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Title: Quantifying the Extent of Hydration of a Surface-Bound Peptide Using Neutron Reflectometry

Abstract

Establishing how water, or the absence of water, affects the structure, dynamics, and function of proteins in contact with inorganic surfaces is critical to developing successful protein immobilization strategies. In this work, the quantity of water hydrating a monolayer of helical peptides covalently attached to self-assembled monolayers (SAMs) of alkyl thiols on Au was measured using neutron reflectometry (NR). The peptide sequence was composed of repeating LLKK units in which the leucines were aligned to face the SAM. When immersed in water, NR measured 2.7 ± 0.9 water molecules per thiol in the SAM layer and between 75 ± 13 and 111 ± 13 waters around each peptide. The quantity of water in the SAM was nearly twice that measured prior to peptide functionalization, suggesting that the peptide disrupted the structure of the SAM. To identify the location of water molecules around the peptide, we compared our NR data to previously published molecular dynamics simulations of the same peptide on a hydrophobic SAM in water, revealing that 49 ± 5 of 95 ± 8 total nearby water molecules were directly hydrogen-bound to the peptide. Finally, we show that immersing the peptide in water compressed its structure into the SAM surface.more » Together, these results demonstrate that there is sufficient water to fully hydrate a surface-bound peptide even at hydrophobic interfaces. Given the critical role that water plays in biomolecular structure and function, these results are expected to be informative for a broad array of applications involving proteins at the bio/abio interface.« less

Authors:
 [1]; ORCiD logo [1];  [2]; ORCiD logo [2];  [2]; ORCiD logo [1]
  1. Univ. of Texas, Austin, TX (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Sandia National Lab. (SNL-NM), Albuquerque, NM (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE National Nuclear Security Administration (NNSA); USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; National Science Foundation (NSF)
OSTI Identifier:
1618090
Alternate Identifier(s):
OSTI ID: 1619215; OSTI ID: 1761705
Report Number(s):
SAND-2019-13693J; SAND-2019-9230J
Journal ID: ISSN 0743-7463; 681292
Grant/Contract Number:  
AC04-94AL85000; CHE-1807215; NA0003525; AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Langmuir
Additional Journal Information:
Journal Volume: 36; Journal Issue: 2; Journal ID: ISSN 0743-7463
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; thickness; atmospheric chemistry; peptides and proteins; layers; molecules

Citation Formats

Fies, Whitney A., First, Jeremy T., Dugger, Jason W., Doucet, Mathieu, Browning, James F., and Webb, Lauren J.. Quantifying the Extent of Hydration of a Surface-Bound Peptide Using Neutron Reflectometry. United States: N. p., 2019. Web. https://doi.org/10.1021/acs.langmuir.9b02559.
Fies, Whitney A., First, Jeremy T., Dugger, Jason W., Doucet, Mathieu, Browning, James F., & Webb, Lauren J.. Quantifying the Extent of Hydration of a Surface-Bound Peptide Using Neutron Reflectometry. United States. https://doi.org/10.1021/acs.langmuir.9b02559
Fies, Whitney A., First, Jeremy T., Dugger, Jason W., Doucet, Mathieu, Browning, James F., and Webb, Lauren J.. Tue . "Quantifying the Extent of Hydration of a Surface-Bound Peptide Using Neutron Reflectometry". United States. https://doi.org/10.1021/acs.langmuir.9b02559. https://www.osti.gov/servlets/purl/1618090.
@article{osti_1618090,
title = {Quantifying the Extent of Hydration of a Surface-Bound Peptide Using Neutron Reflectometry},
author = {Fies, Whitney A. and First, Jeremy T. and Dugger, Jason W. and Doucet, Mathieu and Browning, James F. and Webb, Lauren J.},
abstractNote = {Establishing how water, or the absence of water, affects the structure, dynamics, and function of proteins in contact with inorganic surfaces is critical to developing successful protein immobilization strategies. In this work, the quantity of water hydrating a monolayer of helical peptides covalently attached to self-assembled monolayers (SAMs) of alkyl thiols on Au was measured using neutron reflectometry (NR). The peptide sequence was composed of repeating LLKK units in which the leucines were aligned to face the SAM. When immersed in water, NR measured 2.7 ± 0.9 water molecules per thiol in the SAM layer and between 75 ± 13 and 111 ± 13 waters around each peptide. The quantity of water in the SAM was nearly twice that measured prior to peptide functionalization, suggesting that the peptide disrupted the structure of the SAM. To identify the location of water molecules around the peptide, we compared our NR data to previously published molecular dynamics simulations of the same peptide on a hydrophobic SAM in water, revealing that 49 ± 5 of 95 ± 8 total nearby water molecules were directly hydrogen-bound to the peptide. Finally, we show that immersing the peptide in water compressed its structure into the SAM surface. Together, these results demonstrate that there is sufficient water to fully hydrate a surface-bound peptide even at hydrophobic interfaces. Given the critical role that water plays in biomolecular structure and function, these results are expected to be informative for a broad array of applications involving proteins at the bio/abio interface.},
doi = {10.1021/acs.langmuir.9b02559},
journal = {Langmuir},
number = 2,
volume = 36,
place = {United States},
year = {2019},
month = {12}
}

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