Sequence-Selective Binding of Peptides in Water by a Synthetic Receptor Molecule

Torneiro, Mercedes; Still, W. Clark

doi:10.1021/ja00126a043

Cited by 79 publications

(34 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They have one characteristic feature in common, however, namely that their side chains contain either an ammonium or carboxylic acid group, which both exhibit the ability to form hydrogen bonds. On the other hand, of the seven amino acids, only Tyr contained an aromatic residue, while the widely reported CD interactions with Phe and Trp [3,6,12,32] did not occur in the CD complexes described here, even though these amino acids were part of the sequence of most of the investigated peptides.…”

Section: Resultscontrasting

confidence: 53%

Determining the Binding Sites of β-Cyclodextrin and Peptides by Electron-Capture Dissociation High Resolution Tandem Mass Spectrometry

Geib

Volmer

2015

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

Cyclodextrins (CDs) are a group of cyclic oligosaccharides, which readily form inclusion complexes with hydrophobic compounds to increase bioavailability, thus making CDs ideal drug excipients. Recent studies have also shown that CDs exhibit a wide range of protective effects, preventing proteins from aggregation, degradation, and folding. These effects strongly depend on the binding sites on the protein surface. CDs only exhibit weak interactions with amino acids, however; conventional analytical techniques therefore usually fail to reveal the exact location of the binding sites. Moreover, some studies even suggest that CD inclusion complexes are merely electrostatic adducts. Here, electron capture dissociation (ECD) was applied in this proof-of-concept study to examine the exact nature of the CD/peptide complexes, and CD binding sites were unambiguously located for the first time via Fourier-transform ion cyclotron resonance (FTICR) tandem mass spectrometry.

show abstract

Section: Resultscontrasting

confidence: 53%

Determining the Binding Sites of β-Cyclodextrin and Peptides by Electron-Capture Dissociation High Resolution Tandem Mass Spectrometry

Geib

Volmer

2015

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

show abstract

“…Natural molecules use a hydrophobic microenvironment that shields the hydrogen bonding from the water such as in the double helix of DNA (1) and the interior of proteins (31, 32). Synthetic systems using this principle have been demonstrated (21)(22)(23)(24)(25)(33)(34)(35)(36)(37)(38)(39)(40)(41). It was anticipated that such a microenvironment, which is required for the creation of multimolecular helical columnar architectures in water analogous to those observed for 2 in dodecane, would be created by the arene-arene stacking of the hydrophobic aromatic surfaces of the molecules.…”

mentioning

confidence: 99%

Hierarchical formation of helical supramolecular polymers via stacking of hydrogen-bonded pairs in water

Brunsveld

Vekemans

Hirschberg

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

197

View full text Add to dashboard Cite

Bifunctional ureido-s-triazines provided with penta(ethylene oxide) side chains are able to self assemble in water, leading to helical columns via cooperative stacking of the hydrogen-bonded pairs (DADA array). Monofunctional ureido-s-triazines do not form such helical architectures. The presence of a linker, covalently connecting the two ureido-s-triazine units, is essential as it generates a high local concentration of aromatic units, favorable for stacking interactions. This hydrophobic stacking of the aromatic units occurs at concentrations as low as 5⅐10 ؊6 M and can be visualized by using fluorescence spectroscopy. The stacking generates a hydrophobic microenvironment that allows intermolecular hydrogen bonding to occur at higher concentrations because the hydrogen bonds are shielded from competitive hydrogen bonding with water. This hierarchical process results in the formation of a helical self-assembled polymer in water at concentrations above 10 ؊4 M. Chiral side chains attached to the ureido-striazine units bias the helicity of these columns as concluded from CD spectroscopy and ''Sergeants and Soldiers'' experiments.I n DNA, the well known double helical motif originates from self assembly and is directed by lateral hydrogen bonds between bases and stabilized by solvophobic interactions between the covalently linked bases perpendicular to the hydrogen bonds (1). Control over the intrinsic helicity of the structure is governed by the peripheral chirality in the sugar-phosphate backbone. In synthetic systems, noncovalent interactions have been used to obtain well defined self-assembled architectures in organic solvents (2-7). Peripheral chiral centers in assemblies (8-11) and chiral side chains attached to a polymer backbone (12-20) have been shown to bias chirality at the supramolecular level. Highly ordered multimolecular supramolecular structures stable in water, held together by hydrophobic interactions or with additional hydrogen bonding, are also known (21-25). However, it remains difficult to exploit directional noncovalent interactions in a cooperative way for the formation of discrete multimolecular assemblies stable in water. In this solvent, water molecules strongly compete with directional polar interactions such as hydrogen bonds, resulting in low association constants.The formation of helical self-assembled polymers in solution by both stacking and hydrogen bonding has recently been demonstrated by us (26, 27). Self-complementary apolar molecules 1 and 2 dimerize via strong cooperative 4-fold hydrogen bonding (ADAD) in chloroform (28), giving rise to the formation of a dimer by 1 and a random coil polymer by 2, the latter featuring viscous solutions at higher concentrations. Additional to the hydrogen bonding, solvophobic interactions between the aromatic surfaces arise for 1 and 2 in alkanes. Association via hydrogen bonding of the ureido-s-triazine functional groups leads to the formation of a large and planar aromatic core surrounded by six flexible chains, a structure that is conduciv...

show abstract

“…4 In contrast to the abundance of biological systems that reflect the conformational change, e.g ., the folding or unfolding, of their molecular components on the resultant intermolecular association and supramolecular assembly, synthetic self-assembling systems based on designed molecules have mainly focused on stably folded oligomers, i.e ., foldamers, 5 or on adjusting the specificity and strength of intermolecular association. 6,7 Few examples that show altered supramolecular outcomes due to conformational change of molecular components are known.…”

mentioning

confidence: 99%

Surprising impact of remote groups on the folding–unfolding and dimer-chain equilibria of bifunctional H-bonding unimers

Cheng

Baker

et al. 2016

Chem. Commun.

View full text Add to dashboard Cite

show abstract

Sequence-Selective Binding of Peptides in Water by a Synthetic Receptor Molecule

Cited by 79 publications

References 0 publications

Determining the Binding Sites of β-Cyclodextrin and Peptides by Electron-Capture Dissociation High Resolution Tandem Mass Spectrometry

Determining the Binding Sites of β-Cyclodextrin and Peptides by Electron-Capture Dissociation High Resolution Tandem Mass Spectrometry

Hierarchical formation of helical supramolecular polymers via stacking of hydrogen-bonded pairs in water

Surprising impact of remote groups on the folding–unfolding and dimer-chain equilibria of bifunctional H-bonding unimers

Contact Info

Product

Resources

About