Publications

Straus group members indicated in bold. Underlining indicates corresponding author.

  1. “Developing novel Lin28 inhibitors by computer aided drug design.” V.M. Matias-Barrios, M. Radaeva, G. Rosellinny, Q. Jia, N. Xie, M.T.L. Villanueva, H. Ibrahim, J. Smith, M. Gleave, N. Lallous, S.K. Straus, A. Cherkasov, X. Dong, Cell Death Discov. 11(1):5 (2025).
  2. “Novel active Trp- and Arg-rich antimicrobial peptides with high solubility and low red blood cell toxicity designed using machine learning tools”, B.A.B. Henson, F. Li, J.A. Álvarez-Huerta, P.G. Wedamulla, A.V. Palacios, M.R.M. Scott, D.T.E. Lim, W.M.H. Scott, M.T.L. Villanueva, E. Ye, S.K. Straus, Int. J. Antimicrob. Agents. 65(1):107399 (2025).
  3. “Interaction between the Polyelectrolytes Unfractionated Heparin and Universal Heparin Reversal Agents”, H.K. S
    aini, A.L. Creagh, C.C. La, D.T.E. Lim, J.N. Kizhakkedathu, C.A. Haynes, S. Srebnik, S.K. Straus, M. Ballauff, J. Phys. Chem. B. 128(51):12808-12817 (2024).
  4. “Tryptophan- and arginine-rich antimicrobial peptides: Anti-infectives with great potential”, S.K. Straus, BBA-Biomembranes, 1866(3):184260 (2023).
  5. “Smart Thrombosis Inhibitors Without Bleeding Side Effects via Charge Tunable Ligand Design”, C. La, S.A Smith, S. Vappala, R. Adili, S. Abbina, H. Luo, I. Chafeeva, L.A. Creagh, M. de Guadalupe Jaraquemada-Peláez, M.T. Kalathottukaren, M. Holinstat, S.K. Straus, C. Du, E.M. Conway, C.A. Haynes, J.H. Morrissey, J.N. Kizhakkedathu, Nature Comm. 14(1):2177 (2023).
  6. “Novel alligator cathelicidin As-CATH8 demonstrates anti-infective activity against clinically relevant and crocodylian bacterial pathogens”, F.L. Santana, K. Estrada, M.A. Alford, B.C. Wu, M. Dostert, L. Pedraz, N. Akhoundsadegh, P. Kalsi, E.F. Haney, S.K. Straus, G. Corzo, R.E.W. Hancock, Antibiotics, 11(11):1603 (2022).
  7. “Studying the Interactions of U24 from HHV-6 in Order to Further Elucidate Its Potential Role in MS”, K.-S. Pi, D. Bortolotti, Y. Sang, G. Schiuma, S. Beltrami, S. Rizzo, A. Bortoluzzi, E. Baldi, A.L. Creagh, C.A. Haynes, R. Rizzo, S.K. Straus, Viruses. 14(11):2384 (2022).
  8. Correction to: “Multifunctional Antibiotic-Host Defense Peptide Conjugate Kills Bacteria, Eradicates Biofilms and Modulates the Innate Immune Response”, H. Etayash, M. Alford, N Akhoundsadegh, M. Drayton, S.K. Straus, R.E.W. Hancock, J Med Chem. 65(3):2710-2711 (2022).
  9. “Viral proteins with PxxP and PY motifs may play a role in multiple sclerosis”, K.-S. Pi, Y. Sang, S.K. Straus, Viruses, 14(2):281(2022).
  10. “Multifunctional Antibiotic-Host Defense Peptide Conjugate Kills Bacteria, Eradicates Biofilms and Modulates the Innate Immune Response”, H. Etayash, M. Alford, N Akhoundsadegh, M. Drayton, S.K. Straus, R.E.W. Hancock, J Med Chem. 64(22):16854-16863 (2021).
