Conformations of a model cyclic hexapeptide, CYIQNC: ¹H-NMR and molecular dynamics studies

References

• Aue, W. P., Bartholidi, E., & Ernst, R. R. (1976). Two dimensional spectroscopy: Application to nuclear magnetic resonance. The Journal of Chemical Physics, 64, 2229–2246. doi:10.1063/1.43245010.1063/1.432450
   Web of Science ®Google Scholar
• Ballardin, A., Fischman, A. J., Gibbons, W. A., Roy, J., Schwartz, I. L., Smith, C. W., … Wyssbrod, H. R. (1978). Conformational studies on [Pro3,Gly4]-oxytocin in dimethyl sulfoxide by proton nuclear magnetic resonance spectroscopy: Evidence for a type II β turn in the cyclic moiety. Biochemistry, 17, 4443–4454. doi:10.1021/bi00614a01410.1021/bi00614a014
   PubMed Web of Science ®Google Scholar
• Barth, T., Rychlík, I., Zaoral, M., & Cort, J. H. (1974). Antidiuretic activity of oxytocin-1,6-hexapeptides (tocinoic acid and amide) in the rat. Endocrinologia Experimentalis, 8, 45–50. Retrieved from PMID: 4547704
   PubMedGoogle Scholar
• Bax, A., & Davis, D. G. (1985). MLEV-17 based two-dimensional homonuclear magnetism transfer spectroscopy. Journal of Magnetic Resonance, 65, 355–360. Retrieved from http://spin.niddk.nih.gov/bax/lit/spdf/62.pdf
   Web of Science ®Google Scholar
• Bélec, L., Blankenship, J. W., & Lubell, W. D. (2005). Examination of structural characteristics of the potent oxytocin antagonists [dPen1,Pen6]-OT and [dPen1,Pen6, 5-tBuPro7]-OT by NMR, raman, CD spectroscopy and molecular modeling. Journal of Peptide Science, 11, 365–378. doi:10.1002/psc.637.10.1002/(ISSN)1099-1387
   PubMed Web of Science ®Google Scholar
• Bhaskaran, R., Chuang, C., & Yu, C. (1992). Conformational properties of oxytocin in dimethyl sulfoxide solution: NMR and restrained molecular dynamics studies. Biopolymers, 32, 1599–1608. doi:10.1002/bip.36032120310.1002/(ISSN)1097-0282
   PubMed Web of Science ®Google Scholar
• Blumenstein, M., Hruby, V. J., Viswanatha, V., & Chaturvedi, D. (1984). Carbon-13 chemical shifts on oxytocin as a consequence of its interaction with neurophysins. Biochemistry, 23, 2153–2161. doi:10.1021/bi00305a00810.1021/bi00305a008
   PubMed Web of Science ®Google Scholar
• Braunshweiler, L., & Ernst, R. R. (1983). Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. Journal of Magnetic Resonance, 53, 521–528. doi:10.1016/0022-2364(83)90226-3
   Web of Science ®Google Scholar
• Brewster, A. I. R., & Hruby, V. J. (1973). 300-MHz nuclear magnetic resonance study of oxytocin in aqueous solution: Conformational implications. Proceedings of the National Academy of Sciences, 70, 3806–3809. Retrieved from http://www.pnas.org/content/70/12/3806.abstract?sid=79ed8963-b563-402c-936d-9288be63e50910.1073/pnas.70.12.3806
   PubMed Web of Science ®Google Scholar
• Brewster, A. I. R., Hruby, V. J., Glasel, J. A., & Tonelli, A. E. (1973). Proposed conformations of oxytocin and selected analogs in dimethyl sulfoxide as deduced from proton magnetic resonance studies. Biochemistry, 12, 5294–5304. doi:10.1021/bi00750a01210.1021/bi00750a012
   PubMed Web of Science ®Google Scholar
