A topographically and conformationally constrained, spin-labeled, alpha-amino acid: crystallographic characterization in peptides.

Department of Chemistry, Institute of Biomolecular Chemistry, CNR, University of Padova, 35131 Padova, Italy.
European Journal of Allergy and Clinical Immunology (Impact Factor: 1.3). 07/2005; 65(6):564-79. DOI: 10.1111/j.1399-3011.2005.00258.x
Source: PubMed

ABSTRACT 2,2,6,6-Tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) is a topographically and conformationally restricted, nitroxide containing, C(alpha)-tetrasubstituted alpha-amino acid. Here, we describe the molecular and crystal structures, as determined by X-ray diffraction analyses, of a TOAC terminally protected derivative, the cyclic dipeptide c(TOAC)(2).1,1,1,3,3,3-hexafluoropropan-2-ol (HFIP) solvate, and five TOAC-containing, terminally protected, linear peptides ranging in length from tetra- to hepta-peptides. Incipient and fully developed, regular or distorted 3(10)-helical structures are formed by the linear peptides. A detailed discussion on the average geometry and preferred conformation for the TOAC piperidine ring is also reported. The X-ray diffraction structure of an intramolecularly cyclized side product resulting from a C-activated TOAC residue has also been determined.

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