  11. “Host Defense Peptides: Dual Antimicrobial and Immunomodulatory Action”, M. Drayton, J.P. Deisinger, K.C. Ludwig, N. Raheem, A. Müller, T. Schneider, S.K. Straus, Int. J. Mol. Sci. 22(20):11172 (2021).
  12. “Enzymatically releasable polyethylene glycol – host defense peptide conjugates with improved activity and biocompatibility”, M. Drayton, M.A. Alford, D. Pletzer, E.F. Haney, Y. Machado, H.D. Luo, C.M. Overall, J.N. Kizhakkedathu, R.E.W. Hancock, and S.K. Straus, J. Contr. Release 339:220-231 (2021).
  13. “Lipidation of Antimicrobial Peptides as a Design Strategy for Future Alternatives to Antibiotics”, T. Rounds, S.K. Straus, Int. J. Mol. Sci. (special issue), 21(24):9692 (2020).
  14. “A cyclic derivative of host-defence peptide IDR-1018 improves proteolytic stability, suppresses inflammation, and enhances in vivo activity”, H. Etayash, D. Pletzer, P. Kumar, S.K. Straus, R.E.W. Hancock, J. Med. Chem, 63(17):9228-9236 (2020).
  15. “Design, Engineering and Discovery of Novel α-helical and β-boomerang Antimicrobial Peptides Against Drug Resistant Bacteria”, S. Bhattacharjya, S.K. Straus, Int. J. Mol. Sci. (special issue), 21(16):5773 (2020).
  16. “Towards robust delivery of antimicrobial peptides to combat bacterial resistance”, M. Drayton, J. Kizhakkedathu, S.K. Straus, Macromolecules (special issue), 25(13):3048 (2020).
  17. “Determining the mechanism of action of host defense peptides: Solid State NMR approaches.”, S.K. Straus, A. Takayesu, P. Kumar, IOP Publishing Ltd, Editors: Frances Separovic and Marc-Antoine Sani, Chapter 5 (2020).
  18. “Insights into the mechanism of action of two analogues of aurein 2.2”, N. Raheem, P. Kumar, E. Lee, J.T.J. Cheng, R.E.W. Hancock, S.K. Straus, BBA- Biomembranes special issue in honour of Michele Auger, 1862(6):183262 (2020).
  19. “Mechanisms of Action for Antimicrobial Peptides With Antibacterial and Antibiofilm Functions”, N. Raheem, S.K. Straus, Front. Microbiol. 10:2866 (2019).
  20. “Quantifying cellulose accessibility during enzyme-mediated deconstruction using 2 fluorescence-tagged carbohydrate-binding modules”, V. Novy, K. Aïssa, F. Nielsen, S.K. Straus, P. Ciesielski, C.G. Hunt, J. Saddler, PNAS 116(45):22545-22551 (2019).
  21. “Reassessing the Host Defence Peptide Landscape”, E.F. Haney, S.K. Straus, R.E.W. Hancock, Front. Chem. 7:43 (2019).
  22. “Aurein-derived antimicrobial peptides formulated with pegylated phospholipid micelles to target methicillin-resistant Staphylococcus aureus skin infections”, P. Kumar, D. Pletzer, E.F. Haney, N. Rahanjam, J.T.J. Cheng, M. Yue, W. Aljehani, R.E.W. Hancock, J.N. Kizhakkedathu, S.K. Straus, ACS Infect Dis., 5(3):443-453 (2018).
  23. “Filamentous Bacteriophage Proteins and Assembly”, S.K. Straus, H.E. Bo, Subcell Biochem. 88:261-279 (2018).
  24. “Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo”, P. Kumar, J. Kizhakkedathu, S.K. Straus, Biomolecules, 8(1): pii: E4 (2018).
  25. “Antimicrobial peptide-polymer conjugates with high activity: Influence of polymer molecular weight and peptide sequence on antimicrobial activity, proteolysis and biocompatibility”, P. Kumar, A. Takayesu, U. Abbasi, M.T. Kalathottukaren, S. Abbina, J. Kizhakkedathu, S.K. Straus, ACS Applied Materials & Interfaces, 9(43): 37575-37586 (2017).
