Determination of protein structural flexibility by microsecond force spectroscopy

Dong, Mingdong; Husale, Sudhir; Şahin, Özgür

doi:10.1038/nnano.2009.156

Cited by 141 publications

(179 citation statements)

References 28 publications

Supporting

Mentioning

165

Contrasting

Unclassified

Order By: Relevance

“…Hence, fresh amyloid peptide solution is directly applied onto graphite surface, which allows for the peptide aggregation, whereby it mimics a naturally occurring process where amyloid peptides accumulate on the hydrophobic interface environment. The mediated self‐assembled structure of Aβ 33‐42 was identified by quantitative nanomechanical mapping with force controlled in pN range 14, 21. The topography image ( Figure 2 a) reveals three components, including the fibrils, a few spherical oligomers, and the substrate.…”

Section: Resultsmentioning

confidence: 99%

“…In this work, the different structures of Aβ 33‐42 aggregation were revealed by introducing different surfaces, e.g., graphite, graphene oxide (GO). Molecular monolayer of amyloid peptide was identified by means of a new quantitative nanomechanical spectroscopy technique with force controlled in pico‐Newton (pN) range that is capable of obtaining nanoscale resolution of individual molecule or supramolecular structures 14. Most significant is that the molecular monolayer consists of peptide nanostripes with parallel β‐strand‐like configuration dominated by hydrophobic interactions between peptides.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of a Novel Parallel β‐Strand Conformation within Molecular Monolayer of Amyloid Peptide

Liu

Zhang

et al. 2016

Advanced Science

Self Cite

View full text Add to dashboard Cite

The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early Aβ33‐42 aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide Aβ33‐42 consisting of novel parallel β‐strand‐like structure is further revealed by means of a quantitative nanomechanical spectroscopy technique with force controlled in pico‐Newton range, combining with molecular dynamic simulation. The identified parallel β‐strand‐like structure of molecular monolayer is distinct from the antiparallel β‐strand structure of Aβ33‐42 amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification of a Novel Parallel β‐Strand Conformation within Molecular Monolayer of Amyloid Peptide

Liu

Zhang

et al. 2016

Advanced Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…The new design is using the torsional harmonic cantilever concept that was developed for high-resolution nanomechanical analysis of samples 17,18 . These T-shaped cantilevers generate high-speed force-distance curves during the tapping-mode AFM imaging process.…”

mentioning

confidence: 99%

A nanomechanical interface to rapid single-molecule interactions

Dong

Şahin

2011

Nat Commun

Self Cite

View full text Add to dashboard Cite

single-molecule techniques provide opportunities for molecularly precise imaging, manipulation, assembly and biophysical studies. owing to the kinetics of bond rupture processes, rapid single-molecule measurements can reveal novel bond rupture mechanisms, probe singlemolecule events with short lifetimes and enhance the interaction forces supplied by single molecules. Rapid measurements will also increase throughput necessary for technological use of single-molecule techniques. Here we report a nanomechanical sensor that allows single-molecule force spectroscopy on the previously unexplored microsecond timescale. We probed bond lifetimes around 5 µs and observed significant enhancements in molecular interaction forces. our loading-rate-dependent measurements provide experimental evidence for an additional energy barrier in the biotin-streptavidin complex. We also demonstrate quantitative mapping of rapid single-molecule interactions with high spatial resolution. This nanomechanical interface may allow studies of molecular processes with short lifetimes and development of novel biological imaging, single-molecule manipulation and assembly technologies.

show abstract

“…contact-mode, did 95 not detect this cationic layer. 2,48 However, when imaging PM using a cantilever oscillated at higher frequencies 49 than in the present work, extracellular patches appeared substantially…”

Section: Side-specific Ionic Effetcs : Extracellular Interface Ionic mentioning

confidence: 54%

“…This journal is © The Royal Society of Chemistry [year] thicker than cytoplasmic patches (7.2 nm and 5.7 nm respectively) 49 suggesting that the cationic layer has a viscoelastic behaviour. 5 Unsurprisingly cytoplasmic and extracellular curves cannot be explained with DLVO.…”

Section: Side-specific Ionic Effetcs : Extracellular Interface Ionic mentioning

confidence: 99%

Controlled ionic condensation at the surface of a native extremophilemembrane

2010

View full text Add to dashboard Cite

entor nz gonter D F nd o¤ %t hovskyD uF nd y nD tF pF @PHIHA 9gontrolled ioni ondens tion t the surf e of n tive extremophile mem r neF9D x nos leFD P F ppF PPPEPPWF Further information on publisher's website:httpXGGdxFdoiForgGIHFIHQWGfWx HHPRVu Publisher's copyright statement:Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-pro t purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. At the nanoscale level biological membranes present a complex interface with the solvent. The functional dynamics and relative flexibility of membrane components together with the presence of specific ionic effects can combine to create exciting new phenomena that challenge traditional 10 theories such as the Derjaguin, Landau, Verwey and Overbeek (DLVO) theory or models interpreting the role of ions in terms of their ability to structure water (structure making/breaking).Here we investigate ionic effects at the surface of a highly charged extremophile membrane composed of a proton pump (bacteriorhodopsin) and archaeal lipids naturally assembled into a 2D crystal. Using amplitude-modulation atomic force microscopy (AM-AFM) in solution, we obtained 15 sub-molecular resolution images of ion-induced surface restructuring of the membrane. We demonstrate the presence of a stiff cationic layer condensed at its extracellular surface. This layer cannot be explained by traditional continuum theories. Dynamic force spectroscopy experiments suggest that it is produced by electrostatic correlation mediated by a Manning-type condensation of ions. In contrast, the cytoplasmic surface is dominated by short range repulsive hydration forces. 20These findings are relevant to archaeal bioenergetics and halophilic adaptation. Importantly, they present experimental evidence of a natural system that locally controls its interactions with the surrounding medium and challenges our current understanding of biological interfaces.

show abstract

Determination of protein structural flexibility by microsecond force spectroscopy

Cited by 141 publications

References 28 publications

Identification of a Novel Parallel β‐Strand Conformation within Molecular Monolayer of Amyloid Peptide

Identification of a Novel Parallel β‐Strand Conformation within Molecular Monolayer of Amyloid Peptide

A nanomechanical interface to rapid single-molecule interactions

Controlled ionic condensation at the surface of a native extremophilemembrane

Contact Info

Product

Resources

About