#: Cotten as corresponding author.
&: Featuring independent research on piscidin.
R. Fu, M.T. Rooney, R. Zhang, and M.L. Cotten. Coordination of Redox Ions within a Membrane-Binding Peptide: A Tale of Aromatic Rings. 2021. J. Phys. Chem. Letters. https://doi.org/10.1021/acs.jpclett.1c00636.&#
Rice, M. Rooney, A.I. Greenwood, M.L. Cotten, and J. Wereszczynski. Lipopolysaccharide Simulations are Sensitive to Phosphate Charge and Ion Parameterization. 2020. J. Chem. Theory Comput. https://doi.org/10.1021/acs.jctc.9b00868
Paredes, S. Kim, M.T. Rooney, A.I. Greenwood, K. Hristova, and M.L. Cotten. Effect of Metallation on the Membrane Activity of Piscidin: Mechanistic Insights Gained from 31P Solid-state NMR. Invited manuscript to Biochim. Biophys. Acta – Biomembranes, Commemorative Special Issue in Honor of Michèle Auger. 2020, 1862:183236. https://doi.org/10.1016/j.bbamem.2020.183236.&#
Cetuk, J. Maramba, M. Britt, R. Ernst, E. Mihailescu, M.L. Cotten and S. Sukharev. Differential interactions of Piscidins with phospholipids and lipopolysaccharides at membrane interfaces. Langmuir, April 19, 2020, https://doi.org/10.1021/acs.langmuir.0c00017.
Juliano, L. Serafim, S. Duay, M. Heredia Chavez, G. Sharma, M. Rooney^, F. Comert, A. Radulescu, M.L. Cotten, M. Mihailescu, E. May, A. Greenwood, R. Prabhakar, A. Angeles-Boza. A Potent Host Defense Peptide Triggers DNA Damage and is Active against Multi-Drug Resistant Gram-Negative Pathogens. ACS Infectious Diseases, April 6, 2020, https://doi.org/10.1021/acsinfecdis.0c00051.
M. Mihailescu, M. Sorci, J. Seckute, V. I. Silin, J. Hammer, B. Scott Perrin Jr., J. I. Hernandez, N. Smajic, A. Shrestha, K. A. Bogardus, A. I. Greenwood, R. Fu, J. Blazyk, R. W. Pastor, L. K. Nicholson, G. Belfort, M. L. Cotten. Structure and Function in Antimicrobial Piscidins: Histidine Position, Directionality of Membrane Insertion, and pH-Dependent Permeablization. 2019. J Am Chem Soc. 141:9837-9853.&#
Comert, A.I. Greenwood^, J. Maramba, R. Acevedo, L. Lucas, T. Kulasinghe, L.S. Cairns, Y. Wen, R. Fu, J. Hammer, J. Blazyk, S. Sukharev, M.L. Cotten, and M. Mihailescu. The Host-defense Peptide Piscidin P1 Reorganizes Lipid Domains in Membranes and Decreases Activation Energies in Mechanosensitive Ion Channels. 2019. J. Biol. Chem. 294:18557-18570.&#
- This article features two 3-dimensional structures deposited in the protein data bank: http://www.rcsb.org/structure/6PF0; http://www.rcsb.org/structure/6PEZ.
Oludiran, D.S. Courson, M.D. Stewart, M.L. Cotten, and E. B. Purcell. How Oxygen Availability Affects the Antimicrobial Efficacy of Host Defense Peptides: Lessons Learned from Studying the Copper-binding Peptides Piscidins 1 and 3. 2019. Int J Mol Sci. 20(21).&#
R.K. Rai, A. De Angelis, A. Greenwood, S.J. Opella, M. L. Cotten. Metal-ion Binding to Host Defense Peptide Piscidin 3 Observed in Phospholipid Bilayers by Magic Angle Spinning Solid-State NMR. 2019. Chemphyschem. 20:295-301.&#
S.Y. Kim, F. Zhang, W. Gong, K. Chen, K. Xia, F. Liu, R. Gross, J.M. Wang, R.J. Linhardt, and M.L. Cotten. Copper Regulates the Interactions of Antimicrobial Piscidin Peptides from Fish Mast Cells with Formyl-peptide Receptors and Heparin. 2018. J. Biol. Chem. 293:15381-15396. &#
M.D.J Libardo, A.A. Bahar, B. Ma, R. Fu, L.E. McCormick, J. Zhao, S.A. McCallum, R. Nussinov, D. Ren, A.M. Angeles-Boza, and M.L. Cotten. Nuclease activity gives an edge to host-defense peptide piscidin 3 over piscidin 1, rendering it more effective against persisters and biofilms. 2017. FEBS J. 284:3662-3683.&#
