The Experts below are selected from a list of 264 Experts worldwide ranked by ideXlab platform

Stefan Scheidelaar - One of the best experts on this subject based on the ideXlab platform.

  • Detergent-Free Extraction of the Reaction Center from Rhodobacter sphaeroides into Native Nanodiscs. Nanodisc Size Matters!
    Biophysical Journal, 2015
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, J. Antoinette Killian
    Abstract:

    It has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins directly from their native membrane in the form of nanodiscs [1]. Using the SMA technology, we purified and characterized reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides [2]. Our most significant findings were (i) that the SMA copolymer efficiently solubilizes membranes of this bacterium, (ii) that it allows preservation of the local lipid environment of the solubilized RCs, (iii) that the protein is even more stable in these “native nanodiscs” than in the native membrane, and (iv) that the size of the RC containing nanodiscs is significantly larger than that of protein-free nanodiscs.We next investigated what physical properties of the polymer and lipids determine the efficiency and kinetics of solubilization and how they affect the size of the nanodiscs. In particular, we tested the effect of SMA copolymer length, hydrophobicity, and charge state (varying pH) using different lipid compositions. In complementary assays, we determined how the cross-sectional diameter of a protein affects the size of a nanodisc by using purified constructs of covalently linked oligomeric RCs of different size.Our study contributes to the fundamental knowledge about the mode of action of SMA and thereby to the general applicability of native nanodiscs as host for membrane proteins and protein complexes of different size.1. Knowles et al., 2009, JACS, 131, 7484-74852. Swainsbury & Scheidelaar et al. 2014, Angewandte Chemie, 53, http://dx.doi.org/10.1002/anie.201406412

  • detergent free extraction of membrane proteins into native nanodiscs application to the reaction center of rhodobacter sphaeroides
    Biophysical Journal, 2014
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, Antoinette Killian
    Abstract:

    Recently, it has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins in the form of nanodiscs (SMALPs), also called ‘native nanodiscs’, directly from their native membrane [1,2]. To understand what physical properties of membranes and SMA modulate this unique property of SMA, we first studied the solubilization of vesicles of synthetic phospholipids by SMA using transmission experiments. We found that SMA is an excellent membrane Solubilizer, able to solubilize different types of membranes below, at and above the gel to crystalline-liquid phase temperature. Based on the kinetics of solubilization under different experimental conditions we developed a model for the mode of action of SMA that will also explain why SMA is an efficient Solubilizer, whereas membrane scaffold proteins (MSPs) and amphipols are not.Next we used the SMA technology to purify and characterize reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides in the form of native nanodiscs. Monitoring of heat stability and recombination kinetics of P+QB- in photo-excited RCs in native nanodiscs showed that (1) RCs are much more stable in native nanodiscs than in detergent, and (2) the charge recombination kinetics display native-membrane like behavior.Our study contributes fundamental knowledge about the mode of action of SMA that is essential for optimizing methods to extract membrane proteins from different organisms and it promotes the general applicability of SMALPs as host for membrane proteins in studies on interactions of proteins with native lipids and in protein structure determination studies.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Long et al., 2013, BMC Biotechnology, 13:41.

  • towards detergent free solubilization of membrane proteins into nanodiscs a biophysical study on the interaction between styrene maleic acid sma copolymers and synthetic phospholipid vesicles
    Biophysical Journal, 2013
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, Antoinette Killian
    Abstract:

    Recently, it has been discovered that SMA copolymers are able to solubilize membrane proteins in the form of styrene maleic acid lipid particles (SMALPs) without the use of destabilizing detergents [1,2]. In order to understand this unique property of SMA we studied the solubilization of multilamellar vesicles (MLVs) of synthetic saturated phospholipids by SMA as function of acyl chain length and temperature. The rate of solublization was monitored by transmission experiments. It was found that SMA polymers are excellent phospholipid membrane Solubilizers, that are able to solubilize below, at and above gel to crystalline liquid phase temperature, with most efficient solubilization close to and at the gel to liquid-crystalline phase transition temperature (Tm). The formation of ∼10 nm diameter SMALPs, also referred to as lipid-nanodisks was verified by negative stain-transmission electron microscopy (TEM) and dynamic light scattering (DLS). Comparison with the recombinant apolipoprotein MSP1D1 showed that SMA is a significantly more potent membrane Solubilizer than MSP1D1. Based on these and other results we developed a model for the mode of action of SMA that will be presented here.Our study contributes to the fundamental knowledge about the molecular mode of action of SMA, which is essential to develop general methods to succesfully extract membrane proteins directly from their native environment in the form of lipid-nanodiscs. As proof of principle that this is indeed possible, we succeeded in purifying the potassium channel KcsA from the inner membrane of E-coli using the SMA technology. These results and some of its implications will be presented in an accompanying poster.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Orwick et al., 2012, Angew.Chem., 51,1-6

Antoinette Killian - One of the best experts on this subject based on the ideXlab platform.