  26. “On the quest for the elusive mechanism of action of daptomycin: binding, fusion, and oligomerization”, J. Zhang, W.R.P. Scott, F. Gabel, M. Wu, R. Desmond, J. Bae, G. Zaccai, W.R. Algar, S.K. Straus, BBA – Proteins and Proteomics, 1865(11 Pt B): 1490-1499 (2017).
  27. “Structure and Properties of Lignin Based Carbon Nanofibers”, L. Song, A. Bahi, L.T. Lin, A.P. Dodd, S.K. Straus, F.K. Ko, ICCM-21 Proceedings (2017).
  28. “U24 from Roseolovirus interactions with WW Domains: Canonical vs Non-Canonical”, Y. Sang, R. Zhang, A.L. Creagh, C.A. Haynes, S.K. Straus, NRC Biochem. Cell. Biol., 95(3):350-358 (2017).
  29. “U24 from Roseolovirus interacts strongly with Nedd4 WW Domains”, Y. Sang, R. Zhang, W.R.P. Scott, A.L. Creagh, C.A. Haynes, S.K. Straus, Sci. Rep., 7:39776 (2017).
  30. “Daptomycin leakage is selective”, J. Zhang, K. Scoten, S.K. Straus, ACS-Infect. Dis., 2(10):682-687 (2016).
  31. “Antimicrobial peptides from the aurein family form ion-selective pores in Bacillus subtilis”, M. Wenzel, C.H.R. Senges, J. Zhang, S. Suleman, M. Nguyen, P. Kumar, A.I. Chiriac, J.J. Stepanek, N. Raatschen, C. May, U. Krämer, H.-G. Sahl, S. K. Straus, J. E. Bandow, ChemBioChem, 16(7):1101-8 (2015).
  32. “Bioconjugation of aurein antimicrobial peptides and hyperbranchedpolyglycerol systems”, P. Kumar, R.A. Shenoi, B.F. Lai, M. Nguyen, J. Kizhakkedathu, S.K. Straus, Biomacromolecules, 16(3):913-23 (2015).
  33. “Determining and Visualising Flexibility in Protein Structures”, W.R.P. Scott, S.K. Straus, Proteins: Structure, Function, Bioinformatics, 83(5):820-6 (2015).
  34. “Characterization of fractions obtained from two industrial softwood Kraft lignins”, A.P. Dodd, J. F. Kadla, S.K. Straus, Sus. Chem. Eng. (ACS), 3: 103-110 (2015).
  35. “Probing the Interaction between U24 and the SH3 Domain of Fyn Tyrosine Kinase”, Y. Sang, A.R. Tait, W.R.P. Scott, A.L. Creagh, P. Kumar, C.A. Haynes, S.K. Straus, Biochemistry, 53(38):6092-102 (2014).
  36. “Broad-spectrum anti-biofilm peptide that targets a cellular stress response”, C. de la Fuente-Núñez, F. Reffuveille, E.F. Haney, S.K. Straus, R.E.W. Hancock, PLOS Pathogens, 10(5):e1004152. doi: 10.1371 (2014).
  37. “Small cationic antimicrobial peptides delocalize peripheral membrane proteins”, M. Wenzel, A.I. Chiriac, A. Otto, D. Zweytick, C. May, C. Schumacher, R. Gust, H.B. Albada, M. Penkova, U. Krämer, R. Erdmann, N. Metzler-Nolte, S.K. Straus, E. Bremer, D. Becher, H. Brötz-Oesterhelt, H.G. Sahl, J.E. Bandow, PNAS, 111(14):E1409-18 (2014).
  38. “Structure and assembly of filamentous bacteriophages”, D.A. Marvin, M.F. Symmons, S.K. Straus, Prog. Biophys. Mol. Biol., 114(2):80-122 (2014).
  39. “The influence of MoP properties on the hydrodeoxygenation of 4‑methylphenol”, V.M.L. Whiffen, K.J. Smith, S.K. Straus, Applied Catalysis A: General, 419: 111-125 (2012).
