Membrane Protein Insertion into and Compatibility with Biomimetic Membranes

Tingwei Ren, Mustafa Erbakan, Yuexiao Shen, Eduardo Barbieri, Patrick Saboe, Hasin Feroz, Hengjing Yan, Samantha McCuskey, Joseph F. Hall, A. Benjamin Schantz, Guillermo C. Bazan, Peter J. Butler, Mariusz Grzelakowski, Manish Kumar

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Membrane protein and membrane protein–mimic functionalized materials are rapidly gaining interest across a wide range of applications, including drug screening, DNA sequencing, drug delivery, sensors, water desalination, and bioelectronics. In these applications, material performance is highly dependent on activity-per-protein and protein packing density in bilayer and bilayer-like structures collectively known as biomimetic membranes. However, a clear understanding of, and accurate tools to study these properties of biomimetic membranes does not exist. This paper presents methods to evaluate membrane protein compatibility with biomimetic membrane materials. The methods utilized provide average single protein activity, and for the first time, provide experimentally quantifiable measures of the chemical and physical compatibility between proteins (and their mimics) and membrane materials. Water transport proteins, rhodopsins, and artificial water channels are reconstituted into the full range of current biomimetic membrane matrices to evaluate the proposed platform. Compatibility measurement results show that both biological and artificial water channels tested largely preserve their single protein water transport rates in biomimetic membranes, while their reconstitution density is variable, leading to different overall membrane permeabilities. It is also shown that membrane protein insertion efficiency inversely correlates with both chemical and physical hydrophobicity mismatch between membrane protein and the membrane matrix.

Original languageEnglish (US)
Article number1700053
JournalAdvanced Biosystems
Volume1
Issue number7
DOIs
StatePublished - Jul 2017

Fingerprint

Biomimetics
Membrane Proteins
Proteins
Membranes
Aquaporins
Water
Biomimetic Materials
Preclinical Drug Evaluations
Rhodopsin
Protein Transport
Desalination
Hydrophobicity
Drug delivery
Hydrophobic and Hydrophilic Interactions
DNA Sequence Analysis
Permeability
Carrier Proteins
Screening
DNA

All Science Journal Classification (ASJC) codes

  • Biomaterials
  • Biomedical Engineering
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Ren, T., Erbakan, M., Shen, Y., Barbieri, E., Saboe, P., Feroz, H., ... Kumar, M. (2017). Membrane Protein Insertion into and Compatibility with Biomimetic Membranes. Advanced Biosystems, 1(7), [1700053]. https://doi.org/10.1002/adbi.201700053
Ren, Tingwei ; Erbakan, Mustafa ; Shen, Yuexiao ; Barbieri, Eduardo ; Saboe, Patrick ; Feroz, Hasin ; Yan, Hengjing ; McCuskey, Samantha ; Hall, Joseph F. ; Schantz, A. Benjamin ; Bazan, Guillermo C. ; Butler, Peter J. ; Grzelakowski, Mariusz ; Kumar, Manish. / Membrane Protein Insertion into and Compatibility with Biomimetic Membranes. In: Advanced Biosystems. 2017 ; Vol. 1, No. 7.
@article{dc4fc8f1e87a44bbb3d7f17258e55a53,
title = "Membrane Protein Insertion into and Compatibility with Biomimetic Membranes",
abstract = "Membrane protein and membrane protein–mimic functionalized materials are rapidly gaining interest across a wide range of applications, including drug screening, DNA sequencing, drug delivery, sensors, water desalination, and bioelectronics. In these applications, material performance is highly dependent on activity-per-protein and protein packing density in bilayer and bilayer-like structures collectively known as biomimetic membranes. However, a clear understanding of, and accurate tools to study these properties of biomimetic membranes does not exist. This paper presents methods to evaluate membrane protein compatibility with biomimetic membrane materials. The methods utilized provide average single protein activity, and for the first time, provide experimentally quantifiable measures of the chemical and physical compatibility between proteins (and their mimics) and membrane materials. Water transport proteins, rhodopsins, and artificial water channels are reconstituted into the full range of current biomimetic membrane matrices to evaluate the proposed platform. Compatibility measurement results show that both biological and artificial water channels tested largely preserve their single protein water transport rates in biomimetic membranes, while their reconstitution density is variable, leading to different overall membrane permeabilities. It is also shown that membrane protein insertion efficiency inversely correlates with both chemical and physical hydrophobicity mismatch between membrane protein and the membrane matrix.",
author = "Tingwei Ren and Mustafa Erbakan and Yuexiao Shen and Eduardo Barbieri and Patrick Saboe and Hasin Feroz and Hengjing Yan and Samantha McCuskey and Hall, {Joseph F.} and Schantz, {A. Benjamin} and Bazan, {Guillermo C.} and Butler, {Peter J.} and Mariusz Grzelakowski and Manish Kumar",
year = "2017",
month = "7",
doi = "10.1002/adbi.201700053",
language = "English (US)",
volume = "1",
journal = "Advanced Biosystems",
issn = "2366-7478",
publisher = "Wiley-VCH Verlag",
number = "7",

