Determining the Orientation and Localization of Membrane-Bound Peptides

Hohlweg, W; Kosol, Simone; Zangger, Klaus

doi:10.2174/138920312800785049

Cited by 20 publications

(17 citation statements)

References 120 publications

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“…Both NMR and ESR experiments can be used to verify helix formation, and fluorescence quenching experiments can assess membrane insertion [17]. Oriented circular dichroism can further provide information about helicity and orientation relative to the membrane plane [18].…”

Section: Amphipathic Helices Coupling With Membrane Curvaturementioning

confidence: 99%

The 2018 biomembrane curvature and remodeling roadmap

Bassereau

Jin

Baumgart

et al. 2018

J. Phys. D: Appl. Phys.

247

187

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The importance of curvature as a structural feature of biological membranes has been recognized for many years and has fascinated scientists from a wide range of different backgrounds. On the one hand, changes in membrane morphology are involved in a plethora of phenomena involving the plasma membrane of eukaryotic cells, including endo- and exocytosis, phagocytosis and filopodia formation. On the other hand, a multitude of intracellular processes at the level of organelles rely on generation, modulation, and maintenance of membrane curvature to maintain the organelle shape and functionality. The contribution of biophysicists and biologists is essential for shedding light on the mechanistic understanding and quantification of these processes. Given the vast complexity of phenomena and mechanisms involved in the coupling between membrane shape and function, it is not always clear in what direction to advance to eventually arrive at an exhaustive understanding of this important research area. The 2018 Biomembrane Curvature and Remodeling Roadmap of Journal of Physics D: Applied Physics addresses this need for clarity and is intended to provide guidance both for students who have just entered the field as well as established scientists who would like to improve their orientation within this fascinating area.

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Section: Amphipathic Helices Coupling With Membrane Curvaturementioning

confidence: 99%

The 2018 biomembrane curvature and remodeling roadmap

Bassereau

Jin

Baumgart

et al. 2018

J. Phys. D: Appl. Phys.

247

187

View full text Add to dashboard Cite

show abstract

“…In addition, atomic resolution structures of small membrane-bound peptides can be obtained on a routine basis by solution NMR spectroscopy. Besides the structure, the localization and orientation in the membrane is often even more important to get insight into the biological function(s) of these hydrophobic peptides and proteins [5]. A plethora of biophysical techniques is available to determine the orientation of proteins and peptides in a membrane or membrane-mimetic, with magnetic resonance methods being arguably the most commonly used approach.…”

Section: Introductionmentioning

confidence: 99%

Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes

2013

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Many peptides and proteins are attached to or immersed in a biological membrane. In order to understand their function not only the structure but also their topology in the membrane is important. Solution NMR spectroscopy is one of the most often used approaches to determine the orientation and localization of membrane-bound peptides and proteins. Here we give an application-oriented overview on the use of paramagnetic probes for the investigation of membrane-bound peptides and proteins. The examples discussed range from the large pool of antimicrobial peptides, bacterial toxins, cell penetrating peptides to domains of larger proteins or the calcium regulating protein phospholamban. Topological information is obtained in all these examples by the use of either attached or freely mobile paramagnetic tags. For some examples information obtained from the paramagnetic probes was included in the structure determination.

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“…Zangger and coworkers [307] monitored the proton longitudinal relaxation rates upon addition of the freely water-soluble and the inert paramagnetic probe Gd (DTPA-BMA) of the a-helical peptide CM15, and determined the orientation of the fifteenresidue peptide in DPC micelles. This method has also been applied to study complete positioning of the AMPs CM15 and maximin H6 in DPC and SDS micelles [308,309]. This technique has the considerable advantage that isotopic labeling or chemical modifications of the peptide are not necessary.…”

Section: Nuclear Magnetic Resonance (Nmr) Spectroscopymentioning

confidence: 99%

Biophysical approaches for exploring lipopeptide-lipid interactions

et al. 2020

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a b s t r a c tIn recent years, lipopeptides (LPs) have attracted a lot of attention in the pharmaceutical industry due to their broad-spectrum of antimicrobial activity against a variety of pathogens and their unique mode of action. This class of compounds has enormous potential for application as an alternative to conventional antibiotics and for pest control. Understanding how LPs work from a structural and biophysical standpoint through investigating their interaction with cell membranes is crucial for the rational design of these biomolecules. Various analytical techniques have been developed for studying intramolecular interactions with high resolution. However, these tools have been barely exploited in lipopeptide-lipid interactions studies. These biophysical approaches would give precise insight on these interactions. Here, we reviewed these state-of-the-art analytical techniques. Knowledge at this level is indispensable for understanding LPs activity and particularly their potential specificity, which is relevant information for safe application. Additionally, the principle of each analytical technique is presented and the information acquired is discussed. The key challenges, such as the selection of the membrane model are also been briefly reviewed.Published by Elsevier B.V. 1.2.

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Determining the Orientation and Localization of Membrane-Bound Peptides

Cited by 20 publications

References 120 publications

The 2018 biomembrane curvature and remodeling roadmap

The 2018 biomembrane curvature and remodeling roadmap

Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes

Biophysical approaches for exploring lipopeptide-lipid interactions

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