Membrane Protein Insertion into and Compatibility with Biomimetic Membranes. Issue 7 (16th June 2017)
- Record Type:
- Journal Article
- Title:
- Membrane Protein Insertion into and Compatibility with Biomimetic Membranes. Issue 7 (16th June 2017)
- Main Title:
- Membrane Protein Insertion into and Compatibility with Biomimetic Membranes
- Authors:
- 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 - Abstract:
- 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 physicalAbstract : 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. Abstract : Chemical and physical hydrophobicity mismatch are the key factors influencing membrane protein compatibility with biomimetic membranes. Chemical hydrophobic mismatch describes the hydrophobic character difference between protein outer surfaces and membrane hydrophobic cores. It is measured using a distyrylbenzene chromophore based assay presented in this article. Physical hydrophobicity mismatch is the thickness difference between protein hydrophobic length and bilayer hydrophobic core length. … (more)
- Is Part Of:
- Advanced biosystems. Volume 1 :Issue 7 (2017)
- Journal:
- Advanced biosystems
- Issue:
- Volume 1 :Issue 7 (2017)
- Issue Display:
- Volume 1, Issue 7 (2017)
- Year:
- 2017
- Volume:
- 1
- Issue:
- 7
- Issue Sort Value:
- 2017-0001-0007-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2017-06-16
- Subjects:
- amphiphilic block copolymers -- biomimetic membranes -- fluorescence correlation spectroscopy (FCS) -- hydrophobicity mismatch -- membrane proteins
Biological systems -- Periodicals
Biotechnology -- Periodicals
Bioengineering -- Periodicals
Biomedical engineering -- Periodicals
Biological Science Disciplines
Periodicals
Periodicals
660.6 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2366-7478 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/adbi.201700053 ↗
- Languages:
- English
- ISSNs:
- 2366-7478
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0696.830500
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2782.xml