An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

Seo, Jongcheol; Hoffmann, Waldemar; Warnke, Stephan; Huang, Xing; Gewinner, Sandy; Schöllkopf, Wieland; Bowers, Michael T.; Helden, Gert von; Pagel, Kevin

doi:10.1038/nchem.2615

Cited by 191 publications

(193 citation statements)

References 41 publications

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“…Again space constraints prevent the details from being given here. It was found that β-sheet onset was spectroscopically observed for both VEALYL and YVEALL with onset at n = 4 extending to n = 9 (the largest oligomer studied) but no β-sheet absorptions were observed for VELYAL in accordance of expectations from both IMS-MS and TEM results (83). This direct spectroscopic observation of β-sheet onset in oligomer growth is potentially a very important result and suggests that this type of investigation may be possible on systems of direct biological importance.…”

Section: Case 2: Peptide Assembly and The Amyloid Paradigmsupporting

confidence: 76%

“…These results indicate the IMS-MS/FEL technique developed in the FHI in Berlin has a bright future in the analysis of the secondary structure of peptides and proteins and their assemblies adding a very powerful compliment to the ability of IMS-MS methods to directly measure tertiary structure of monomers and the quaternary structure of assemblies (36,83). …”

Section: Case 2: Peptide Assembly and The Amyloid Paradigmmentioning

confidence: 94%

“…The blue and red Gaussians represent IR bands corresponding to turn-like (1660–1685 cm −1 ) and β-sheet structures (1610–1640 cm –1 and ~1690 cm −1 ), respectively. For details about the fitting procedure see reference (83) from which the figure was reconstructed.…”

Section: Figurementioning

confidence: 99%

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The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

Bleiholder

Bowers

2017

Annual Rev. Anal. Chem.

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Ion mobility spectrometry-mass spectrometry (IMS-MS) methods are increasingly used to study noncovalent assemblies of peptides and proteins. This review focuses on the noncovalent self-assembly of amino acids and peptides, systems at the heart of the amyloid process that play a central role in a number of devastating diseases. Three different systems are discussed in detail: the 42-residue peptide amyloid-β42 implicated in the etiology of Alzheimer's disease, several amyloid-forming peptides with 6–11 residues, and the assembly of individual amino acids. We also discuss from a more fundamental perspective the processes that determine how quickly proteins and their assemblies denature when the analyte ion has been stripped of its solvent in an IMS-MS measurement and how to soften the measurement so that biologically meaningful data can be recorded.

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Section: Case 2: Peptide Assembly and The Amyloid Paradigmsupporting

confidence: 76%

Section: Case 2: Peptide Assembly and The Amyloid Paradigmmentioning

confidence: 94%

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The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

Bleiholder

Bowers

2017

Annual Rev. Anal. Chem.

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“…[22][23][24] Further, IM-MS can be used to prepare samples for gas-phase IR spectroscopy. [25][26][27][28][29] Here ions are simultaneously mass-tocharge (m/z) selected by MS and specific oligomers are geometrical size selected by IMS. This is in contrast to experiments where only m/z selection is used which can suffer from signal overlap between a cluster and its larger counterpart, which, for example, have twice the mass and twice the charge.…”

Section: Introductionmentioning

confidence: 99%

Infrared spectrum and structure of the homochiral serine octamer–dichloride complex