B.S. Perrin, Jr., R. Fu, M.L. Cotten, and R.W. Pastor. Multimicrosecond simulations of membrane disrupting peptides II: AMP Piscidin 1 favors surface defects over pores. 2016. Biophys. J. 111:1258-66.&
E. Mihailescu, V. Silin, K. Bogardus, M.L. Cotten#. Observing Transitions from Surface-Bound to Inserted States of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Lipid Membranes: Insight into the Mechanism of Membrane Disruption. Manuscript submitted.&#
M.D.J. Libardo, D. Ren, A.M. Angeles-Boza, R. Fu, and M.L. Cotten. Piscidins 1 and 3 as Antimicrobial Metallopeptides: Nuclease Activity Reveals New Insights into Vertebrate Innate Immunity. Manuscript submitted. &#
M. Sorci, J. Seckute, N. Smajic*, B.S. Perrin, Jr., L.K. Nicholson, J. Blazyk, R.W. Pastor, G. Belfort and M.L. Cotten. Structural Flexibility, Hydrophobicity, and Charge Regulation in Histidine-Rich Antimicrobial Piscidins Underpin Membrane Association, Thinning, and Destabilization Examined in Real Time. Manuscript in preparation.&#
R.M. Hayden*, G.K. Goldberg*, B.M. Ferguson*, M.W. Schoeneck*, M.D.J. Libardo, S.E. Mayeux*, A. Shrestha*, K.A. Bogardus*, J. Hammer, S. Pryshchep, H.K. Lehman, M.L. McCormick, J. Blazyk, A.M. Angeles-Boza, R. Fu, and M.L. Cotten. Complementary Effects of Host Defense Peptides Piscidin 1 and Piscidin 3 on DNA and Lipid Membranes: Biophysical Insights into Contrasting Biological Activities. 2015. J. Phys. Chem. B. 119:15235-46. &#
B.S. Perrin, A.J. Sodt, M. Cotten, and R.W. Pastor. The Curvature Induction of Surface-Bound Antimicrobial Peptides Piscidin 1 and Piscidin 3 Varies With Lipid Chain Length. 2015. J. Membr. Biol. 248:455-67&
W. Chen, M.L. Cotten. Expression, purification, and micelle reconstitution of antimicrobial piscidin 1 and piscidin 3 for NMR studies. 2014. Protein Expr. Purif. 102:63-68. &#
B.S. Perrin Jr., Y. Tian, R. Fu, C.V. Grant, E.Y. Chekmenev, W.E. Wieczorek*, A.E. Dao*, R.M. Hayden*, C.M. Burzynski*, R.M. Venable, M. Sharma, S.J. Opella, R.W. Pastor, and M.L. Cotten. High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion. 2014. J. Am. Chem. Soc. 136: 3491–3504. Cover story, podcast, and spotlight entitled “Solid-State NMR Reveals How a Kinky Peptide Slays Microbes”. &#
B.S. Perrin Jr., R. W. Pastor and M. Cotten. Combining NMR Spectroscopic Measurements and Molecular Dynamics Simulations to Determine the Orientation of Amphipathic Peptides in Lipid Bilayers in Advances. In Biological Solid-State NMR: Proteins and Membrane-Active Peptides; Separovic, F., Naito, A., Eds.; Royal Society of Chemistry: Cambridge, 2014; chap. 2, pp 18−35. &#
R.B. Kinnel, A.W. Van Wynsberghe, I.J. Rosenstein, K.S. Brewer, M. Cotten, G.C. Shields, C.J. Borton, S.Z. Senior, G.S. Rahn, and T.E. Elgren. A Departmental Focus on High Impact Undergraduate Research Experiences. In Developing and Maintaining a Successful Undergraduate Research Program; Chapp, T.W., Benvenuto, M.A., Eds.; American Chemical Society: Washington, DC, 2013; ACS Symposium series, vol. 1156, chapter 2, pp 5–22.
AA. De Angelis, C.V. Grant, M.K. Baxter*, J.A. McGavin*, S.J. Opella, and M.L. Cotten. Amphipathic Antimicrobial Piscidin in Magnetically Aligned Lipid Bilayers. 2011. Biophys. J. 105: 1086-1094. &#
F. Separovic, J.A. Killian, M. Cotten, D.D. Busath and T.A. Cross. Modeling the Membrane Environment for Membrane Proteins. 2011. Biophys. J. 100:2073-2074.
