proposed theoretical approach of forced partitioning for three structurally different beta-barrel channels: voltage-dependent anion channel from outer mitochondrial membrane VDAC, bacterial porin OmpC (outer membrane protein C), and bacterial channel-forming toxin alpha-hemolysin. Our interpretation is based on the idea that relatively less-penetrating polymers push the more easily penetrating ones into nanosize channels in excess of their bath concentration. Comparison of the theory with experiments is excellent for VDAC. Polymer partitioning data for the other two channels are consistent with theory if additional assumptions regarding the energy penalty of pore penetration are included. In conclusion, the obtained results demonstrate that the general concept of "polymers pushing polymers" is helpful in understanding and quantification of concrete examples of size-dependent forced partitioning of polymers into protein nanopores.},
doi = {10.1073/pnas.1602716113},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 32,
volume = 113,
place = {United States},
year = {Wed Jul 27 00:00:00 EDT 2016},
month = {Wed Jul 27 00:00:00 EDT 2016}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1073/pnas.1602716113

Citation Metrics:
Cited by: 5 works
Citation information provided by
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Works referenced in this record:

Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences
journal, June 2008