  • detergent free extraction of membrane proteins into native nanodiscs application to the reaction center of rhodobacter sphaeroides
    Biophysical Journal, 2014
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, Antoinette Killian
    Abstract:

    Recently, it has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins in the form of nanodiscs (SMALPs), also called ‘native nanodiscs’, directly from their native membrane [1,2]. To understand what physical properties of membranes and SMA modulate this unique property of SMA, we first studied the solubilization of vesicles of synthetic phospholipids by SMA using transmission experiments. We found that SMA is an excellent membrane Solubilizer, able to solubilize different types of membranes below, at and above the gel to crystalline-liquid phase temperature. Based on the kinetics of solubilization under different experimental conditions we developed a model for the mode of action of SMA that will also explain why SMA is an efficient Solubilizer, whereas membrane scaffold proteins (MSPs) and amphipols are not.Next we used the SMA technology to purify and characterize reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides in the form of native nanodiscs. Monitoring of heat stability and recombination kinetics of P+QB- in photo-excited RCs in native nanodiscs showed that (1) RCs are much more stable in native nanodiscs than in detergent, and (2) the charge recombination kinetics display native-membrane like behavior.Our study contributes fundamental knowledge about the mode of action of SMA that is essential for optimizing methods to extract membrane proteins from different organisms and it promotes the general applicability of SMALPs as host for membrane proteins in studies on interactions of proteins with native lipids and in protein structure determination studies.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Long et al., 2013, BMC Biotechnology, 13:41.

  • towards detergent free solubilization of membrane proteins into nanodiscs a biophysical study on the interaction between styrene maleic acid sma copolymers and synthetic phospholipid vesicles
    Biophysical Journal, 2013
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, Antoinette Killian
    Abstract:

    Recently, it has been discovered that SMA copolymers are able to solubilize membrane proteins in the form of styrene maleic acid lipid particles (SMALPs) without the use of destabilizing detergents [1,2]. In order to understand this unique property of SMA we studied the solubilization of multilamellar vesicles (MLVs) of synthetic saturated phospholipids by SMA as function of acyl chain length and temperature. The rate of solublization was monitored by transmission experiments. It was found that SMA polymers are excellent phospholipid membrane Solubilizers, that are able to solubilize below, at and above gel to crystalline liquid phase temperature, with most efficient solubilization close to and at the gel to liquid-crystalline phase transition temperature (Tm). The formation of ∼10 nm diameter SMALPs, also referred to as lipid-nanodisks was verified by negative stain-transmission electron microscopy (TEM) and dynamic light scattering (DLS). Comparison with the recombinant apolipoprotein MSP1D1 showed that SMA is a significantly more potent membrane Solubilizer than MSP1D1. Based on these and other results we developed a model for the mode of action of SMA that will be presented here.Our study contributes to the fundamental knowledge about the molecular mode of action of SMA, which is essential to develop general methods to succesfully extract membrane proteins directly from their native environment in the form of lipid-nanodiscs. As proof of principle that this is indeed possible, we succeeded in purifying the potassium channel KcsA from the inner membrane of E-coli using the SMA technology. These results and some of its implications will be presented in an accompanying poster.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Orwick et al., 2012, Angew.Chem., 51,1-6

Martijn C Koorengevel - One of the best experts on this subject based on the ideXlab platform.

  • Detergent-Free Extraction of the Reaction Center from Rhodobacter sphaeroides into Native Nanodiscs. Nanodisc Size Matters!
    Biophysical Journal, 2015
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, J. Antoinette Killian
    Abstract:

    It has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins directly from their native membrane in the form of nanodiscs [1]. Using the SMA technology, we purified and characterized reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides [2]. Our most significant findings were (i) that the SMA copolymer efficiently solubilizes membranes of this bacterium, (ii) that it allows preservation of the local lipid environment of the solubilized RCs, (iii) that the protein is even more stable in these “native nanodiscs” than in the native membrane, and (iv) that the size of the RC containing nanodiscs is significantly larger than that of protein-free nanodiscs.We next investigated what physical properties of the polymer and lipids determine the efficiency and kinetics of solubilization and how they affect the size of the nanodiscs. In particular, we tested the effect of SMA copolymer length, hydrophobicity, and charge state (varying pH) using different lipid compositions. In complementary assays, we determined how the cross-sectional diameter of a protein affects the size of a nanodisc by using purified constructs of covalently linked oligomeric RCs of different size.Our study contributes to the fundamental knowledge about the mode of action of SMA and thereby to the general applicability of native nanodiscs as host for membrane proteins and protein complexes of different size.1. Knowles et al., 2009, JACS, 131, 7484-74852. Swainsbury & Scheidelaar et al. 2014, Angewandte Chemie, 53, http://dx.doi.org/10.1002/anie.201406412

