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Miniaturized hemoproteins
Author(s) -
Nastri Flavia,
Lombardi Angela,
D'Andrea Luca D.,
Sanseverino Marina,
Maglio Ornella,
Pavone Vincenzo
Publication year - 1998
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1998)47:1<5::aid-bip3>3.0.co;2-y
Subject(s) - hemeprotein , chemistry , porphyrin , molecule , peptide , heme , combinatorial chemistry , covalent bond , molecular model , stereochemistry , biochemistry , organic chemistry , enzyme
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. © 1998 John Wiley & Sons, Inc. Biopoly 47: 5–22, 1998