Biomimetic antimicrobial polymers: recent advances in molecular design

Antimicrobial peptides of multicellular organisms

Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829

Bad Bugs, No Drugs: No ESKAPE! An Update from the Infectious Diseases Society of America

Boucher, H. W., Talbot, G. H., Bradley, J. S., Edwards, J. E., Gilbert, D., Rice, L. B., Scheld, M., Spellberg, B., & Bartlett, J. (2009) · Clinical Infectious Diseases · doi:10.1086/595011 · Cited by 4,958

Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies

Hancock, R. E. W., & Sahl, H.-G. (2006) · Nature Biotechnology · doi:10.1038/nbt1267 · Cited by 4,208

APD3: the antimicrobial peptide database as a tool for research and education

Wang, G., Li, X., & Wang, Z. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1278 · Cited by 2,388

Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.

Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305

Designing antimicrobial peptides: form follows function

Fjell, C. D., Hiss, J. A., Hancock, R. E. W., & Schneider, G. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3591 · Cited by 2,035

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides

Shai, Y. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(99)00200-x · Cited by 1,869

The Chemistry and Applications of Antimicrobial Polymers: A State-of-the-Art Review

Kenawy, E.-R., Worley, S. D., & Broughton, R. (2007) · Biomacromolecules · doi:10.1021/bm061150q · Cited by 1,558

Polymeric materials with antimicrobial activity

Muñoz-Bonilla, A., & Fernández-García, M. (2012) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2011.08.005 · Cited by 1,221

Why and how are peptide–lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes

Matsuzaki, K. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(99)00197-2 · Cited by 1,010

APD2: the updated antimicrobial peptide database and its application in peptide design.

Wang, G., Li, X., & Wang, Z. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn823 · Cited by 941

Combating multidrug-resistant Gram-negative bacteria with structurally nanoengineered antimicrobial peptide polymers

Lam, S. J., O'Brien-Simpson, N. M., Pantarat, N., Sulistio, A., Wong, E. H. H., Chen, Y.-Y., Lenzo, J. C., Holden, J. A., Blencowe, A., Reynolds, E. C., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.162 · Cited by 821

APD: the Antimicrobial Peptide Database

Wang, Z. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh025 · Cited by 808

Antimicrobial peptides in mammalian and insect host defence

Lehrer, R. I., & Ganz, T. (1999) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)80005-3 · Cited by 723

Amphipathic α helical antimicrobial peptides.: A systematic study of the effects of structural and physical properties on biological activity

Giangaspero, A., Sandri, L., & Tossi, A. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2001.02494.x · Cited by 636

Biodegradable nanostructures with selective lysis of microbial membranes

Nederberg, F., Zhang, Y., Tan, J. P. K., Xu, K., Wang, H., Yang, C., Gao, S., Guo, X. D., Fukushima, K., Li, L., et al. (2011) · Nature Chemistry · doi:10.1038/nchem.1012 · Cited by 614

Magainins as paradigm for the mode of action of pore forming polypeptides

Matsuzaki, K. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00014-8 · Cited by 589

Antimicrobial polymers: mechanism of action, factors of activity, and applications

Timofeeva, L., & Kleshcheva, N. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2920-9 · Cited by 579

Aliphatic Polyesters: Great Degradable Polymers That Cannot Do Everything

Vert, M. (2005) · Biomacromolecules · doi:10.1021/bm0494702 · Cited by 565

Toroidal pores formed by antimicrobial peptides show significant disorder

Sengupta, D., Leontiadou, H., Mark, A. E., & Marrink, S.-J. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.06.007 · Cited by 563

De Novo Design of Antimicrobial Polymers, Foldamers, and Small Molecules: From Discovery to Practical Applications

Tew, G. N., Scott, R. W., Klein, M. L., & DeGrado, W. F. (2010) · Accounts of Chemical Research · doi:10.1021/ar900036b · Cited by 552

Tuning the Hemolytic and Antibacterial Activities of Amphiphilic Polynorbornene Derivatives

Ilker, M. F., Nüsslein, K., Tew, G. N., & Coughlin, E. B. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045664d · Cited by 502

Antimicrobial peptides in animals and their role in host defences

Brogden, K. A., Ackermann, M., McCray, P. B., & Tack, B. F. (2003) · International Journal of Antimicrobial Agents · doi:10.1016/s0924-8579(03)00180-8 · Cited by 458

Relationship of Membrane Curvature to the Formation of Pores by Magainin 2

Matsuzaki, K., Sugishita, K.-I., Ishibe, N., Ueha, M., Nakata, S., Miyajima, K., & Epand, R. M. (1998) · Biochemistry · doi:10.1021/bi980539y · Cited by 452

Mimicry of Antimicrobial Host-Defense Peptides by Random Copolymers

Mowery, B. P., Lee, S. E., Kissounko, D. A., Epand, R. F., Epand, R. M., Weisblum, B., Stahl, S. S., & Gellman, S. H. (2007) · Journal of the American Chemical Society · doi:10.1021/ja077288d · Cited by 443

Sequence-controlled polymerizations: the next Holy Grail in polymer science?