E.Y. Chekmenev, B.S. Vollmar, and M. Cotten. Can antimicrobial peptides scavenge around a cell in less than a second? Invited contribution. 2010. Biochim. Biophys. Acta. 1798:228-234. &#
R. Fu, E.D. Gordon, D.J. Hibbard, and M. Cotten. High resolution heteronuclear correlation NMR spectroscopy of an aligned antimicrobial peptide: Direct evidence of spectral enhancement at high magnetic field and peptide-water interactions at the water-bilayer interface. 2009. J. Am. Chem. Soc. 131: 10830–10831. &#
R. Fu, M. Truong, R.J. Saager, M. Cotten, and T.A. Cross. High Resolution Heteronuclear Correlation Spectroscopy in Solid State NMR of Aligned Samples. 2007. J. Magn. Reson. 188: 41–48. &
P.L. Gor’kov, E.Y. Chekmenev, C. Li, M. Cotten, J.J. Buffy, N.J. Traaseth, G. Veglia, W.W. Brey. Using Low-E resonators to reduce RF heating in biological samples for static solid-state NMR up to 900 MHz. 2007. J. Magn. Reson. 185: 77–93. &
E.Y. Chekmenev, S.M. Jones, Y.N. Nikolayeva, B.S. Vollmar, T.J. Wagner, P.L. Gor’kov, W.W. Brey, McK. N. Manion, K.C. Daugherty, and M. Cotten. High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface. 2006. J. Am. Chem. Soc. 128: 5308-5309. &#
E.Y. Chekmenev, B.S. Vollmar, K.T. Forseth, McK.N. Manion, S.M. Jones, T.J. Wagner, R.M. Endicott, B.P. Kyriss, L.M. Homem, M. Pate, J. He, J. Raines, P.L. Gor’kov, W.W. Brey, D.J. Mitchell, A.J. Auman, M.J. Ellard-Ivey, J. Blazyk, and M. Cotten. Investigating Molecular Recognition and Biological Function at Interfaces Using Piscidins, Antimicrobial Peptides from Fish. 2006. Invited paper. Biochim. Biophys. Acta. 1758: 1359-1372. &#
P.L. Gor’kov, E.Y. Chekmenev, R. Fu, J. Hu, T.A. Cross, M. Cotten, W.W. Brey. A Large Volume Flat Coil Probe for Oriented Membrane Proteins. 2006. J. Magn. Reson. 181: 9-20. &
C. D. Cole, A. S. Frost, N. Thompson, M. Cotten, T. A. Cross and D. D. Busath. Noncontact dipole effects on channel permeation. VI. 5F-and 6F-Trp gramicidin channel currents. 2002. Biophys. J. 83: 1974-1986.
G. P. Drobny, J. R. Long, W. S. Shaw, M. Cotten, and P. S. Stayton. Studies of Structure and Dynamics of Proteins Adsorbed to Biomaterial Interfaces. In Encyclopedia of Nuclear Magnetic Resonance, Advances in NMR; John Wiley & Sons Ltd: Hoboken, NJ, 2002; vol. 9, pp. 458-468.
N. Thompson, G. Thompson, C. D. Cole, M. Cotten, T. A. Cross, and D. D. Busath. Noncontact Dipole Effects on Channel Permeation. IV. Kinetic Model of 5F-Trp13 Gramicidin A Currents. 2001. Biophys. J. 81: 1245-1254.
R. Fu, M. Cotten, and T. A. Cross. Intermolecular Distance Measurements by Solid State NMR to determine Gramicidin Dimer Structures in Hydrated Phospholipid Bilayers. 2000. J Biomol NMR. 16:261-268.
R. Phillips, C. D. Cole, R. J. Hendershot, M. Cotten, T. A. Cross, D. D. Busath. Noncontact dipole effects on channel permeation. III. Anomalous proton conductance effects in gramicidin. 1999. Biophys J. 77:2492-2501.
M. Cotten, C. Tian, D. Busath, R. B. Shirts, and T. A. Cross. Modulating Dipoles for Structure-Function Correlations in the Gramicidin Channel. 1999. Biochemistry. 38:9185-9197.
M. Cotten, R. Fu, and T. A. Cross. Solid State NMR and Hydrogen Deuterium Exchange in a Bilayer Solubilized Peptide: Structural and Mechanistic Implications. 1999. Biophys. J. 76:1179-1189.
D. A. Busath, C. D. Thulin, R. W. Hendershot, L. R. Revell Philips, P. Maughan, C. D. Cole, N. C. Bingham, S. Morisson, L. C. Baird, R. J. Hendershot, M. Cotten, and T. A. Cross. Non-Contact Dipole Effects on Channel Permeation. I. Experiments with (5F-Indole) Trp-13 Gramicidin A Channels. 1998. Biophys. J. 75:2830-2844.
M. Cotten, Feng Xu, and T. A. Cross. Protein Stability and Conformational Rearrangements in Lipid Bilayers: Linear Gramicidins, a Model System. 1997. Biophys. J. 73:614-623.
M. Cotten, V. G. Soghomonian, W. Hu, and T. A. Cross. High Resolution and High Fields in Biological State NMR. 1997. Solid State NMR. 9:77-80.
V. G. Soghomonian, M. Cotten, R. Rosanske, and T. A. Cross. Field Stabilization and 2H NMR Spectroscopy in a 24.6 T Resistive Magnet. 1997. J. Magn. Reson. 125:212-215.
S. Aramugam, S. Pascal, C. L. North, W. Hu, K. -C Lee, M. Cotten, R. R. Ketchem, F. Xu., M. Brenneman, F. Kovacs, F. Tian, A. Wang, S. Huo, and T. A. Cross. Conformational Trapping in a Membrane Environment: a Regulatory Mechanism for Protein Activity. 1996. Proc. Natl. Acad. Sci. USA. 93:5872-5876.