• Budesínsky, M., Procházka, Z., & Slaninová, J. (2005). Oxytocin and its analogs, methyl-substituted in ortho-, meta- or para- position of aromatic ring of phenylalanine in position 2: NMR study and biological activities. Protein and Peptide Letters, 12, 343–347. doi: 10.2174/092986605376575210.2174/0929866053765752
   PubMed Web of Science ®Google Scholar
• Carnazzi, E., Aumelas, A., Mouillac, B., Breton, C., Guillou, L., Barberis, C., & Seyer, R. (2001). Design, synthesis and pharmacological characterization of a potent radioiodinated and photoactivatable peptidic oxytocin antagonist. Journal of Medicinal Chemistry, 44, 3022–3030. doi:10.1021/jm010125u10.1021/jm010125u
   PubMed Web of Science ®Google Scholar
• Constantine, K. L., Friedricks, M. S., & Stouch, T. R. (1996). Extensive molecular dynamics simulation of a β-hairpin forming peptide. Biopolymers, 39, 591–614. doi:10.1002/(SICI)1097-0282(199610)39::4<591:AID-BIP9>3.0.CO;2-S
   Web of Science ®Google Scholar
• Cowburn, D., Live, D. H., Fischman, A. J., & Agosta, W. D. (1983). Side chain conformations of oxytocin and vasopressin studied by NMR observation of isotopic isomers. Journal of the American Chemical Society, 105, 7435–7442. doi:10.1021/ja00363a03810.1021/ja00363a038
   Web of Science ®Google Scholar
• Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A., & Wright, P. K. (1988). Folding of immunogenic peptide fragments of proteins in water solution. Journal of Molecular Biology, 201, 161–200. doi:10.1016/0022-2836(88)90446-910.1016/0022-2836(88)90446-9
   PubMed Web of Science ®Google Scholar
• Efimov, A. V. (1993). Standard structures in proteins. Progress in Biophysics and Molecular Biology, 60, 201–239. doi:10.1016/0079-6107(93)90015-C10.1016/0079-6107(93)90015-C
   PubMed Web of Science ®Google Scholar
• Eubanks, S., Lu, M., Peyton, D., & Breslow, E. (1999). Expression, folding, and thermodynamic properties of the bovine oxytocin–neurophysin precursor: Relationships to the intermolecular oxytocin–neurophysin complex. Biochemistry, 38, 13530–13541. doi:10.1021/bi991295010.1021/bi9912950
   PubMed Web of Science ®Google Scholar
• Feeney, J., Roberts, G. C. K., Rockey, J. H., & Burgen, A. S. V. (1971). Conformational studies of oxytocin and lysine vasopressin in aqueous solution using high resolution NMR spectroscopy. Nature New Biology, 232, 108–110. doi:10.1038/newbio232108a010.1038/newbio232108a0
   PubMedGoogle Scholar
• Gibson, K. D., & Scheraga, H. A. (1967). Minimization of polypeptide energy. II. Preliminary structures of oxytocin, vasopressin, and an octapeptide from ribonuclease. Proceedings of the National Academy of Sciences, 58, 1317–1323. Retrieved from http://www.pnas.org/content/58/4/1317.full.pdf10.1073/pnas.58.4.1317
   PubMed Web of Science ®Google Scholar
• Gimpl, G., & Fahrenholz, F. (2001). The oxytocin receptor system: structure, function, and regulation. Physiological Review, 2, 629–683. Retrieved from http://physrev.physiology.org/content/physrev/81/2/629.full.pdf
   Google Scholar
• Glickson, J. D., Rowan, R., Pitner, T. P., Dadok, J., Bothner-By, A. A., & Walter, R. (1976). Proton nuclear magnetic resonance double resonance study of oxytocin in aqueous solution. Biochemistry, 15, 1111–1119. doi:10.1021/bi00650a02510.1021/bi00650a025
   PubMed Web of Science ®Google Scholar
