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The influence of modification at position 2 on the side-chain conformation in oxytocin analogs

100%
Śmiech B., Kaźmierkiewicz R., Lammek B.
Acta Biochimica Polonica
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2006
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vol. 53
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issue 1
113-120
EN
The nonapeptide oxytocin (OT) is used in medicine to help begin and/or continue childbirth. Its analogs can be also used to control bleeding following fetus delivery. The main function of oxytocin is to stimulate contraction of uterus smooth muscle and the smooth muscle of mammary glands, thus regulating lactation. This paper describes theoretical simulations of the distribution of the torsional angles χ1 in the non-standard methylated phenylalanine residues of three oxytocin analogs: [(Phe)2o-Me]OT, [(Phe)2m-Me]OT, [(Phe)2p-Me]OT. The conformations of the oxytocin analogs were studied both in vacuum and in solution. We found some correlations between the biological activity of the considered peptides and the side-chain conformations of amino-acid residues 2 and 8.
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Solution structure of conformationally restricted vasopressin analogues.

100%
Trzepałka E., Oleszczuk M., Maciejczyk M., Lammek B.
Acta Biochimica Polonica
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2004
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vol. 51
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issue 1
33-49
EN
In recent years, a massive effort has been directed towards designing potent and selective antagonists of neurohypophyseal hormones substituted at position 3. Modification of vasopressin at position 3 with 4,4'-biphenylalanine results in pharmacologically inactive analogues. Chemically, this substitution appears to vary only slightly from those previously made by us (1-Nal or 2-Nal), which afforded potent agonists of V2 receptors. In this situation, it seemed worthwhile to study the structure of the analogues with 4,4'-biphenylalanine (BPhe) at position 3 in aqueous solution using NMR spectroscopy and total conformational analysis. This contribution is part of extensive studies aimed at understanding spatial structures of 3-substituted [Arg8]vasopressin analogues of different pharmacological properties. NMR data were used to calculate 3D structures for all the analogues using two methods, EDMC with the ECEPP/3 force field, and molecular dynamic with the simulated annealing (SA) algorithm. The structures obtained by the first method show a better fit between the NMR spectral evidence and the calculation for all the peptides.
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Molecular docking-based test for affinities of two ligands toward vasopressin and oxytocin receptors.

88%
Ślusarz R., Kaźmierkiewicz R., Giełdoń A., Lammek B., Ciarkowski J.
Acta Biochimica Polonica
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2001
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vol. 48
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issue 1
131-135
EN
Molecular docking simulations are now fast developing area of research. In this work we describe an effective procedure of preparation of the receptor-ligand complexes. The amino-acid residues involved in ligand binding were identified and described.
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