}

Ren, T, Erbakan, M, Shen, Y, Barbieri, E, Saboe, P, Feroz, H, Yan, H, McCuskey, S, Hall, JF, Schantz, AB, Bazan, GC, Butler, PJ, Grzelakowski, M & Kumar, M 2017, 'Membrane Protein Insertion into and Compatibility with Biomimetic Membranes', Advanced Biosystems, vol. 1, no. 7, 1700053. https://doi.org/10.1002/adbi.201700053

Membrane Protein Insertion into and Compatibility with Biomimetic Membranes. / Ren, Tingwei; Erbakan, Mustafa; Shen, Yuexiao; Barbieri, Eduardo; Saboe, Patrick; Feroz, Hasin; Yan, Hengjing; McCuskey, Samantha; Hall, Joseph F.; Schantz, A. Benjamin; Bazan, Guillermo C.; Butler, Peter J.; Grzelakowski, Mariusz; Kumar, Manish.

In: Advanced Biosystems, Vol. 1, No. 7, 1700053, 07.2017.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Membrane Protein Insertion into and Compatibility with Biomimetic Membranes

AU - Ren, Tingwei

AU - Erbakan, Mustafa

AU - Shen, Yuexiao

AU - Barbieri, Eduardo

AU - Saboe, Patrick

AU - Feroz, Hasin

AU - Yan, Hengjing

AU - McCuskey, Samantha

AU - Hall, Joseph F.

AU - Schantz, A. Benjamin

AU - Bazan, Guillermo C.

AU - Butler, Peter J.

AU - Grzelakowski, Mariusz

AU - Kumar, Manish

PY - 2017/7

Y1 - 2017/7

N2 - Membrane protein and membrane protein–mimic functionalized materials are rapidly gaining interest across a wide range of applications, including drug screening, DNA sequencing, drug delivery, sensors, water desalination, and bioelectronics. In these applications, material performance is highly dependent on activity-per-protein and protein packing density in bilayer and bilayer-like structures collectively known as biomimetic membranes. However, a clear understanding of, and accurate tools to study these properties of biomimetic membranes does not exist. This paper presents methods to evaluate membrane protein compatibility with biomimetic membrane materials. The methods utilized provide average single protein activity, and for the first time, provide experimentally quantifiable measures of the chemical and physical compatibility between proteins (and their mimics) and membrane materials. Water transport proteins, rhodopsins, and artificial water channels are reconstituted into the full range of current biomimetic membrane matrices to evaluate the proposed platform. Compatibility measurement results show that both biological and artificial water channels tested largely preserve their single protein water transport rates in biomimetic membranes, while their reconstitution density is variable, leading to different overall membrane permeabilities. It is also shown that membrane protein insertion efficiency inversely correlates with both chemical and physical hydrophobicity mismatch between membrane protein and the membrane matrix.

AB - Membrane protein and membrane protein–mimic functionalized materials are rapidly gaining interest across a wide range of applications, including drug screening, DNA sequencing, drug delivery, sensors, water desalination, and bioelectronics. In these applications, material performance is highly dependent on activity-per-protein and protein packing density in bilayer and bilayer-like structures collectively known as biomimetic membranes. However, a clear understanding of, and accurate tools to study these properties of biomimetic membranes does not exist. This paper presents methods to evaluate membrane protein compatibility with biomimetic membrane materials. The methods utilized provide average single protein activity, and for the first time, provide experimentally quantifiable measures of the chemical and physical compatibility between proteins (and their mimics) and membrane materials. Water transport proteins, rhodopsins, and artificial water channels are reconstituted into the full range of current biomimetic membrane matrices to evaluate the proposed platform. Compatibility measurement results show that both biological and artificial water channels tested largely preserve their single protein water transport rates in biomimetic membranes, while their reconstitution density is variable, leading to different overall membrane permeabilities. It is also shown that membrane protein insertion efficiency inversely correlates with both chemical and physical hydrophobicity mismatch between membrane protein and the membrane matrix.

UR - http://www.scopus.com/inward/record.url?scp=85048368388&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85048368388&partnerID=8YFLogxK

U2 - 10.1002/adbi.201700053

DO - 10.1002/adbi.201700053

M3 - Article

AN - SCOPUS:85048368388

VL - 1

JO - Advanced Biosystems

JF - Advanced Biosystems

SN - 2366-7478

IS - 7

M1 - 1700053

ER -

Ren T, Erbakan M, Shen Y, Barbieri E, Saboe P, Feroz H et al. Membrane Protein Insertion into and Compatibility with Biomimetic Membranes. Advanced Biosystems. 2017 Jul;1(7). 1700053. https://doi.org/10.1002/adbi.201700053