  • detergent free extraction of membrane proteins into native nanodiscs application to the reaction center of rhodobacter sphaeroides
    Biophysical Journal, 2014
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, Antoinette Killian
    Abstract:

    Recently, it has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins in the form of nanodiscs (SMALPs), also called ‘native nanodiscs’, directly from their native membrane [1,2]. To understand what physical properties of membranes and SMA modulate this unique property of SMA, we first studied the solubilization of vesicles of synthetic phospholipids by SMA using transmission experiments. We found that SMA is an excellent membrane Solubilizer, able to solubilize different types of membranes below, at and above the gel to crystalline-liquid phase temperature. Based on the kinetics of solubilization under different experimental conditions we developed a model for the mode of action of SMA that will also explain why SMA is an efficient Solubilizer, whereas membrane scaffold proteins (MSPs) and amphipols are not.Next we used the SMA technology to purify and characterize reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides in the form of native nanodiscs. Monitoring of heat stability and recombination kinetics of P+QB- in photo-excited RCs in native nanodiscs showed that (1) RCs are much more stable in native nanodiscs than in detergent, and (2) the charge recombination kinetics display native-membrane like behavior.Our study contributes fundamental knowledge about the mode of action of SMA that is essential for optimizing methods to extract membrane proteins from different organisms and it promotes the general applicability of SMALPs as host for membrane proteins in studies on interactions of proteins with native lipids and in protein structure determination studies.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Long et al., 2013, BMC Biotechnology, 13:41.

  • towards detergent free solubilization of membrane proteins into nanodiscs a biophysical study on the interaction between styrene maleic acid sma copolymers and synthetic phospholipid vesicles
    Biophysical Journal, 2013
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, Antoinette Killian
    Abstract:

    Recently, it has been discovered that SMA copolymers are able to solubilize membrane proteins in the form of styrene maleic acid lipid particles (SMALPs) without the use of destabilizing detergents [1,2]. In order to understand this unique property of SMA we studied the solubilization of multilamellar vesicles (MLVs) of synthetic saturated phospholipids by SMA as function of acyl chain length and temperature. The rate of solublization was monitored by transmission experiments. It was found that SMA polymers are excellent phospholipid membrane Solubilizers, that are able to solubilize below, at and above gel to crystalline liquid phase temperature, with most efficient solubilization close to and at the gel to liquid-crystalline phase transition temperature (Tm). The formation of ∼10 nm diameter SMALPs, also referred to as lipid-nanodisks was verified by negative stain-transmission electron microscopy (TEM) and dynamic light scattering (DLS). Comparison with the recombinant apolipoprotein MSP1D1 showed that SMA is a significantly more potent membrane Solubilizer than MSP1D1. Based on these and other results we developed a model for the mode of action of SMA that will be presented here.Our study contributes to the fundamental knowledge about the molecular mode of action of SMA, which is essential to develop general methods to succesfully extract membrane proteins directly from their native environment in the form of lipid-nanodiscs. As proof of principle that this is indeed possible, we succeeded in purifying the potassium channel KcsA from the inner membrane of E-coli using the SMA technology. These results and some of its implications will be presented in an accompanying poster.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Orwick et al., 2012, Angew.Chem., 51,1-6

Hans Meeldijk - One of the best experts on this subject based on the ideXlab platform.

  • Detergent-Free Extraction of the Reaction Center from Rhodobacter sphaeroides into Native Nanodiscs. Nanodisc Size Matters!
    Biophysical Journal, 2015
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, J. Antoinette Killian
    Abstract:

