Interactions of Small Protected Peptides with Aminopyrazole Derivatives: The Efficiency of Blocking a β‐Sheet Model in the Gas Phase

Fricke, Holger; Gerlach, Andreas; Unterberg, C.; Wehner, Markus; Schräder, Thomas; Gerhards, Markus

doi:10.1002/anie.200802396

Cited by 19 publications

(25 citation statements)

References 18 publications

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“…Pyrazole and pyrazole derivatives were investigated as template molecules by aggregating them with protected amino acids and small protected peptides 163,506 . In a first publication, the aggregation between the wellanalyzed protected amino acid Ac-Phe-OMe and pyrazole (Py) or 5-amino-3-methylpyrazole (MAP) (cf.…”

Section: Pyrazole-based Template Molecules As Potential β-Sheet Blockersmentioning

confidence: 99%

“…Comparison between experiments and theory is not only mandatory for proposing a basic interpretation, but is also at the heart of several of the most outstanding outcomes in the field. 72,74,103,113,133,134,141,144,150,152,153,[157][158][159][160]162,163,181,203,218,219,241,284,301,314,334,387,391,423,517 Nowadays, quantum chemistry suites are often sophisticated black boxes: even if an in-depth rationalization of the underlying phenomena is not easy to extract from calculations, they provide experimentalists with a reliable and relevant prediction of some of the experimental observables in the ground electronic state, like vibrational modes. The situation is more contrasted as far as the electronic structure and dynamical properties of the excited states of aromatic residues are concerned.…”

Section: Experimental Data Vs Theoretical Predictionsmentioning

confidence: 99%

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Neutral Peptides in the Gas Phase: Conformation and Aggregation Issues

et al. 2020

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Combined IR and UV laser spectroscopic techniques in molecular beams merged with theoretical approaches have proven to be an ideal tool to elucidate intrinsic structural properties on a molecular level. It offers the possibility to analyze structural changes by successively adding aggregation partners and thus an environment to a molecule. By this, it further makes these techniques a valuable starting point for a bottom-up approach in understanding the forces shaping larger molecular systems. This bottomup approach was successfully applied to neutral amino acids starting around the 1990s. Ever since experimental and theoretical methods developed further and investigations could be extended to larger peptide systems. Beyond, the review gives an introduction to secondary structures and experimental methods as well as a summary on theoretical approaches. Vibrational frequencies being characteristic probes of molecular structure and interactions are especially addressed. Archetypal biologically relevant secondary structures investigated by molecular beam spectroscopy are described and the influences of specific peptide residues on conformational preferences as well as the competition between secondary structures are discussed. Important influences like microsolvation or aggregation behaviour are presented. Beyond the linear α-peptides the main results of structural analysis on cyclic systems as well as on β-and γ-peptides are summarized. Overall, this contribution addresses current aspects of molecular beam spectroscopy on peptides and related species and provides molecular level insights into manifold issues of chemical and biochemical relevance. 45) , non-protected (cf. e.g. 46-48) and protected amino acids (cf. e.g. 49) up to dipeptide models (cf. e.g. 50).In this context, laser spectroscopic techniques combining IR and UV excitations, that one can consider as belonging to the so-called 'action spectroscopies', provide an isomer-selective method of choice to tackle the 87 ) or immunoglobulins (cf. e.g. 88), but they are also found in context with neurodegenerative diseases (cf. e.g. [89][90][91][92][93][94][95] and Section 12). A further structure associated with these diseases (cf. e.g. 96 ) is the β-helix, which presents a protein structure of several parallel β-strands in a helical arrangement with a frequently repetitive amino acid sequence. The structure is stabilized by H-bonds, sometimes ionic interactions or so called protein-protein interactions, which e.g. include electrostatic and hydrophobic effects. Further aspects of peptide structure in gas phase The role of protection groupsWith the unmodified N-and C-terminus amino acids and peptides can exhibit strong preferences for intramolecular H-bonds involving the N-and C-terminus, and can also form intermolecular H-bonds leading to polymer chains. Nevertheless, in a context where the description of the properties of a protein or a long peptide (with respect to its backbone) by smaller peptides is targeted, the introduction of protecting groups at the N-and...

