Conformationally constrained histidines in the design of peptidomimetics: Strategies for the χ-space control

36Citations
Citations of this article
36Readers
Mendeley users who have this article in their library.

Abstract

A successful design of peptidomimetics must come to terms with χ-space control. The incorporation of χ-space constrained amino acids into bioactive peptides renders the χ1 and χ2 torsional angles of pharmacophore amino acids critical for activity and selectivity as with other relevant structural features of the template. This review describes histidine analogues characterized by replacement of native α and/or β-hydrogen atoms with alkyl substituents as well as analogues with α, β-didehydro unsaturation or Cα-Cβ cyclopropane insertion (ACC derivatives). Attention is also dedicated to the relevant field of β-aminoacid chemistry by describing the synthesis of β2- and β3-models (β-hHis). Structural modifications leading to cyclic imino derivatives such as spinacine, aza-histidine and analogues with shortening or elongation of the native side chain (nor-histidine and homo-histidine, respectively) are also described. Examples of the use of the described analogues to replace native histidine in bioactive peptides are also given. © 2011 by the authors.

Cite

CITATION STYLE

APA

Stefanucci, A., Pinnen, F., Feliciani, F., Cacciatore, I., Lucente, G., & Mollica, A. (2011). Conformationally constrained histidines in the design of peptidomimetics: Strategies for the χ-space control. International Journal of Molecular Sciences, 12(5), 2853–2890. https://doi.org/10.3390/ijms12052853

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free