• Glickson, J. D., Urry, D. W., & Walter, R. (1972). Method for correlation of proton magnetic resonance assignments in different solvents: Conformational transition of oxytocin and lysine vasopressin from dimethylsulfoxide to Water. Proceedings of the National Academy of Sciences, 69, 2566–2569. Retrieved from http://www.pnas.org/content/69/9/2566.abstract10.1073/pnas.69.9.2566
   PubMed Web of Science ®Google Scholar
• Griensinger, C., Sorensen, O. W., & Ernst, R. R. (1985). Two dimensional correlation of connected NMR transitions. Journal of the American Chemical Society, 107, 6394–6396. doi:10.1021/ja00308a04210.1021/ja00308a042
   Web of Science ®Google Scholar
• Hruby, V. J. (1987). Implications of the X-ray structure of deamino-oxytocin to agonist/antagonist–receptor interactions. Trends in Pharmacological Sciences, 8, 336–339. doi:10.1016/0165-6147(87)90142-810.1016/0165-6147(87)90142-8
   Web of Science ®Google Scholar
• Johnson, L. F., Schwartz, I. L., & Walter, R. (1969). Oxytocin and neurohypophyseal peptides: Spectral assignment and conformational analysis by 220 MHz nuclear magnetic resonance. Proceedings of the National Academy of Sciences, 64, 1269–1275. Retrieved from http://www.pnas.org/content/64/4/1269.abstract
   PubMed Web of Science ®Google Scholar
• Kato, T., Endo, S., Fujiwara, T., & Nagayama, K. (1993). Oxytocin solution structure changes upon protonation of the N-terminus in dimethyl sulfoxide. Journal of Biomolecular NMR, 3, 653–673. doi:10.1007/BF00198370
   PubMed Web of Science ®Google Scholar
• van Kesteren, R. E., Smit, A. B., Dirks, R. W., de With, N. D., Geraerts, W. P., & Joosse, J. (1992). Evolution of the vasopressin/oxytocin superfamily: Characterization of a cDNA encoding a vasopressin-related precursor, preproconopressin, from the mollusc Lymnaea stagnalis. Proceedings of the National Academy of Sciences, 89, 4593–4597. doi:10.1073/pnas.89.10.459310.1073/pnas.89.10.4593
   PubMed Web of Science ®Google Scholar
• Kotelchuck, D., Scheraga, H. A., & Walter, R. (1972). Conformational energy studies of oxytocin and its cyclic moiety. Proceedings of the National Academy of Sciences, 69, 3629–3633. Retrieved from http://www.pnas.org/content/69/12/3629.abstract10.1073/pnas.69.12.3629
   PubMed Web of Science ®Google Scholar
• Kumar, A., Ernst, R. R., & Wuthrich, K. (1980). A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton–proton cross-relaxation networks in biological macromolecules. Biochemical and Biophysical Research Communications, 95, 1–6. doi:10.1016/0006-291X(80)90695-610.1016/0006-291X(80)90695-6
   PubMed Web of Science ®Google Scholar
• Lebl, M., Hill, P., Kazmierski, W., Kárászová, L., Slaninová, J., Fric, I., & Hruby, V. J. (1990). Conformationally restricted analogues of oxytocin; Stabilization of inhibitory conformation. International Journal of Peptide and Protein Research, 36, 321–330. doi:10.1111/j.1399-3011.1990.tb01289.x
   PubMedGoogle Scholar
• Lewis, P. N., Momany, F. A., & Scheraga, H. A. (1973). Chain reversals in proteins. Biochemica et Biophysica Acta, 303, 211–229. doi: 10.1016/0005-2795(73)90350-410.1016/0005-2795(73)90350-4
   PubMed Web of Science ®Google Scholar
