The crystal structure of Afc-containing peptides

Lombardi, Angela; Simone, Giuseppina De; Galdiero, Stefania; Nastri, Flavia; Costanzo, Luigi Di; Makihira, Kazunari; Yamada, Takashi; Pavone, Vincenzo

doi:10.1002/(sici)1097-0282(200002)53:2<150::aid-bip5>3.0.co;2-c

Cited by 15 publications

(16 citation statements)

References 54 publications

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“…The onset of a folded structure by Hms(Ipr) (O,O‐isopropylidene‐C α ‐hydroxymethylserine) (Figure 8) containing compounds may be prevented by (peptide) N i +1 H … O

_{γ}^{italici}

(side‐chain ether) intramolecular H‐bonds, thus favoring the fully extended conformation (Figure 11). 134 The related Afc (9‐amino‐9‐fluorenecarboxylic acid)135–137 and Daf (9‐amino‐4,5‐diazafluorene‐9‐carboxylic acid)138 residues (Figure 8), by virtue of their central five‐membered ring (as in Ac 5 c) and the two aromatic moieties directly linked to the α‐carbon (as in DΦg), may adopt either the turn/helical or the fully extended conformation. The fully extended conformation of these residues is more frequently observed in amino acid derivatives and very short peptides.…”

Section: Discussionmentioning

confidence: 99%

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

et al. 2001

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The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by conformational energy computations, crystal‐state (x‐ray diffraction) analyses, and solution (1H‐NMR and spectroscopic) investigations, are reviewed. It is concluded that 310/α‐helical structures and the fully extended (C5) conformation are preferentially adopted by peptide sequences characterized by this family of amino acids, depending upon overall bulkiness and nature (e.g., whether acyclic or C αi ↔ C αitalici cyclized) of their side chains. The intriguing relationship between α‐carbon chirality and bend/helix handedness is also illustrated. γ‐Bends and semiextended conformations are rarely observed. Formation of β‐sheet structures is prevented. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 396–419, 2001

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“…The onset of a folded structure by Hms(Ipr) (O,O‐isopropylidene‐C α ‐hydroxymethylserine) (Figure 8) containing compounds may be prevented by (peptide) N i +1 H … O

_{γ}^{italici}

Section: Discussionmentioning

confidence: 99%

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

et al. 2001

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“…1 Consequently, design of conformational constrained peptides is one of the approaches for development of bioactive species with high activity and selectivity towards a specific receptor. 2,3 Owing to steric crowding within the neighbourhood of the α-carbon atom of α,αdialkyl glycines, conformational rigidity can be obtained by inserting one or more residue of these amino acids into the peptide chain. In addition, special conformational features imparted to the peptide backbone by these amino acid residues 4-7 may be used to modulate activity and selectivity.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and kinetic investigation of the selective acidolysis of para-substituted N-benzyl- or N-phenyl-N-phenylacetyl-α,α-dialkylglycine cyclohexylamides

Pinto¹,

Pereira-Lima²,

Ventura³

et al. 2006

Tetrahedron

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Several derivatives of N-phenylacetyl-N-benzyl-α,α-dimethylglycine cyclohexylamide and their α,α-dibenzylglycine analogues were synthesised by a Ugi-Passerini reaction. In addition, a few analogues of the former but having an N-phenyl instead of a benzyl group at the nitrogen atom were synthesised. The compounds in each of these three sets differed from each other at the position 4 of the N-benzyl (and N-phenyl) group. These adducts were submitted to acidolysis with TFA to obtain the corresponding free acids, the reactions being monitored by HPLC and data collected for kinetic purposes. The kinetic data were submitted to Hammett uni-and biparametric relationships and the results analysed in terms of structure-reactivity in connection to the sensitivity of the reaction rates to the electronic contributions of the various substituents in position 4 of the aromatic rings. The results allowed comparison with information obtained in previous investigations and rationalise the contribution of the substituent at the nitrogen atom to the lability of the C-terminal amide bond.

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“…This conformational rigidity is a requirement to increase potency and selectivity, to improve bioavailabitlity, and to enhance the resistance to peptidases. 1 In addition, the design of conformational constrained sequences is one of the approaches for development of bioactive peptides with high activity and selectivity towards a specific receptor. 2 Deltorfin and Leuenkephalin analogues containing α,α-dialkyl glycine residues are examples of this strategy.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Conformational Investigation of Tetrapeptide Analogues of the Fragment B23‐B26 of Insulin.

2004

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The crystal structure of Afc-containing peptides

Cited by 15 publications

References 54 publications

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Synthesis and kinetic investigation of the selective acidolysis of para-substituted N-benzyl- or N-phenyl-N-phenylacetyl-α,α-dialkylglycine cyclohexylamides

Synthesis and Conformational Investigation of Tetrapeptide Analogues of the Fragment B23‐B26 of Insulin.

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