Oligosaccharide-Peptide Interaction. Binding of Maltodextrin to Trp-Trp via Sugar-Bisindole Intercalation

Otsuki, Jun-ichi; Kobayashi, Kenji; Toi, Hiroo; Aoyama, Yasuhiro

doi:10.1016/s0040-4039(00)91970-1

Cited by 31 publications

(14 citation statements)

References 15 publications

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“…The PIN–starch granule surface interaction may hypothetically involve the PIN Trp‐rich domain binding to the starch granule surface through hydrophobic parallel stacking of indole rings with glucose rings [32]. The substitution of one of the Trp residues in the PIN‐b Trp‐rich domain with an Arg residue will reduce the hydrophobicity of the Trp‐rich domain of PIN‐b considerably and may reduce not only the potential for hydrophobic stacking significantly but also the lipid‐binding ability of the protein.…”

Section: Discussionmentioning

confidence: 99%

Characterization of wheat puroindoline proteins

et al. 2006

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Puroindoline proteins were purified from selected UK‐grown hexaploid wheats. Their identities were confirmed on the basis of capillary electrophoresis mobilities, relative molecular mass and N‐terminal amino acid sequencing. Only one form of puroindoline‐a protein was found in those varieties, regardless of endosperm texture. Three allelic forms of puroindoline‐b protein were identified. Nucleotide sequencing of cDNA produced by RT‐PCR of isolated mRNA indicated that these were the ‘wild‐type’, found in soft wheats, puroindoline‐b containing a Gly→Ser amino acid substitution (position 46) and puroindoline‐b containing a Trp→Arg substitution (position 44). The latter two were found in hard wheats. Microheterogeneity, due to short extensions and/or truncations at the N‐terminus and C‐terminus, was detected for both puroindoline‐a and puroindoline‐b. The type of microheterogeneity observed was more consistent for puroindoline‐a than for puroindoline‐b, and may arise through slightly different post‐translational processing pathways. A puroindoline‐b allele corresponding to a Leu→Pro substitution (position 60) was identified from the cDNA sequence of the hard variety Chablis, but no mature puroindoline‐b protein was found in this or two other European varieties known to possess this puroindoline‐b allele. Wheats possessing the puroindoline‐b proteins with point mutations appeared to contain lower amounts of puroindoline protein. Such wheats have a hard endosperm texture, as do wheats from which puroindoline‐a or puroindoline‐b are absent. Our results suggest that point mutations in puroindoline‐b genes may confer hard endosperm texture through accumulation of allelic forms of puroindoline‐b proteins with altered functional properties and/or through lower amounts of puroindoline proteins.

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Section: Discussionmentioning

confidence: 99%

Characterization of wheat puroindoline proteins

et al. 2006

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“…More relevant is the simple dipeptide Trp-Trp 49 (Fig. 9) investigated by the Aoyama group [94] and inspired by the sandwiching of saccharides between aromatic surfaces in some lectins (e.g. Fig.…”

Section: Peptide-based Designsmentioning

confidence: 99%

Progress in biomimetic carbohydrate recognition

Walker

Joshi

Davis

2009

Cell. Mol. Life Sci.

109

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The importance of carbohydrate recognition in biology, and the unusual challenges involved, have lead to great interest in mimicking saccharide-binding proteins such as lectins. In this review, we discuss the design of artificial carbohydrate receptors, focusing on those which work under natural (i.e. aqueous) conditions. The problem is intrinsically difficult because of the similarity between substrate (carbohydrate) and solvent (water) and, accordingly, progress has been slow. However, recent developments suggest that solutions can be found. In particular, the "temple" family of carbohydrate receptors show good affinities and excellent selectivities for certain all-equatorial substrates. One example is selective for O-linked beta-N-acetylglucosamine (GlcNAc, as in the O-GlcNAc protein modification), while another is specific for beta-cellobiosyl and closely related disaccharides. Both show roughly millimolar affinities, matching the strength of some lectin-carbohydrate interactions.

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“…Titration data was consistent with 1:1 binding, but with K a values of just 1m À1 for 95 and 8 m À1 for 96. [76] A study employing CD spectroscopy revealed that bilirubin (98) can also associate with 95 and 96, as well as other di-and oligo-saccharides (but not glucose). [77] Cyclotetrachromotropylene (92) has been found to bind cyclodextrins, with K a 85 ± 140 m À1 .…”

Section: 32oligosaccharidesmentioning

confidence: 99%

Carbohydrate Recognition through Noncovalent Interactions: A Challenge for Biomimetic and Supramolecular Chemistry

Davis

Wareham

1999

Angew. Chem. Int. Ed.

480

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Carbohydrates are not always as "sticky" as one might expect. Even in organic solvents they are difficult targets for the supramolecular chemist, due to their complex, three-dimensional structures. In their natural environment (water) they are especially elusive, presenting challenges which will occupy synthetic and theoretical chemists for some time to come. The complex of an octaamide supramolecular receptor with beta-D-glucopyranose, which binds through apolar and polar contacts, is shown.

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Oligosaccharide-Peptide Interaction. Binding of Maltodextrin to Trp-Trp via Sugar-Bisindole Intercalation

Cited by 31 publications

References 15 publications

Characterization of wheat puroindoline proteins

Characterization of wheat puroindoline proteins

Progress in biomimetic carbohydrate recognition

Carbohydrate Recognition through Noncovalent Interactions: A Challenge for Biomimetic and Supramolecular Chemistry

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