• Lippens, G., Hallenga, K., Van Belle, D., Wodak, S. J., Nirmala, N. R., Hill, P., … Hruby, V. J. (1993). Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I. Biochemistry, 32, 9423–9434. doi:10.1021/bi00087a02210.1021/bi00087a022
   PubMed Web of Science ®Google Scholar
• Live, D. H., Cowburn, D., & Breslow, E. (1987). Binding of oxytocin and 8-arginine-vasopressin to neurophysin studied by nitrogen-15 NMR using magnetization transfer and indirect detection via protons. Biochemistry, 26, 6415–6422. doi:10.1021/bi00394a01810.1021/bi00394a018
   PubMed Web of Science ®Google Scholar
• Liwo, A., Tempczyk, A., & Grzonka, Z. (1989). Molecular mechanics calculations on deaminooxytocin and on deamino-arginine-vasopressin and its analogues. Journal of Computer-Aided Molecular Design, 2, 281–309. doi:10.1007/BF0153299110.1007/BF01532991
   PubMed Web of Science ®Google Scholar
• Liwo, A., Tempczyk, A., Oldziej, S., Shenderovich, M. D., Hruby, V. J., & Talluri, S. (1996). Exploration of the conformational space of oxytocin and arginine-vasopressin using the electrostatically driven monte carlo and molecular dynamics methods. Biopolymers, 38, 157–175. doi:https://doi.org/10.1002/(SICI)1097-0282(199602)38:2<157:AID-BIP3>3.0.CO;2-U
   PubMed Web of Science ®Google Scholar
• Lubecka, E. A., Sikorska, E., Marcinkowska, A., & Ciarkowski, J. (2014). Conformational studies of neurohypophyseal hormones analogues with glycoconjugates by NMR spectroscopy. Journal of Peptide Science, 20, 406–414. doi:10.1002/psc.262810.1002/psc.v20.6
   PubMed Web of Science ®Google Scholar
• Manning, M., Coy, E., & Sawyer, W. H. (1970). Solid-phase synthesis of (4-threonine)-oxytocin. A more potent and specific oxytocic agent than oxytocin. Biochemistry (Moscow), 9, 3925–3930. doi:10.1021/bi00822a010
   Web of Science ®Google Scholar
• Manning, M., Coy, E., & Sawyer, W. H. (1977). Relative conformational rigidity in oxytocin and (1-penicillamine)-oxytocin: A proposal for the relationship of conformational flexibility to peptide hormone agonism and antagonism. Proceedings of the National academy of Sciences of the United States of America, 74, 1373–1377. Retrieved from http://www.pnas.org/content/74/4/1373.abstract
   PubMed Web of Science ®Google Scholar
• Mosberg, H. I., Hruby, V. J., & Meraldi, J. P. (1981). Conformational study of the potent peptide hormone antagonist [1-penicillamine,2-leucine]oxytocin in aqueous solution. Biochemistry, 20, 2822–2828. doi:10.1021/bi00513a01810.1021/bi00513a018
   PubMed Web of Science ®Google Scholar
• Newschaffer, C. J., Croen, L. A., Daniels, J., Giarelli, E., Grether, J. K., Levy, S. E., … Windham, G. C. (2007). The epidemiology of autism spectrum disorders. Annual Review of Public Health, 28, 235–258. doi:10.1146/annurev.publhealth.28.021406.14400710.1146/annurev.publhealth.28.021406.144007
   PubMed Web of Science ®Google Scholar
• Nikiforovich, G. V., Leonova, V. I., Galaktionov, S. G., & Chipens, G. I. (1979). Theoretical conformational analysis of oxytocin molecule. International Journal of Peptide and Protein Research, 13, 363–373. doi:10.1111/j.1399-3011.1979.tb01894.x
   PubMedGoogle Scholar
• NMRchitect 95.0. (1995). Molecular simulations package. Biosym Technologies: San Diego.
