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Preferred conformation of peptides rich in Ac8c, a medium-ring alicyclic Cα,α-disubstituted glycine

✍ Scribed by Vittorio Moretto; Fernando Formaggio; Marco Crisma; Gian Maria Bonora; Claudio Toniolo; Ettore Benedetti; Antonello Santini; Michele Saviano; Benedetto Di Blasio; Carlo Pedone

Book ID
105360240
Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
983 KB
Volume
2
Category
Article
ISSN
1075-2617

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Preferred conformation of peptides rich
Preferred conformation of peptides rich in alicyclic Cα,α-disubstituted glycines
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The conformational preferences of the alicyclic C","-disubstituted glycines Ac,c (I-amino-I-cycloalkane-carboxylic acid; n = 4 , 7, 9, 1 2 ) were assessed in selected model compounds, including homopeptides and Ala (or Aib, a-aminoisobutyric acid)lAc,c peptides containing a small total number of res

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## Abstract The conformational preference of C^α,α^‐diphenylglycinc (Døg) and C^α,α^‐dibenzylglycine (Dbz) residues was assessed in selected derivatives and small peptides by conformational energy computations, ir absorption, ^1^H‐nmr, and x‐ray diffraction. Conformational energy computations on th

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## Abstract The preferred conformation of the C^α,α^‐diphenylglycine residue was determined in simple derivatives and dipeptides. The dipeptides were synthesized by the 5(4__H__)‐oxazolone (from the N‐__para__‐bromobenzoylated amino acid) method. This activated intermediate and a reaction by‐produc

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The molecular structures of four protected isovaline-(Iva-)containing peptides to the pentamer level have been determined by x-ray diffraction. The peptides are t-Boc-Ala-( S ) -1va-Ala-OMe ( t-Boc : tert-butyloxycarbonyl; OMe : methoxy) and its ( R ) -1va diastereomer, and t-Boc-[ Ala-( R ) -Iva],-

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A series of N-and C-protected, monodispersed homo-oligopeptides (to the pentamer level) from the cycloaliphatic C Y -dialkylated glycine 1-aminocyclononane-1-carboxylic acid (Ac W c) and two Ala/Ac W c tripeptides have been synthesized by solution methods and fully characterized. The conformational