et al. 2017

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The amino acid serine is known to form a very stable octamer which has properties that sets it apart from serine complexes having different sizes or from complexes composed of other amino acids. For example, both singly protonated serine octamers and anionic octamers complexed with two halogen ions, strongly prefer homochirality even when assembled from racemic D, L mixtures.Consequently, the structures of these complexes are of great interest but no acceptable candidates have so far been identified. Here we investigate anionic serine octamers coordinated with two chloride ions using a novel ion mobility/infrared spectroscopy technique in combination with theoretical calculations. The results allow the identification of a unique structure for (Ser 8 Cl 2 ) 2-that is highly symmetric, very stable, homochiral and whose calculated properties match those observed in the experiments. 3Clusters of atoms or molecules with unusually high relative intensities in mass spectra are termed "magic". In many instances, those "magic" clusters could be assigned to specific structures, often of high symmetry. Examples are numerous and include rare gas clusters 1 , fullerenes, most notably C 60 , 2 Ti 8 C 12 "metallocarbohedrane", 3 metal clusters such as Au 20 , 4,5 and highly symmetric protonated water clusters. 6,7 In the case of C 60 , the initial observation of magic numbers in mass spectra eventually led to the discovery of a new group of materials and a new form of carbon.Occasionally a "magic" cluster resists structural characterization. A famous example is the serine octamer. After electrospray of solutions containing serine, it was first observed that a cluster with the composition (Ser 8 H) + dominated the mass spectrum. 8 This is in contrast to mass spectra of other amino acid clusters, for which the intensity patterns of peaks in their mass spectra show much smoother evolution. The experimental observations have spurred calculations, and several candidates for structures of cationic serine octamers have been proposed. 8,17,[19][20][21] However, for most of them, the proposed structures do not provide an obvious reason for the observed homochirality. In addition, while the calculations indicate that the proposed structures are stable, they are not dramatically more stable compared to serine clusters of different sizes. Thus, there is no general consensus of the structure of serine octamer clusters and the quest for finding a structure that is compatible with the experimental observations is still ongoing. 4In contrast to the abundance of studies on the cationic serine octamer, little attention has so far been given to the anionic species. Here, we present results from a study on serine cluster anions, in which we couple ion mobility-mass spectrometry (IMS-MS) with infrared (IR) spectroscopy.IMS-MS gives the absolute, angle averaged collision cross section (CCS) of specific clusters and this value can be used to determine the overall size of the cluster and to judge if particular calculated structures are compa...

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“…Furthermore, the CO stretching vibration can be used as an effective marker for hydrogen bonding. 40,41 Two typical stretching bands appeared at 1743 and 1702 cm −1 , which are ascribed to the carbonyl C O stretching of the free and intramolecular H-bonded carboxylic acid. The disappearance of the former band and red shifts of the bands after sonication treatment reveal the breakage of weaker intramolecular interactions and formation of stronger intermolecular hydrogen bonding interactions.…”

Section: Resultsmentioning

confidence: 99%

Crystalline Dipeptide Nanobelts Based on Solid–Solid Phase Transformation Self-Assembly and Their Polarization Imaging of Cells

Song

Xing

Jiao

et al. 2018

ACS Appl. Mater. Interfaces

102

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Controlled phase transformation involving biomolecular organization to generate dynamic biomimetic selfassembly systems and functional materials is currently an appealing topic of research on molecular materials. Herein, we achieve by ultrasonic irradiation the direct solid−solid transition of bioinspired dipeptide organization from triclinic structured aggregates to nanofibers and eventually to monoclinic nanobelts with strong polarized luminescence. It is suggested that the locally high temperature and pressure produced by cavitation effects cleaves the hydrophobic, π−π stacking or self-locked intramolecular interactions involved in one phase state and then rearranges the molecular packing to form another well-ordered aromatic dipeptide crystalline structure. Such a sonication-modulated solid−solid phase transition evolution is governed by distinct molecular interactions at different stages of structural organization. The resulting crystalline nanobelts are for the first time applied for polarization imaging of cells, which can be advantageous to directly inspect the uptake and fate of nanoscale delivery platforms without labeling of fluorescent dyes. This finding provides a new perspective to comprehend the dynamic evolution of biomolecular self-organization with energy supply by an external field and open up a facile and versatile approach of using anisotropic nanostructures for polarization imaging of cells and even live organisms in future.

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An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

Cited by 191 publications

References 41 publications

The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

Infrared spectrum and structure of the homochiral serine octamer–dichloride complex

Crystalline Dipeptide Nanobelts Based on Solid–Solid Phase Transformation Self-Assembly and Their Polarization Imaging of Cells

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