    It has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins directly from their native membrane in the form of nanodiscs [1]. Using the SMA technology, we purified and characterized reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides [2]. Our most significant findings were (i) that the SMA copolymer efficiently solubilizes membranes of this bacterium, (ii) that it allows preservation of the local lipid environment of the solubilized RCs, (iii) that the protein is even more stable in these “native nanodiscs” than in the native membrane, and (iv) that the size of the RC containing nanodiscs is significantly larger than that of protein-free nanodiscs.We next investigated what physical properties of the polymer and lipids determine the efficiency and kinetics of solubilization and how they affect the size of the nanodiscs. In particular, we tested the effect of SMA copolymer length, hydrophobicity, and charge state (varying pH) using different lipid compositions. In complementary assays, we determined how the cross-sectional diameter of a protein affects the size of a nanodisc by using purified constructs of covalently linked oligomeric RCs of different size.Our study contributes to the fundamental knowledge about the mode of action of SMA and thereby to the general applicability of native nanodiscs as host for membrane proteins and protein complexes of different size.1. Knowles et al., 2009, JACS, 131, 7484-74852. Swainsbury & Scheidelaar et al. 2014, Angewandte Chemie, 53, http://dx.doi.org/10.1002/anie.201406412

  • detergent free extraction of membrane proteins into native nanodiscs application to the reaction center of rhodobacter sphaeroides
    Biophysical Journal, 2014
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, Antoinette Killian
    Abstract:

    Recently, it has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins in the form of nanodiscs (SMALPs), also called ‘native nanodiscs’, directly from their native membrane [1,2]. To understand what physical properties of membranes and SMA modulate this unique property of SMA, we first studied the solubilization of vesicles of synthetic phospholipids by SMA using transmission experiments. We found that SMA is an excellent membrane Solubilizer, able to solubilize different types of membranes below, at and above the gel to crystalline-liquid phase temperature. Based on the kinetics of solubilization under different experimental conditions we developed a model for the mode of action of SMA that will also explain why SMA is an efficient Solubilizer, whereas membrane scaffold proteins (MSPs) and amphipols are not.Next we used the SMA technology to purify and characterize reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides in the form of native nanodiscs. Monitoring of heat stability and recombination kinetics of P+QB- in photo-excited RCs in native nanodiscs showed that (1) RCs are much more stable in native nanodiscs than in detergent, and (2) the charge recombination kinetics display native-membrane like behavior.Our study contributes fundamental knowledge about the mode of action of SMA that is essential for optimizing methods to extract membrane proteins from different organisms and it promotes the general applicability of SMALPs as host for membrane proteins in studies on interactions of proteins with native lipids and in protein structure determination studies.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Long et al., 2013, BMC Biotechnology, 13:41.

  • towards detergent free solubilization of membrane proteins into nanodiscs a biophysical study on the interaction between styrene maleic acid sma copolymers and synthetic phospholipid vesicles
    Biophysical Journal, 2013
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, Antoinette Killian
    Abstract:

    Recently, it has been discovered that SMA copolymers are able to solubilize membrane proteins in the form of styrene maleic acid lipid particles (SMALPs) without the use of destabilizing detergents [1,2]. In order to understand this unique property of SMA we studied the solubilization of multilamellar vesicles (MLVs) of synthetic saturated phospholipids by SMA as function of acyl chain length and temperature. The rate of solublization was monitored by transmission experiments. It was found that SMA polymers are excellent phospholipid membrane Solubilizers, that are able to solubilize below, at and above gel to crystalline liquid phase temperature, with most efficient solubilization close to and at the gel to liquid-crystalline phase transition temperature (Tm). The formation of ∼10 nm diameter SMALPs, also referred to as lipid-nanodisks was verified by negative stain-transmission electron microscopy (TEM) and dynamic light scattering (DLS). Comparison with the recombinant apolipoprotein MSP1D1 showed that SMA is a significantly more potent membrane Solubilizer than MSP1D1. Based on these and other results we developed a model for the mode of action of SMA that will be presented here.Our study contributes to the fundamental knowledge about the molecular mode of action of SMA, which is essential to develop general methods to succesfully extract membrane proteins directly from their native environment in the form of lipid-nanodiscs. As proof of principle that this is indeed possible, we succeeded in purifying the potassium channel KcsA from the inner membrane of E-coli using the SMA technology. These results and some of its implications will be presented in an accompanying poster.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Orwick et al., 2012, Angew.Chem., 51,1-6

Eefjan Breukink - One of the best experts on this subject based on the ideXlab platform.