   Google Scholar
• Ohno, A., Kawasaki, N., Okuda, H., & Yamaguchi, H. (2010). Complete NMR analysis of oxytocin in phosphate buffer. Magnetic Resonance in Chemistry, 48, 168–172. doi:10.1002/mrc.2557
   PubMed Web of Science ®Google Scholar
• Parent, A. S., Rasier, G., Matagne, V., Lomniczi, A., Lebrethon, M. C., Gérard, A., … Bourguignon, J. P. (2008). Oxytocin facilitates female sexual maturation through a glia-to-neuron signaling pathway. Endocrinology, 149, 1358–1365. doi:10.1210/en.2007-105410.1210/en.2007-1054
   PubMed Web of Science ®Google Scholar
• Pedersen, C. A., Ascher, J. A., Monroe, Y. L., & Prange, A. J., Jr (1982). Oxytocin induces maternal behaviour in virgin female rats. Science, 216, 648–650. doi:10.1126/science.707160510.1126/science.7071605
   PubMed Web of Science ®Google Scholar
• Postina, R., Kojro, E., & Fahrenholz, F. (1996). Separate agonist and peptide antagonist binding sites of the oxytocin receptor defined by their transfer into the V2 vasopressin receptor. Journal of Biological Chemistry, 271, 31593–31601. doi:10.1074/jbc.271.49.3159310.1074/jbc.271.49.31593
   PubMed Web of Science ®Google Scholar
• Ramachandran, G. N., & Sasisekharan, V. (1968). Conformation of polypeptides and proteins. Advances in Protein Chemistry, 23, 283–437. Retrieved from 10.1016/S0065-323310.1016/S0065-3233(08)60402-7
   PubMedGoogle Scholar
• Rettori, V., Canteros, G., Renoso, R., Gimeno, M., & McCann, S. M. (1997). Oxytocin stimulates the release of luteinizing hormone-releasing hormone from medial basal hypothalamic explants by releasing nitric oxide. Proceedings of the National Academy of Sciences, 94, 2741–2744. doi:10.1073/pnas.94.6.274110.1073/pnas.94.6.2741
   PubMed Web of Science ®Google Scholar
• Rodziewicz-Motowidlo, S., Sikorska, E., Oleszczuk, M., & Czaplewski, C. (2008). Conformational studies of vasopressin and mesotocin using NMR spectroscopy and molecular modelling methods. Part II: Studies in the SDS micelle. Journal of Peptide Science, 14, 85–96. doi:10.1002/psc.91710.1002/(ISSN)1099-1387
   PubMed Web of Science ®Google Scholar
• Rose, J. P., Wu, C. K., Hsiao, C. D., Breslow, E., & Wang, B. C. (1996). Crystal structure of the neurophysin-oxytocin complex. Nature Structural & Molecular Biology, 3, 163–169. doi:10.1038/nsb0296-163
   Web of Science ®Google Scholar
• Sikorska, E., & Kwiatkowska, A. (2013). Micelle-bound conformations of neurohypophyseal hormone analogues modified with a Cα-disubstituted residue: NMR and molecular modelling studies. Journal of Biomolecular Structure & Dynamics, 31, 748–764. doi:10.1080/07391102.2012.709459
   PubMed Web of Science ®Google Scholar
• Sikorska, E., & Rodzeiwicz-Motowidlo, S. (2008). Conformational studies of vasopressin and mesotocin using NMR spectroscopy and molecular modelling methods. Part I: Studies in water. Journal of Peptide Science, 14, 76–84. doi:10.1002/psc.91810.1002/(ISSN)1099-1387
   PubMed Web of Science ®Google Scholar
• Ślusarz, M. J., Ślusarz, R., & Ciarkowski, J. (2006). Molecular dynamics simulation of human neurohypophyseal hormone receptors complexed with oxytocin – modeling of an activated state. Journal of Peptide Science, 12, 171–179. doi:10.1002/psc.71310.1002/(ISSN)1099-1387
   PubMed Web of Science ®Google Scholar
• Tarnowska, M., Liwo, A., Shenderovich, M. D., Liepiga, I., Golbraikh, A. A., Grzonka, Z., & Tempczyk, A. (1993). A molecular mechanics study of the effect of substitution in position 1 on the conformational space of the oxytocin/vasopressin ring. Journal of Computer-Aided Molecular Design, 7, 699–719. doi:10.1007/BF0012532710.1007/BF00125327
   Web of Science ®Google Scholar
