Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbit[8]uril–methyl viologen complex

Ali, Omar A.; Olson, Eric M.; Urbach, Adam R.

doi:10.1080/10610278.2013.810338

Cited by 14 publications

(14 citation statements)

References 41 publications

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“…To further understand the role of rigidity on ternary complex formation (introduced into the system by the cystine bridge) the affinity of the linear version (Seq‐ l ) of the selected sequences was also evaluated. Fluorescence titrations carried out on linear sequences also showed quenching, but generally to a lower extent compared to the cyclic sequences (as marked by dashed lines in Figure S9), suggesting lower affinity as previously reported for Trp containing peptides binding to MV⋅CB[8] . The ITC data, reported in Table and in Figures d and S9, showed a general decrease in affinity for all of the sequences.…”

Section: Figuresupporting

confidence: 74%

High Affinity Recognition of a Selected Amino Acid Epitope within a Protein by Cucurbit[8]uril Complexation

Sonzini

Marcozzi

Gübeli³

et al. 2016

Angewandte Chemie

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Supramolecular interactions between the host cucurbit[8]uril (CB[8]) and amino acids have been widely interrogated, but recognition of specific motifs within a protein domain have never been reported. A phage display approach was herein used to select motifs with the highest binding affinity for the heteroternary complex with methyl viologen and CB[8] (MV⋅CB[8]) within a vast pool of cyclic peptide sequences. From the selected motifs, an epitope consisting of three amino acid was extrapolated and incorporated into a solvent‐exposed loop of a protein domain; the protein exhibited micromolar binding affinity for the MV⋅CB[8] complex, matching that of the cyclic peptide. By achieving selective CB[8]‐mediated conjugation of a small molecule to a recombinant protein scaffold we pave the way to biomedical applications of this simple ternary system.

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Section: Figuresupporting

confidence: 74%

High Affinity Recognition of a Selected Amino Acid Epitope within a Protein by Cucurbit[8]uril Complexation

Sonzini

Marcozzi

Gübeli³

et al. 2016

Angewandte Chemie

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“…Fluorescence titrations carried out on linear sequences also showed quenching, but generally to al ower extent compared to the cyclic sequences (as marked by dashed lines in Figure S9), suggesting lower affinity as previously reported for Tr pc ontaining peptides binding to MV·CB [8]. [30] TheI TC data, reported in Table 2 and in Figures 3d and S9, showed ag eneral decrease in affinity for all of the sequences.W hile Seq 2-l showed an increase of more than 3.5 fold in dissociation constant, Seq 1l did not present any binding and Seq 3-l displayed al ow enthalpic interaction that did not allow for fitting of the data points ( Figure S9 b). Them ain difference in thermodynamic contributions between Seq 2-c and l is in the entropic term (more unfavorable for the linear sequence), suggesting an introduction of rigidity in the linear peptide upon binding.On account of the overall data, it is possible to infer that the steric constraints introduced by the cystine bridge are fundamental towards the enhancement in affinity.…”

supporting

confidence: 74%

“…Thepositive entropic contribution is likely related to the release of additional water molecules,both from the solvating sphere of the peptide and possibly the CB [8] cavity. [30] TheI TC data, reported in Table 2 and in Figures 3d and S9, showed ag eneral decrease in affinity for all of the sequences.W hile Seq 2-l showed an increase of more than 3.5 fold in dissociation constant, Seq 1l did not present any binding and Seq 3-l displayed al ow enthalpic interaction that did not allow for fitting of the data points (Figure S9 b). Fluorescence titrations carried out on linear sequences also showed quenching, but generally to al ower extent compared to the cyclic sequences (as marked by dashed lines in Figure S9), suggesting lower affinity as previously reported for Tr pc ontaining peptides binding to MV·CB [8].…”

mentioning

confidence: 86%

High Affinity Recognition of a Selected Amino Acid Epitope within a Protein by Cucurbit[8]uril Complexation

Sonzini

Marcozzi

Gübeli³

et al. 2016

Angew Chem Int Ed

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Supramolecular interactions between the host cucurbit[8]uril (CB[8]) and amino acids have been widely interrogated, but recognition of specific motifs within a protein domain have never been reported. A phage display approach was herein used to select motifs with the highest binding affinity for the heteroternary complex with methyl viologen and CB[8] (MV⋅CB[8]) within a vast pool of cyclic peptide sequences. From the selected motifs, an epitope consisting of three amino acid was extrapolated and incorporated into a solvent-exposed loop of a protein domain; the protein exhibited micromolar binding affinity for the MV⋅CB[8] complex, matching that of the cyclic peptide. By achieving selective CB[8]-mediated conjugation of a small molecule to a recombinant protein scaffold we pave the way to biomedical applications of this simple ternary system.

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“…Given that binding of the MGG‐YFP complex does not involve the MGG N‐terminus, most likely in‐chain aromatic amino acid side‐chains are responsible. It has been described that not only tryptophan, but also the aromatic amino acids phenylalanine and tyrosine can bind to the cucurbit[8]uril⋅methylviologen complex 59–62. It is thus most likely that MGG‐YFP, and potentially in part also WGG‐YFP, interact with the cucurbit[8]uril⋅methylviologen complex through some of its other aromatic amino acids.…”

Section: Resultsmentioning

confidence: 99%

Supramolecular Protein Immobilization on Lipid Bilayers

Bosmans

Hendriksen

Verheijden

et al. 2015

Chemistry A European J

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Protein immobilization on surfaces, and on lipid bilayerss pecifically,h as great potential in biomoleculara nd biotechnological research. Of current special interest is the immobilizationo fp roteins using supramolecular noncovalent interactions. This allows for ar eversible immobilization and obviates the use of harsh ligation conditions that could denature fragile proteins.I nt he work presented here, reversible supramolecular immobilization of proteins on lipid bilayer surfaces was achieved by using the host-guest interaction of the macrocyclic molecule cucurbit[8]uril. Af luorescent protein was successfully immobilized on the lipid bilayer by making use of the property of cucurbit [8]uril to host together am ethylviologen and the indole of at ryptophan positionedo nthe N-terminal of the protein. The supramolecular complex was anchored to the bilayer through ac holesterol moiety that was attached to the methylviologen tethered with asmall polyethylene glycolspacer.Protein immobilization studies using aq uartz crystal microbalance (QCM)s howedt he assembly of the supramolecular complexeso nt he bilayer. Specific immobilization through the protein N-terminus is more efficient than through protein side-chain events. Reversible surfacer eleaseo ft he proteins could be achieved by washing with cucurbit[8]uril or buffer alone.T he described system shows the potentialo fs upramolecular assembly of proteins and providesamethod for site-specific protein immobilization under mild conditions in ar eversible manner.

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Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbit[8]uril–methyl viologen complex

Cited by 14 publications

References 41 publications

High Affinity Recognition of a Selected Amino Acid Epitope within a Protein by Cucurbit[8]uril Complexation

High Affinity Recognition of a Selected Amino Acid Epitope within a Protein by Cucurbit[8]uril Complexation

High Affinity Recognition of a Selected Amino Acid Epitope within a Protein by Cucurbit[8]uril Complexation

Supramolecular Protein Immobilization on Lipid Bilayers

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