Conformational Analysis of Constrained Dilactam-bridged Tetrapeptides
1988; Elsevier BV; Volume: 44; Issue: 3 Linguagem: Inglês
10.1016/s0040-4020(01)86125-1
ISSN1464-5416
AutoresRebecca Rone, Nick J. Manesis, Moises Hassan, Murray Goodman, A. T. Hagler, David H. Kitson, Victoria A. Roberts,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoIn order to probe constrained regions in polypeptides, a series of lactambridged derivatives were prepared: Our approach has been to limit mobility of the peptide backbone by coupling side chains on adjacent residues. This allows rotation about the torsion angles ψ2 and φ3 in the tetrapeptides. These model compounds, therefore, can mimic turns in polypeptides. The conformations of these peptides has been investigated by circular dichroism and nuclear magnetic resonance spectroscopy as well as via molecular dynamics simulations and energy minimization calculations. The results from these studies are consistent with the presence of a β-turn in the “LLDD LysGlu” tetrapeptide (compound 1) and with a variety of C7 structures for the other tetrapeptides (compounds 2, 4, and 5).
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