• Turner, R. J., Matsoukas, J. M., & Moore, G. J. (1990). Tyrosinate fluorescence lifetimes for oxytocin and vasopressin in receptor-simulating environments: Relationship to biological activity and 1H-NMR data. Biochemical and Biophysical Research Communications, 171, 996–1001. doi:10.1016/0006-291X(90)90782-I10.1016/0006-291X(90)90782-I
   PubMed Web of Science ®Google Scholar
• Urry, D. W., Ohnishi, M., & Walter, R. (1970). Secondary structure of the cyclic moiety of the peptide hormone oxytocin and its deamino analog. Proceedings of the National Academy of Sciences, 66, 111–116. Retrieved from http://www.pnas.org/content/66/1/111.abstract10.1073/pnas.66.1.111
   PubMed Web of Science ®Google Scholar
• Urry, D. W., & Walter, R. W. (1971). Proposed Conformation of Oxytocin in Solution. Proceedings of the National Academy of Sciences, 68, 956–958. Retrieved from http://www.pnas.org/content/68/5/95610.1073/pnas.68.5.956
   PubMed Web of Science ®Google Scholar
• Vuister, G. W., & Bax, A. (1993). Quantitative J correlation: A new approach for measuring homonuclear three-bond J(HNH.alpha.) coupling constants in 15N-enriched proteins. Journal of the American Chemical Society, 115, 7772–7777. doi:10.1021/ja00070a02410.1021/ja00070a024
   Web of Science ®Google Scholar
• Wagner, G., Neuhaus, D., Worgotter, E., Vasak, M., Kagi, J. H. R., & Wuthrich, K. (1986). Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary structure in rabbit liver metallothionein-2. Journal of Molecular Biology, 187, 131–135. doi:10.1016/0022-2836(86)90413-410.1016/0022-2836(86)90413-4
   PubMed Web of Science ®Google Scholar
• Walter, R. (1977). Identification of sites in oxytocin involved in uterine receptor recognition and activation. Federation Proceedings of the National Academy of Sciences of the United States of America of American Society for Experimental Biology, 36, 1872–1878. Retrieved from PMID: 192603
   Google Scholar
• Walter, R., Prasad, K. U. M., Deslauriers, R., & Smith, I. C. P. (1973). Conformational studies of oxytocin, lysine vasopressin, arginine vasopressin, and arginine vasotocin by carbon-13 nuclear magnetic resonance spectroscopy. Proceedings of the National Academy of Sciences, 70, 2086–2090. Retrieved from http://www.pnas.org/content/70/7/2086.abstract10.1073/pnas.70.7.2086
   PubMed Web of Science ®Google Scholar
• Walter, R., Skala, G., & Smith, C. W. (1978). [5-Aspartic acid]-oxytocin: first 5-position neurohypophyseal hormone analog possessing significant biological activity. Journal of the American Chemical Society, 100, 972–973. doi:10.1021/ja00471a05310.1021/ja00471a053
   Web of Science ®Google Scholar
• Ward, D. J., Chen, Y., Platt, E., & Robson, B. (1991). Development and testing of protocols for computer-aided design of peptide drugs, using oxytocin. Journal of Theoretical Biology, 148, 193–227. doi:10.1016/S0022-5193(05)80341-810.1016/S0022-5193(05)80341-8
   PubMed Web of Science ®Google Scholar
• Wittelsberger, A., Patiny, L., Slaninova, J., Barberis, C., & Mutter, M. (2005). Introduction of a cis-prolyl mimic in position 7 of the peptide hormone oxytocin does not result in antagonistic activity. Journal of Medicinal Chemistry, 48, 6553–6562. doi:10.1021/jm049205z10.1021/jm049205z
   PubMed Web of Science ®Google Scholar
• Wood, S. P., Tickle, I. J., Treharne, A. M., Pitts, J. E., Mascarenhas, Y., Li, J. Y., … Wyssbrod, H. R. (1986). Crystal structure analysis of deamino-oxytocin: Conformational flexibility and receptor binding. Science, 232, 633–636. doi:10.1126/science.300833210.1126/science.3008332
   PubMed Web of Science ®Google Scholar
• Wuthrich, K. (1986). NMR of proteins and nucleic acids. New York, NY: Wiley.
   Google Scholar
• Wüthrich, K., Billeter, M., & Braun, W. (1984). Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton–proton distances. Journal of Molecular Biology, 180, 715–740. doi:10.1016/0022-2836(84)90034-210.1016/0022-2836(84)90034-2
   PubMed Web of Science ®Google Scholar