Correlation between biological activity and conformational dynamics properties of tetra- and pentapeptides derived from fetoplacental proteins |
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Authors: | N T Moldogazieva A A Terentiev M Yu Antonov A N Kazimirsky K V Shaitan |
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Institution: | 1.Russian State Medical University,Moscow,Russia;2.Lomonosov Moscow State University,Moscow,Russia |
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Abstract: | In this work, using molecular dynamics simulation, we study conformational and dynamic properties of biologically active penta-
and tetrapeptides derived from fetoplacental proteins such as alpha-fetoprotein, pregnancy specific β1-glycoprotein, and carcinoembryonic
antigen. Existence of correlation between flexibility of peptide backbone and biological activity of the investigated peptides
was shown. It was also demonstrated that flexibility of peptide backbone depends not only on its length, but also on the presence
of reactive functional groups in amino acid side chains that participate in intramolecular interactions. Peptides that demonstrate
similar biological effects in regulation of proliferation of lymphocytes and expression of differentiation antigens on their
surface (LDSYQCT, PYECE, YECE, and YVCE) are characterized by rigidity of their peptide backbone. Increased backbone flexibility
in peptides PYQCE, YQCE, SYKCE, YQCT, YQCS, YVCS, YACS, and YACE is correlated with decreased biological activity. Conformational
mobility of amino acid residues does not depend on physicochemical properties only, but also on intramolecular interactions.
So, evolutionary restrictions should exist to maintain such interactions in the environment of functionally important sites. |
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