Intramolecular host-guest complexes of D- and L-mono-6-phenylalanyl-amino-6-deoxy cyclomalto-heptaoses

Parrot‐Lopez, Hélène; Galons, Hervé; Coleman, Anthony W.; Djedaïni, Florence; Keller, N.; Perly, Bruno

doi:10.1016/0957-4166(90)90035-9

Cited by 43 publications

(16 citation statements)

References 9 publications

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“…Mono-attachment of the peptide moiety to the symmetric cyclodextrin molecule via the succinyl spacer leads to an asymmetric cyclodextrin derivative with concomitant partial resolution of the resonances in the 1D 1H-NMR spectrum. This dispersion may, therefore, not necessarily reflect self-inclusion of the peptide as suggested previously in mono-derivatized cyclodextrins [29,30]. The NOESY spectra in both solvents and the ROESY spectrum in water show sequential NH-CHtx, NH-side-chain and NH-spacer NOEs (ROEs) within the peptide chain and the spacer residue.…”

Section: Resultsmentioning

confidence: 91%

Cyclodextrins as templates for the presentation of protease inhibitors

Schaschke¹,

Hj²,

Assfalg-Machleidt³

et al. 1996

FEBS Letters

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Mono(6-succinylamido-6-deoxy)-13-cyclodextrin was synthesized by classical carbohydrate chemistry and used as a template mono-functionalized with the linear, fully flexible 4C-spacer carboxylate for covalent linkage of the calpain inhibitor leucyl-leucyl-norleucinal. Spectroscopic analyses of the conjugate do not support a self-inclusion of part of the hydrophobic peptide tail, but confirm its intra-or intermolecular interaction with the template moiety that leads to full water solubility. The inhibitory potency of the ~-cyclodextrin/peptide aldehyde construct was compared with that of the parent Ac-Leu-Leu-Nle-H against cathepsin B and calpain. Despite the large size of the template the inhibition of cathepsin B was only slightly reduced in full agreement with the X-ray structure of this enzyme which shows full accessibility of the S-subsites. For this enzyme the 4C-spacer is apparently sufficient to guarantee optimal interaction of the peptide tail with the binding cleft. Conversely, for gcalpain a significantly decreased inhibitory potency was obtained with the conjugate suggesting steric interference of the template in the binding process. These results show that the beneficial properties of the cyclodextrin template can be retained in conjugates with bioactive peptides if attention is paid to optimize in each case the size and nature of the spacer for optimal recognition of the grafted biomolecule.

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Section: Resultsmentioning

confidence: 91%

Cyclodextrins as templates for the presentation of protease inhibitors

Schaschke¹,

Hj²,

Assfalg-Machleidt³

et al. 1996

FEBS Letters

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“…l o For 4, the band at 225 nm arising from the tryptophan residue was observed; in Borneo1 Fig. 6 Postulated hydrogen-bonded binary complex between 3 and borneol the case of 4 alone a positive band was observed, while in the presence of borneol the intensity of this band was strongly diminished and a second negative band at 200 nm appears. This is consistent with the tryptophan residue being displaced from the cavity.…”

Section: 6mentioning

confidence: 92%

Fluorescent amino acids as reporter systems in peptido-cyclodextrin inclusion compounds

Eddaoudi¹,

Parrot‐Lopez²,

Lamotte³

et al. 1996

J. Chem. Soc., Perkin Trans. 2

Self Cite

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“…Several different types of covalent peptidecyclodextrin conjugates have been reported. Among the first were publications by Parrot-Lopez et al on the preparation of cyclodextrins singly substituted with amino acids [67][68][69] or peptides, 70 by Vecchio 76 and coworkers in 1992, Å kerfeldt and DeGrado 81 in 1994, Hanessian 79 and coworkers in 1995, Moroder 83 and coworkers and Stoddart 80 in separate publications in 1996. cyclodextrins have been used extensively in the de novo design of potential, biomimetic catalysts. However, in general, these designs do not incorporate peptides as such, with a few exceptions.…”

Section: Cyclo-dextrin-peptide Conjugatesmentioning

confidence: 99%

Carbohydrates in peptide and protein design

Jensen¹,

Brask²

2005

Biopolymers

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Monosaccharides and amino acids are fundamental building blocks in the assembly of nature's polymers. They have different structural aspects and, to a significant extent, different functional groups. Oligomerization gives rise to oligosaccharides and peptides, respectively. While carbohydrates and peptides can be found conjoined in nature, e.g., in glycopeptides, the aim of this review is the radical redesign of peptide structures using carbohydrates, particularly monosaccharides and cyclic oligosaccharides, to produce novel peptides, peptidomimetics, and abiotic proteins. These hybrid molecules, chimeras, have properties arising largely from the combination of structural characteristics of carbohydrates with the functional group diversity of peptides. This field includes de novo designed synthetic glycopeptides, sugar (carbohydrate) amino acids, carbohydrate scaffolds for nonpeptidal peptidomimetics of cyclic peptides, cyclodextrin functionalized peptides, and carboproteins, i.e., carbohydrate-based proteinmimetics. These successful applications demonstrate the general utility of carbohydrates in peptide and protein architecture. #

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Intramolecular host-guest complexes of D- and L-mono-6-phenylalanyl-amino-6-deoxy cyclomalto-heptaoses

Cited by 43 publications

References 9 publications

Cyclodextrins as templates for the presentation of protease inhibitors

Cyclodextrins as templates for the presentation of protease inhibitors

Fluorescent amino acids as reporter systems in peptido-cyclodextrin inclusion compounds

Carbohydrates in peptide and protein design

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