  • Detergent-Free Extraction of the Reaction Center from Rhodobacter sphaeroides into Native Nanodiscs. Nanodisc Size Matters!
    Biophysical Journal, 2015
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, J. Antoinette Killian
    Abstract:

    It has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins directly from their native membrane in the form of nanodiscs [1]. Using the SMA technology, we purified and characterized reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides [2]. Our most significant findings were (i) that the SMA copolymer efficiently solubilizes membranes of this bacterium, (ii) that it allows preservation of the local lipid environment of the solubilized RCs, (iii) that the protein is even more stable in these “native nanodiscs” than in the native membrane, and (iv) that the size of the RC containing nanodiscs is significantly larger than that of protein-free nanodiscs.We next investigated what physical properties of the polymer and lipids determine the efficiency and kinetics of solubilization and how they affect the size of the nanodiscs. In particular, we tested the effect of SMA copolymer length, hydrophobicity, and charge state (varying pH) using different lipid compositions. In complementary assays, we determined how the cross-sectional diameter of a protein affects the size of a nanodisc by using purified constructs of covalently linked oligomeric RCs of different size.Our study contributes to the fundamental knowledge about the mode of action of SMA and thereby to the general applicability of native nanodiscs as host for membrane proteins and protein complexes of different size.1. Knowles et al., 2009, JACS, 131, 7484-74852. Swainsbury & Scheidelaar et al. 2014, Angewandte Chemie, 53, http://dx.doi.org/10.1002/anie.201406412

  • detergent free extraction of membrane proteins into native nanodiscs application to the reaction center of rhodobacter sphaeroides
    Biophysical Journal, 2014
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, David J. K. Swainsbury, Rienk Van Grondelle, Michael R. Jones, Antoinette Killian
    Abstract:

    Recently, it has been discovered that styrene-maleic acid (SMA) copolymers are able to solubilize membrane proteins in the form of nanodiscs (SMALPs), also called ‘native nanodiscs’, directly from their native membrane [1,2]. To understand what physical properties of membranes and SMA modulate this unique property of SMA, we first studied the solubilization of vesicles of synthetic phospholipids by SMA using transmission experiments. We found that SMA is an excellent membrane Solubilizer, able to solubilize different types of membranes below, at and above the gel to crystalline-liquid phase temperature. Based on the kinetics of solubilization under different experimental conditions we developed a model for the mode of action of SMA that will also explain why SMA is an efficient Solubilizer, whereas membrane scaffold proteins (MSPs) and amphipols are not.Next we used the SMA technology to purify and characterize reaction centers (RCs) from the purple bacterium Rhodobacter sphaeroides in the form of native nanodiscs. Monitoring of heat stability and recombination kinetics of P+QB- in photo-excited RCs in native nanodiscs showed that (1) RCs are much more stable in native nanodiscs than in detergent, and (2) the charge recombination kinetics display native-membrane like behavior.Our study contributes fundamental knowledge about the mode of action of SMA that is essential for optimizing methods to extract membrane proteins from different organisms and it promotes the general applicability of SMALPs as host for membrane proteins in studies on interactions of proteins with native lipids and in protein structure determination studies.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Long et al., 2013, BMC Biotechnology, 13:41.

  • towards detergent free solubilization of membrane proteins into nanodiscs a biophysical study on the interaction between styrene maleic acid sma copolymers and synthetic phospholipid vesicles
    Biophysical Journal, 2013
    Co-Authors: Stefan Scheidelaar, Martijn C Koorengevel, Hans Meeldijk, Eefjan Breukink, Antoinette Killian
    Abstract:

    Recently, it has been discovered that SMA copolymers are able to solubilize membrane proteins in the form of styrene maleic acid lipid particles (SMALPs) without the use of destabilizing detergents [1,2]. In order to understand this unique property of SMA we studied the solubilization of multilamellar vesicles (MLVs) of synthetic saturated phospholipids by SMA as function of acyl chain length and temperature. The rate of solublization was monitored by transmission experiments. It was found that SMA polymers are excellent phospholipid membrane Solubilizers, that are able to solubilize below, at and above gel to crystalline liquid phase temperature, with most efficient solubilization close to and at the gel to liquid-crystalline phase transition temperature (Tm). The formation of ∼10 nm diameter SMALPs, also referred to as lipid-nanodisks was verified by negative stain-transmission electron microscopy (TEM) and dynamic light scattering (DLS). Comparison with the recombinant apolipoprotein MSP1D1 showed that SMA is a significantly more potent membrane Solubilizer than MSP1D1. Based on these and other results we developed a model for the mode of action of SMA that will be presented here.Our study contributes to the fundamental knowledge about the molecular mode of action of SMA, which is essential to develop general methods to succesfully extract membrane proteins directly from their native environment in the form of lipid-nanodiscs. As proof of principle that this is indeed possible, we succeeded in purifying the potassium channel KcsA from the inner membrane of E-coli using the SMA technology. These results and some of its implications will be presented in an accompanying poster.1. Knowles et al., 2009, JACS, 131, 7484-7485.2. Orwick et al., 2012, Angew.Chem., 51,1-6