The use of 2D NMR to study β-cyclodextrin complexation and debittering of amino acids and peptides

Linde, Giani Andréa; Laverde, Antônio; Faria, Eliete Vaz de; Colauto, Nelson Barros; Moraes, Flávio Faria de; Zanin, Gisella Maria

doi:10.1016/j.foodres.2009.09.025

Cited by 56 publications

(35 citation statements)

References 31 publications

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“…Taken together, the data indicate that the stability of the aromatic amino acids:β-CD complexes is in the following order: Tyr > Trp > Phe. This finding is quite different from the results previously published in which the single amino acids alone were considered (in that case the order was: l-Trp > L-Tyr > L-Phe) (Linde et al 2010), suggesting that the interaction is also influenced by the position that the residue under consideration occupies within the peptide chain.…”

Section: Determination Of Binding Constant By Uv-vis Spectroscopycontrasting

confidence: 99%

“…This behavior fosters the flanking residues to establish interactions with the hydroxyl groups of the upper rim of the host resulting in a further stabilization of the complex. This, also, explains why the incorporation of the aromatic amino acids into tripeptides results in a change in selectivity with respect to the corresponding monomeric amino acids (Linde et al 2010).…”

Section: Resultsmentioning

confidence: 89%

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Investigating the inclusion properties of aromatic amino acids complexing beta-cyclodextrins in model peptides

et al. 2015

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Cyclodextrins are commonly used as complexing agents in biological, pharmaceutical, and industrial applications since they have an effect on protein thermal and proteolytic stability, refolding yields, solubility, and taste masking. β-cyclodextrins (β-CD), because of their cavity size are a perfectly suited complexing agent for many common guest moieties. In the case of peptide-cyclodextrin and protein-cyclodextrin host-guest complexes the aromatic amino acids are reported to be the principal responsible of the interaction. For these reasons, we have investigated the inclusion properties of nine designed tripeptides, obtained permuting the position of two L-alanines (Ala, A) with that of one L-tryptophan (Trp, W), L-phenylalanine (Phe, F), or L-tyrosine (Tyr, Y), respectively. Interestingly, the position of the aromatic side-chain in the sequence appears to modulate the β-CD:peptide binding constants, determined via UV-Vis and NMR spectroscopy, which in turn assumes values higher than those reported for the single amino acid. The tripeptides containing a tyrosine showed the highest binding constants, with the central position in the Ac-AYA-NH2 peptide becoming the most favorite for the interaction. A combined NMR and Molecular Docking approach permitted to build detailed complex models, highlighting the stabilizing interactions of the neighboring amino acids backbone atoms with the upper rim of the β-CD.

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Section: Determination Of Binding Constant By Uv-vis Spectroscopycontrasting

confidence: 99%

Section: Resultsmentioning

confidence: 89%

Investigating the inclusion properties of aromatic amino acids complexing beta-cyclodextrins in model peptides

et al. 2015

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“…For the α-cyclodextrins the binding efficiency decreases in the sequence: phenylalanine ~ tryptophan > proline > isoleucine ~ tyrosine ~ histidine (52) while for the β-cyclodextrins the binding efficiency decreases: tryptophan > tyrosine > phenylalanine > proline > histidine > isoleucine (53). Both cyclodextrins changed the taste of the amino acids but there was no consistent suppression of bitterness.…”

Section: Delivery Systems To Mask Bitter Tastementioning

confidence: 99%

“…Both cyclodextrins changed the taste of the amino acids but there was no consistent suppression of bitterness. Cyclodextrins were capable of partially suppressing the bitterness of soy protein, soy protein hydrosylates (52, 53) and whey protein hydrosylates (54). …”

Section: Delivery Systems To Mask Bitter Tastementioning

confidence: 99%

Physical Approaches to Masking Bitter Taste: Lessons from Food and Pharmaceuticals

Coupland

Hayes

2014

Pharm Res

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Many drugs and desirable phytochemicals are bitter, and bitter tastes are aversive. Food and pharmaceutical manufacturers share a common need for bitterness-masking strategies that allow them to deliver useful quantities of the active compounds in an acceptable form and in this review we compare and contrast the challenges and approaches by researchers in both fields. We focus on physical approaches, i.e., micro- or nano-structures to bind bitter compounds in the mouth, yet break down to allow release after they are swallowed. In all of these methods, the assumption is the degree of bitterness suppression depends on the concentration of bitterant in the saliva and hence the proportion that is bound. Surprisingly, this hypothesis has only rarely been fully tested using a combination of adequate human sensory trials and measurements of binding. This is especially true in pharmaceutical systems, perhaps due to the greater experimental challenges in sensory analysis of drugs.

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“…β-Cyclodextrin (βCD) is the least expensive, most accessible, and generally the most useful CD, and is used especially to include molecules with aromatic rings in its structure. [6][7][8][9] . βCD has numerous pharmacological applications; for example, it increases the water solubility and decreases the toxicity of many substances by forming complexes.…”

Section: Introductionmentioning

confidence: 99%

Gold Nanoparticles Interacting with β-Cyclodextrin–Phenylethylamine Inclusion Complex: A Ternary System for Photothermal Drug Release

Sierpe

Lang

Jara

et al. 2015

ACS Appl. Mater. Interfaces

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We report the synthesis of a 1:1 β-cyclodextrin-phenylethylamine (βCD-PhEA) inclusion complex (IC) and the adhesion of gold nanoparticles (AuNPs) onto microcrystals of this complex, which forms a ternary system. The formation of the IC was confirmed by powder X-ray diffraction and NMR analyses ((1)H and ROESY). The stability constant of the IC (760 M(-1)) was determined using the phase solubility method. The adhesion of AuNPs was obtained using the magnetron sputtering technique, and the presence of AuNPs was confirmed using UV-vis spectroscopy (surface plasmon resonance effect), which showed an absorbance at 533 nm. The powder X-ray diffractograms of βCD-PhEA were similar to those of the crystals decorated with AuNPs. A comparison of the one- and two-dimensional NMR spectra of the IC with and without AuNPs suggests partial displacement of the guest to the outside of the βCD due to attraction toward AuNPs, a characteristic tropism effect. The size, morphology, and distribution of the AuNPs were analyzed using TEM and SEM. The average size of the AuNPs was 14 nm. Changes in the IR and Raman spectra were attributed to the formation of the complex and to the specific interactions of this group with the AuNPs. Laser irradiation assays show that the ternary system βCD-PhEA-AuNPs in solution enables the release of the guest.

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The use of 2D NMR to study β-cyclodextrin complexation and debittering of amino acids and peptides

Cited by 56 publications

References 31 publications

Investigating the inclusion properties of aromatic amino acids complexing beta-cyclodextrins in model peptides

Investigating the inclusion properties of aromatic amino acids complexing beta-cyclodextrins in model peptides

Physical Approaches to Masking Bitter Taste: Lessons from Food and Pharmaceuticals

Gold Nanoparticles Interacting with β-Cyclodextrin–Phenylethylamine Inclusion Complex: A Ternary System for Photothermal Drug Release

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