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Structural versatility of peptides from Cα,α-disubstituted glycines: crystal-state conformational analysis of peptides from Cα-methylhomophenylalanine, (αMe)Hph

✍ Scribed by DOI, MITSUNOBU ;ISHIDA, TOSHIMASA ;POLESE, ALESSANDRA ;FORMAGGIO, FERNANDO ;CRISMA, MARCO ;TONIOLO, CLAUDIO ;BROXTERMAN, QUIRINUS B. ;KAMPHUIS, JOHAN

Book ID
115099932
Publisher
Wiley (Blackwell Publishing)
Year
2009
Tongue
English
Weight
567 KB
Volume
47
Category
Article
ISSN
0367-8377

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Structural versatility of peptides from
Structural versatility of peptides from Cα,α-disubstituted glycines: Preferred conformation of the Cα,α-diphenylglycine residue
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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

Peptides from chiral Cα,α-disubstituted
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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],-