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Hemoglobin as a Potential Source of Natural Regulatory Oligopeptides

A. A. Zamyatnin1,2

1Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, 119071 Moscow, Russia; fax: (495) 954-2732; E-mail: aaz@inbi.ras.ru

2Universidad Técnica Federico Santa Maria, Departamento de Informatica, av. Espaňa 1680, Valparaiso, Chile; fax: (5632) 279-7513; E-mail: alexander.zamyatnin@usm.cl

Received January 29, 2008; Revision received March 3, 2008
Theoretical structure–function analysis of all possible hemoglobin molecule fragments was performed to determine sites that could be potential sources of regulatory oligopeptides. Known data on bovine hemoglobin primary structure and information of the EROP-Moscow database concerning structure and functions of natural oligopeptides were used along with a computer program complex. A total of 6750 natural non-hemoglobin oligopeptides with hemoglobin fragments of 2-14 amino acid residues were found. Structures of 20 of them were completely identical to hemoglobin fragments. Most of the revealed oligopeptides exhibit properties of neuropeptides, antimicrobial agents, and hormones. A number of them exhibit functions previously not known for hemoglobin fragments. The possibility of natural formation of regulatory oligopeptides from hemoglobin and other food protein molecules, generation of the exogenous oligopeptide pool, their participation in regulation processes as well as accordance of results obtained here with the oligopeptide continuum concepts are discussed.
KEY WORDS: hemoglobin, fragment, neuropeptide, antimicrobial oligopeptide, EROP-Moscow database, continuum

DOI: 10.1134/S0006297909020114