Miniaturized hemoproteins

Biopolymers. 1998;47(1):5-22. doi: 10.1002/(SICI)1097-0282(1998)47:1<5::AID-BIP3>3.0.CO;2-Y.

Abstract

The present paper highlights and reviews current research in the field of hemoprotein models. Hemoproteins have been extensively studied in order to understand structure-function relationships, and to design new molecules with desired functions. A wide number of synthetic analogues have been developed, using quite different approaches. They differ in molecular structures, ranging from simple meso-substituted tetraaryl-metalloporphyrins and peptide-porphyrin conjugates. In this paper we summarize the state of the art on peptide based hemoprotein models. We also report here the approach used by us to develop a new class of molecules, named mimochromes. They can be regarded as miniaturized hemoproteins, because mimochromes are low molecular weight compounds with some structural and functional properties common to those of the parent high molecular weight protein. The basic structure of mimochromes is a deuteroporphyrin ring covalently linked to two helical peptide chains. Two molecules of this series have been fully characterized. All the information derived from their structural analysis has been applied to the design of new analogues with additional functions.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Biopolymers / chemistry
  • Drug Design
  • Hemeproteins / chemical synthesis
  • Hemeproteins / chemistry*
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Porphyrins / chemical synthesis
  • Porphyrins / chemistry

Substances

  • Biopolymers
  • Hemeproteins
  • Porphyrins