  40. “Biomembrane Interactions of Polymer Brush and Soluble Polymer Tethered Host Defence Peptide 1010: Insight into the Mechanism of Action”, G. Gao, J.T.J. Cheng, R.E.W. Hancock, S.K. Straus, J. Kizhakkedathu, Chemistry and Biology, 19(2):199-209 (2012).
  41. “Overexpression and purification of U24 from Human Herpesvirus Type-6 in coli: unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield”, A.R. Tait, S.K. Straus, Microb. Cell Fact.,10:51 (2011).
  42. “Antimicrobial properties of MX-2401, a second generation lipopeptide active in presence of lung surfactant”, D. Dugourd, H. Yang, M. Elliott, R. Siu, J.J. Clement, S.K. Straus, R.E.W. Hancock, E. Rubinchik, Antimicrobial Agents Chemotherapy, 55(8):3720-8 (2011).
  43. “Mechanism of action and limited cross resistance of a new lipopeptide MX-2401”, E. Rubinchik, T. Schneider, M. Elliott, W.R.P. Scott, J. Pan, C. Anklin, H. Yang, D. Dugourd, A. Müller, K. Gries, S.K. Straus, H.G. Sahl, R.E.W. Hancock, Antimicrobial Agents Chemotherapy, 55(6):2743-54 (2011).
  44. “The biocompatibility and biofilm resistance of implant coatings based on hydrophilic polymer brushes conjugated with antimicrobial peptides”, G. Gao, D. Lange, K. Hilpert, J. Kindrachuk, Y. Zou, J.T.J. Cheng, M. Kazemzadeh-Narbat, K. Yu, R. Wang, S.K. Straus, D.E. Brooks, B.H. Chew, R.E.W. Hancock, J.N. Kizhakkedathu, Biomaterials, 32(16): 3899-3909 (2011).
  45. “Single Molecule Force Spectroscopy Reveals that Electrostatic Interactions Affect the Mechanical Stability of Proteins”, P. Zheng, Y. Cao, T. Bu, S.K. Straus, H. Li, Biophys. J., 100(6):1534-41 (2011).
  46. “The Importance of Bacterial Membrane Composition in the Structure and Function of Aurein 2.2 and selected Variants”, J.T.J. Cheng, J.D. Hale, M. Elliott, R.E.W. Hancock, S.K. Straus, BBA-Biomembranes, 1808(3):622-33 (2011).
  47. “Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR”, S.K. Straus, W.R.P Scott, C.D. Schwieters, D.A. Marvin, Eur. Biophys. J., 40(3):221-34 (2011).
  48. “The Importance of Residue 13 and the C-terminus on the Structure and Activity of the Antimicrobial Peptide Aurein 2.2”, J.T.J. Cheng, J.D. Hale, J. Kindrachuk, H. Jenssen, M. Elliott, R.E.W. Hancock, S.K. Straus, Biophys. J., 99(9):2926-35 (2010).
  49. “Structural studies of a peptide with immune modulating and direct antimicrobial activity”, M. Wieczorek, H. Jenssen, J. Kindrachuk, W.R.P. Scott, M. Elliott, K. Hilpert, J.T.J. Cheng, R.E.W. Hancock, S.K. Straus, Chem. Biol., 17(9):970-80 (2010).
  50. “Parameters Affecting the Chiral Nematic Phase of Nanocrystalline cellulose films”, J. Pan, W. Hamad, S.K. Straus, Macromolecules, 43(8): 3851-8 (2010).
  51. “Synthetic Fusion Peptides of Tick-Borne Encephalitis Virus as Models for Membrane Fusion”, J. Pan, C.B. Lai, W.R.P. Scott, S.K. Straus, Biochemistry, 49(2):287-96 (2010).
