Partially Reversible Adsorption of Annexin A1 on POPC/POPS Bilayers Investigated by QCM Measurements, SFM, and DMC Simulations

Kastl, Katja; Menke, Manuela; Lüthgens, Eike; Faiß, Simon; Gerke, Volker; Janshoff, Andreas; Steinem, Claudia

doi:10.1002/cbic.200500265

Cited by 19 publications

(12 citation statements)

References 33 publications

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“…Thus, under these conditions the observed FRET is a reflection of calcium-induced PS clustering rather than clustering induced by protein-protein interaction. A very similar model has been recently proposed to explain the high affinity binding of annexin I to PS/PC membranes (55).…”

Section: Enthalpy and Entropy As A Function Of Membrane Occupancy-mentioning

confidence: 72%

Entropic and Enthalpic Contributions to Annexin V-Membrane Binding

Jeppesen

Smith

Gibson

et al. 2008

Journal of Biological Chemistry

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Annexin V binds to membranes with very high affinity, but the factors responsible remain to be quantitatively elucidated. Analysis by isothermal microcalorimetry and calcium titration under conditions of low membrane occupancy showed that there was a strongly positive entropy change upon binding. For vesicles containing 25% phosphatidylserine at 0.15 M ionic strength, the free energy of binding was ؊53 kcal/mol protein, whereas the enthalpy of binding was ؊38 kcal/mol. Addition of 4 M urea decreased the free energy of binding by about 30% without denaturing the protein, suggesting that hydrophobic forces make a significant contribution to binding affinity. This was confirmed by mutagenesis studies that showed that binding affinity was modulated by the hydrophobicity of surface residues that are likely to enter the interfacial region upon protein-membrane binding. The change in free energy was quantitatively consistent with predictions from the WimleyWhite scale of interfacial hydrophobicity. In contrast, binding affinity was not increased by making the protein surface more positively charged, nor decreased by making it more negatively charged, ruling out general ionic interactions as major contributors to binding affinity. The affinity of annexin V was the same regardless of the head group present on the anionic phospholipids tested (phosphatidylserine, phosphatidylglycerol, phosphatidylmethanol, and cardiolipin), ruling out specific interactions between the protein and non-phosphate moieties of the head group as a significant contributor to binding affinity. Analysis by fluorescence resonance energy transfer showed that multimers did not form on phosphatidylserine membranes at low occupancy, indicating that annexin-annexin interactions did not contribute to binding affinity. In summary, binding of annexin V to membranes is driven by both enthalpic and entropic forces. Dehydration of hydrophobic regions of the protein surface as they enter the interfacial region makes an important contribution to overall binding affinity, supplementing the role of protein-calcium-phosphate chelates.

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Section: Enthalpy and Entropy As A Function Of Membrane Occupancy-mentioning

confidence: 72%

Entropic and Enthalpic Contributions to Annexin V-Membrane Binding

Jeppesen

Smith

Gibson

et al. 2008

Journal of Biological Chemistry

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“…To address the question of how annexins, which participate in various membrane‐related processes, including endocytosis and exocytosis, bind to and aggregate membranes, the association of annexin A6 (Buzhynskyy et al , 2009), annexin A5 (Garnier et al , 2009) and annexin A1 (Kastl et al , 2006; Faiss et al , 2008) with model phospholipid membranes was studied using QCM and other techniques. Another important membrane‐protein interaction probed by QCM was the membrane association of the hepatitis C virus NS5A protein, which is required for viral replication (Cho et al ., 2007a).…”

Section: Lipids and Membranesmentioning

confidence: 99%

A survey of the 2006–2009 quartz crystal microbalance biosensor literature

Becker

Cooper

2011

J of Molecular Recognition

162

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Since the publication of the original review of piezoelectric acoustic sensors in this series there has been a consistent, gradual expansion in the number of published papers using 'quartz crystal microbalances' (QCM). Between 2001 and 2009, the number of QCM publications per annum has increased from 49 to 273, with a two-fold increase in papers per annum between 2004 and 2008. Within the field, comparing the time covered by the current to the previous review, there are trends towards increasing use of QCM in the study of protein adsorption to surfaces (93% increase), homeostasis (67% increase), protein-protein interactions (40% increase) and carbohydrates (43% increase). New commercial systems have been released that are driving the uptake of the technology for characterization of binding specificities, affinities, kinetics and conformational changes associated with a molecular recognition event. This paper highlights theoretical and practical aspects of the principles that underpin acoustic analysis, then reviews exemplary papers in key application areas involving small molecular weight ligands, carbohydrates, proteins, nucleic acids, viruses, bacteria, cells and membrane interfaces.

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“…This phenomenon (two layers) is very similar to that of the annexin A1 aggregation on the lipid membrane. 24 At 4 nM, PrP molecules in solution minimize their oligomerization and aggregation. During the initial step of the surface aggregation, the PrP monomers deposit on the POPS-rich lipid membrane and form flat clusters in some small areas, which could be a very common behavior for many membrane proteins such as annexin A1.…”

mentioning

confidence: 99%

“…During the initial step of the surface aggregation, the PrP monomers deposit on the POPS-rich lipid membrane and form flat clusters in some small areas, which could be a very common behavior for many membrane proteins such as annexin A1. 24 Eventually, these small areas merge into a relatively large monolayer of PrP formed on the membrane surface. The aggregation of truncated PrP on the lipid membrane has been investigated at very high concentrations, 13,14 but in our studies, the compact monolayer of full-length PrP on the lipid membrane has been detected for the first time by using a very low concentration.…”

mentioning

confidence: 99%