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Section: Pyrazole-based Template Molecules As Potential β-Sheet Blockersmentioning

confidence: 99%

Section: Experimental Data Vs Theoretical Predictionsmentioning

confidence: 99%

Neutral Peptides in the Gas Phase: Conformation and Aggregation Issues

et al. 2020

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“…Beyond microsolvation, peptide-peptide interactions [31,46,73,87,90,120,124] and complexation with larger molecules have also been considered by several groups, especially to describe specifically interesting interactions between a peptide and its biological environment: peptides have been complexed with pyrazole to 246 E. Gloaguen and M. Mons favour β-sheets [65,100], with sugars to describe the interactions responsible for cellular recognition in glycopeptides [114,197], or to document the anomeric effect [198].…”

Section: Microsolvation Structures and Complexationmentioning

confidence: 99%

“…In this scope, complexation of model peptides [46,53,55,65,73,87,90,100,102,120,124,129,136] shed light on the interface between a protein and its environment.…”

Section: Environment and Flexibilitymentioning

confidence: 99%

Isolated Neutral Peptides

Gloaguen

Mons

2014

Topics in Current Chemistry

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This chapter examines the structural characterisation of isolated neutral amino-acids and peptides. After a presentation of the experimental and theoretical state-of-the-art in the field, a review of the major structures and shaping interactions is presented. Special focus is made on conformationally-resolved studies which enable one to go beyond simple structural characterisation; probing flexibility and excited-state photophysics are given as examples of promising future directions.

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“…1 Combined with mass-selected, double resonance IR-UV spectroscopy, and coupled with molecular mechanics, DFT and ab initio calculations, it enables the preparation, identification and structural assignment of their conformationally-selected molecular complexes. [2][3][4][5][6][7] When their partners are water molecules, this strategy also provides an entry into the 'no-man's land' between isolated biomolecules, probed at low temperatures in the gas phase, and solvated molecules dissolved in aqueous solution at ambient temperatures. 8,9 The influence of bound water molecules on the conformational landscapes of an expanding number of neutral amino acids, [10][11][12][13][14][15][16] small peptides [17][18][19] and especially carbohydrates [20][21][22][23][24][25][26] has been aided by the extreme sensitivity of their OH (and NH) vibrational spectra to hydrogen bonded solutesolvent interactions.…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate hydration: heavy water complexes of α and β anomers of glucose, galactose, fucose and xylose

Mayorkas

Rudić

Cocinero

et al. 2011

Phys. Chem. Chem. Phys.

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The singly and doubly hydrated complexes of the α and β anomers of a systematically varied set of monosaccharides, O-phenyl D-gluco-, D-galacto-, L-fuco- and D-xylopyranoside, have been generated in a cold molecular beam and probed through infrared-ultraviolet double resonance ion-dip (IRID) spectroscopy coupled with quantum mechanical calculations. A new 'twist' has been introduced by isotopic substitution, replacing H(2)O by D(2)O to separate the carbohydrate (OH) and hydrate (OD) vibrational signatures and also to relieve spectral congestion. The new spectroscopic and computational results have exposed subtle aspects of the intermolecular interactions which influence the finer details of their preferred structures, including the competing controls exerted by co-operative hydrogen bonding, bi-furcated and OH-π hydrogen bonding, stereoelectronic changes associated with the anomeric effect, and dispersion interactions. They also reassert the operation of general 'working rules' governing conformational change and regioselectivity in both singly and doubly hydrated monosaccharides.

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Interactions of Small Protected Peptides with Aminopyrazole Derivatives: The Efficiency of Blocking a β‐Sheet Model in the Gas Phase

Cited by 19 publications

References 18 publications

Neutral Peptides in the Gas Phase: Conformation and Aggregation Issues

Neutral Peptides in the Gas Phase: Conformation and Aggregation Issues

Isolated Neutral Peptides

Carbohydrate hydration: heavy water complexes of α and β anomers of glucose, galactose, fucose and xylose

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