  52. “Metabolomic abnormalities in fronto-striatal-thalamic white matter tracts in schizophrenia”, C.A. Beasley, V. Barakauskas, A.J. Dwok, G. Rosoklija, J.J. Mann, B. Mancevski, Z. Jakovski, N. Davceva, A.R. Tait, S.K. Straus, W.G. Honer, Schizophrenia Res., 109(1-3):159-66 (2009).
  53. “The Effect of Membrane Composition on the Antimicrobial Peptides Aurein 2.2 and 2.3 from Australian Southern Bell Frogs”, J.T.J. Cheng, J. Hale, M. Elliott, R.E.W. Hancock, S.K. Straus, Biophys. J., 96(2):552-65 (2009).
  54. “Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis”, A.R. Tait, S.K. Straus, FEBS Letters, 582(18):2685-8 (2008).
  55. “Lipid specific binding of the calcium-dependent antibiotic daptomycin leads to changes in lipid polymorphism of model membranes”, D. Jung, J.P. Powers, S.K. Straus, R.E.W. Hancock, Chem. Phys. Lipids, 154(2):120-8 (2008).
  56. “The hand of filamentous bacteriophage”, S.K. Straus, W.R.P. Scott, D.A. Marvin, Euro. Biophysics J., 37(6):1077-82 (2008).
  57. “Effect of Divalent Cations on the Structure of the Antibiotic Daptomycin”, W. Ho, D. Jung, J.R. Calhoun, J.D. Lear, M. Okon, W.R.P. Scott, R.E.W. Hancock, S.K. Straus, Euro. Biophysics J., 37(4):421-33 (2008).
  58. “On the structures of filamentous bacteriophage Ff (fd,f1,M13)”, S.K. Straus, W.R.P. Scott, M. Symmons, D.A. Marvin, Euro. Biophysics J., 37(4):521-7 (2008).
  59. “NMR Structural Studies of the Antibiotic LipopeptideDaptomycin in DHPC micelles”, W.R.P. Scott, S.B. Baek, D. Jung, R.E.W. Hancock, S.K. Straus, Biochim. Biophys. Acta – Biomembranes, 1768, 3116-26 (2007).
  60. “Characterization of the Structure and Membrane Interaction of the Antimicrobial Peptides Aurein 2.2 and 2.3 from Australian Southern Bell Frogs”, Y.L. Pan, J.T.J. Cheng, J. Hale, J. Pan, R.E.W. Hancock, S.K. Straus, Biophys. J., 92, 2854-64 (2007).
  61. “Optimal Attachment Position and Linker Length Promotes Native-like Character of Cavitand-Based Template Assembled Synthetic Proteins (TASPs)”, E.S. Seo, W.R.P. Scott, S.K. Straus, J.C. Sherman, Chemistry – A European Journal, 13, 3596-605 (2007).
  62. “Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: comparison with cationic antimicrobial peptides and lipopeptides”, S.K. Straus, R.E.W. Hancock, Biochim. Biophys. Acta – Biomembranes, 1758, 1215-23 (2006).
  63. “Characterization of de Novo Four-Helix Bundles by Molecular Dynamics Simulations”, W.R.P. Scott, E. Seo, H. Huttunen, D. Wallhorn, J.C. Sherman, S.K. Straus, Proteins: Structure, Function and Bioinformatics, 64, 719-29 (2006).
  64. “Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane”, D. A. Marvin, L. C. Welsh, M. F. Symmons, W.R.P. Scott, S.K. Straus, J. Mol. Biol., 355, 294-309 (2006).
  65. “Interaction of Alamethicin with Ether-linked Phospholipid Bilayers: Oriented CircularDichroism, 31P Solid-State NMR, and Differential Scanning Calorimetry Studies”, C. Dave, E. Billington, Y.L. Pan, S.K. Straus, Biophys. J.,89, 2434-2442 (2005).
  66. “Can PISEMA Experiments be used to extract Structural Parameters for mobile β-Barrels?”,W. Bleile, W.R.P. Scott, S.K. Straus, J. Biomol. NMR, 32, 101-111 (2005).
