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1. Role of membrane mimetics on biophysical EPR studies of membrane proteins

   https://doi.org/10.1016/j.bbamem.2023.184138  

   Sahu, Indra D.; Lorigan, Gary A. (February 2023, Biochimica et Biophysica Acta (BBA) - Biomembranes)
2. Modeling the Membrane Environment for Membrane Proteins

   https://doi.org/10.1016/j.bpj.2011.02.058  

   Separovic, Frances; Killian, J. Antoinette; Cotten, Myriam; Busath, David D.; Cross, Timothy A. (April 2011, Biophysical Journal)
3. Engineering Functional Membrane–Membrane Interfaces by InterSpy

   https://doi.org/10.1002/smll.202202104  

   Moghimianavval, Hossein; Patel, Chintan; Mohapatra, Sonisilpa; Hwang, Sung‐Won; Kayikcioglu, Tunc; Bashirzadeh, Yashar; Liu, Allen P.; Ha, Taekjip (May 2022, Small)

   Abstract Engineering synthetic interfaces between membranes has potential applications in designing non‐native cellular communication pathways and creating synthetic tissues. Here, InterSpy is introduced as a synthetic biology tool consisting of a heterodimeric protein engineered to form and maintain membrane–membrane interfaces between apposing synthetic as well as cell membranes through the SpyTag/SpyCatcher interaction. The inclusion of split fluorescent protein fragments in InterSpy allows tracking of the formation of a membrane–membrane interface and reconstitution of functional fluorescent protein in the space between apposing membranes. First, InterSpy is demonstrated by testing split protein designs using a mammalian cell‐free expression (CFE) system. By utilizing co‐translational helix insertion, cell‐free synthesized InterSpy fragments are incorporated into the membrane of liposomes and supported lipid bilayers with the desired topology. Functional reconstitution of split fluorescent protein between the membranes is strictly dependent on SpyTag/SpyCatcher. Finally, InterSpy is demonstrated in mammalian cells by detecting fluorescence reconstitution of split protein at the membrane–membrane interface between two cells each expressing a component of InterSpy. InterSpy demonstrates the power of CFE systems in the functional reconstitution of synthetic membrane interfaces via proximity‐inducing proteins. This technology may also prove useful where cell‐cell contacts and communication are recreated in a controlled manner using minimal components. 

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4. Effect of Membrane Properties on the Carbonation of Anion Exchange Membrane Fuel Cells

   https://doi.org/10.3390/membranes11020102  

   Zheng, Yiwei; Irizarry Colón, Lyzmarie Nicole; Ul Hassan, Noor; Williams, Eric R.; Stefik, Morgan; LaManna, Jacob M.; Hussey, Daniel S.; Mustain, William E. (February 2021, Membranes)

   null (Ed.)

   Anion exchange membrane fuel cells (AEMFC) are potentially very low-cost replacements for proton exchange membrane fuel cells. However, AEMFCs suffer from one very serious drawback: significant performance loss when CO2 is present in the reacting oxidant gas (e.g., air) due to carbonation. Although the chemical mechanisms for how carbonation leads to voltage loss in operating AEMFCs are known, the way those mechanisms are affected by the properties of the anion exchange membrane (AEM) has not been elucidated. Therefore, this work studies AEMFC carbonation using numerous high-functioning AEMs from the literature and it was found that the ionic conductivity of the AEM plays the most critical role in the CO2-related voltage loss from carbonation, with the degree of AEM crystallinity playing a minor role. In short, higher conductivity—resulting either from a reduction in the membrane thickness or a change in the polymer chemistry—results in faster CO2 migration and emission from the anode side. Although this does lead to a lower overall degree of carbonation in the polymer, it also increases CO2-related voltage loss. Additionally, an operando neutron imaging cell is used to show that as AEMFCs become increasingly carbonated their water content is reduced, which further drives down cell performance. 

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5. Perspective on the Effect of Membrane Mimetics on Dynamic Properties of Integral Membrane Proteins

   https://doi.org/10.1021/acs.jpcb.2c07324  

   Sahu, Indra D.; Lorigan, Gary A. (April 2023, The Journal of Physical Chemistry B)