  67. “Plasticity of Influenza Hemagglutinin Fusion Peptides and their Interaction with Lipid Bilayers”, L. Vaccaro, K. Cross, J. Kleinjung, S.K. Straus, D.J. Thomas, S.A. Wharton, J.J. Skehel, F. Fraternali, Biophys. J.,88, 25-36 (2005).
  68. “Orientational Constraints of Bacteriorhodopsin in Purple Membrane Film as studied by solid state NMR”, M. Kamihira, T. Voosegaard, A.J. Mason, S.K. Straus, N. Chr. Nielsen, A. Watts, Struct. Biol., 149, 7-16 (2005).
  69. “Recent Developments in MAS NMR of Fully Labelled Peptides and Proteins”, S.K. Straus, Phil. Trans. B, 359, 997-1008 (2004).
  70. “Membrane Protein Structure Determination Using Solid-State NMR”, A. Watts, S.K. Straus, S.L. Grage, M. Kamihira, Y.H. Lam, X. Zhao, in Methods in Molecular Biology – Protein NMR Techniques, K. Downing, ed., Chapter 19, pp. 403-74 (2004).
  71. “Identifying Anisotropic Constraints in Multiply Labelled Membrane Proteins by 15N MAS NMR”, A.J. Mason, S.L. Grage, S.K. Straus, C. Glaubitz, A. Watts, J., 86, 1610-1617 (2004).
  72. “Assessing the Effects of Time & Spatial Averaging in 15N Chemical Shift/15N-1H Dipolar Correlation Solid State NMR Experiments”, S.K. Straus, W.R.P. Scott, A. Watts, Biomol. NMR, 26, 283-295 (2003).
  73. “Expression, purification, and activities of full-length and truncated versions of the integral membrane protein Vpu from HIV-1”, C. Ma, F.M. Marassi, D.H. Jones, S.K. Straus, S. Bour, U. Schubert, K. Strebel, M. Oblatt-Montal, M. Montal, S.J. Opella, Protein Science, 11, 546-557 (2002).
  74. “Correspondence of the Structural and Functional Domains in the Membrane Protein Vpu from HIV-1”, F.M. Marassi, C. Ma, H. Gratkowski, S.K. Straus, K. Strebel, M. Oblatt-Montal, M. Montal, S.J. Opella, Natl. Acad. Sci., 96, 14336-14341 (1999).
  75. “Effects of Dynamics and Environment on 15N Chemical Shift Anisotropy in Proteins. A Combination of DFT, Molecular Dynamics Simulation, and NMR Relaxation”, C. Scheurer, N.R. Skrynnikov, S.F. Lienin, S.K. Straus, R. Brüschweiler, R.R. Ernst, J. Am. Chem. Soc, 121, 4242-4251 (1999).
  76. “Experiments and Strategies for the Assignment of Fully 13C/15N-labelled Polypeptides by Solid State NMR”, S.K. Straus, T. Bremi, R.R. Ernst, J. Biomol. NMR, 12, 39-50 (1998).
  77. “Side-chain Conformation and Dynamics in a Solid Peptide. CP-MAS NMR Study of Valine Rotamers and Methyl-group Relaxation in Fully 13C-labelled Antamanide”, S.K. Straus, T. Bremi, R.R. Ernst, J. Biomol. NMR, 10, 119-128 (1997).
  78. “Resolution Enhancement by Homonuclear J Decoupling in Solid-state MAS NMR”, S.K. Straus, T. Bremi, R.R. Ernst, C. Phys. Lett, 262, 709-715 (1996).
  79. “Use of Fuzzy Mathematics for Complete Automated Assignment of Peptide 1H 2D NMR Spectra”, J. Xu, S.K. Straus, B.C. Sanctuary, L. Trimble, J. Magn. Reson, B103, 53-58 (1994).
  80. “Automation of Protein 2D Proton NMR Assignment by Means of Fuzzy Mathematics and Graph Theory”, J. Xu, S.K. Straus, B.C. Sanctuary, L. Trimble, J. Chem. Inf. Comput. Sci, 33, 668-682 (1993).