Lutz, J.-F. (2010) · Polymer Chemistry · doi:10.1039/b9py00329k · Cited by 443

Crystallization of Antimicrobial Pores in Membranes: Magainin and Protegrin

Yang, L., Weiss, T. M., Lehrer, R. I., & Huang, H. W. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76448-4 · Cited by 437

Molecular Basis for Membrane Selectivity of an Antimicrobial Peptide, Magainin 2

Matsuzaki, K., Sugishita, K., Fujii, N., & Miyajima, K. (1995) · Biochemistry · doi:10.1021/bi00010a034 · Cited by 419

Antimicrobial Polymers Prepared by ROMP with Unprecedented Selectivity: A Molecular Construction Kit Approach

Lienkamp, K., Madkour, A. E., Musante, A., Nelson, C. F., Nüsslein, K., & Tew, G. N. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801662y · Cited by 418

Mimicry of Host-Defense Peptides by Unnatural Oligomers: Antimicrobial β-Peptides

Porter, E. A., Weisblum, B., & Gellman, S. H. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0260871 · Cited by 379

Self-Immolative Polymers

Sagi, A., Weinstain, R., Karton, N., & Shabat, D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801065d · Cited by 366

Emerging trends in macromolecular antimicrobials to fight multi-drug-resistant infections

Engler, A. C., Wiradharma, N., Ong, Z. Y., Coady, D. J., Hedrick, J. L., & Yang, Y.-Y. (2012) · Nano Today · doi:10.1016/j.nantod.2012.04.003 · Cited by 357

The Role of Hydrophobicity in the Antimicrobial and Hemolytic Activities of Polymethacrylate Derivatives

Kuroda, K., Caputo, G. A., & DeGrado, W. F. (2009) · Chemistry – A European Journal · doi:10.1002/chem.200801523 · Cited by 346

Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy

Fantner, G. E., Barbero, R. J., Gray, D. S., & Belcher, A. M. (2010) · Nature Nanotechnology · doi:10.1038/nnano.2010.29 · Cited by 341

De Novo Design, Synthesis, and Characterization of Antimicrobial β-Peptides

Liu, D., & DeGrado, W. F. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0107475 · Cited by 339

Pore formation and translocation of melittin

Matsuzaki, K., Yoneyama, S., & Miyajima, K. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78115-3 · Cited by 339

Chemical Structure of Cationic Groups in Amphiphilic Polymethacrylates Modulates the Antimicrobial and Hemolytic Activities

Palermo, E. F., & Kuroda, K. (2009) · Biomacromolecules · doi:10.1021/bm900044x · Cited by 331

Bacterial programmed cell death: making sense of a paradox

Bayles, K. W. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3136 · Cited by 315

Structure–function relationships in peptoids: Recent advances toward deciphering the structural requirements for biological function

Fowler, S. A., & Blackwell, H. E. (2009) · Organic & Biomolecular Chemistry · doi:10.1039/b817980h · Cited by 292

Structure and Orientation of the Mammalian Antibacterial Peptide Cecropin P1 within Phospholipid Membranes

Gazit, E., Miller, I. R., Biggin, P. C., Sansom, M. S. P., & Shai, Y. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0293 · Cited by 283

Structure−Activity Studies of 14-Helical Antimicrobial β-Peptides: Probing the Relationship between Conformational Stability and Antimicrobial Potency

Raguse, T. L., Porter, E. A., Weisblum, B., & Gellman, S. H. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0270423 · Cited by 283

Structural determinants of antimicrobial activity in polymers which mimic host defense peptides

Palermo, E. F., & Kuroda, K. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2687-z · Cited by 281

Antibacterial and Hemolytic Activities of Pyridinium Polymers as a Function of the Spatial Relationship between the Positive Charge and the Pendant Alkyl Tail

Sambhy, V., Peterson, B. R., & Sen, A. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200702287 · Cited by 271

Structure−activity Relationships among Random Nylon-3 Copolymers That Mimic Antibacterial Host-Defense Peptides

Mowery, B. P., Lindner, A. H., Weisblum, B., Stahl, S. S., & Gellman, S. H. (2009) · Journal of the American Chemical Society · doi:10.1021/ja901613g · Cited by 257

Mechanically triggered heterolytic unzipping of a low-ceiling-temperature polymer

Diesendruck, C. E., Peterson, G. I., Kulik, H. J., Kaitz, J. A., Mar, B. D., May, P. A., White, S. R., Martínez, T. J., Boydston, A. J., & Moore, J. S. (2014) · Nature Chemistry · doi:10.1038/nchem.1938 · Cited by 248

Controlling macromolecular structures towards effective antimicrobial polymers

Ganewatta, M. S., & Tang, C. (2015) · Polymer · doi:10.1016/j.polymer.2015.03.007 · Cited by 246

Single Giant Unilamellar Vesicle Method Reveals Effect of Antimicrobial Peptide Magainin 2 on Membrane Permeability

Tamba, Y., & Yamazaki, M. (2005) · Biochemistry · doi:10.1021/bi051684w · Cited by 246

Escherichia coli Cell Surface Perturbation and Disruption Induced by Antimicrobial Peptides BP100 and pepR

Alves, C. S., Melo, M. N., Franquelim, H. G., Ferré, R., Planas, M., Feliu, L., Bardají, E., Kowalczyk, W., Andreu, D., Santos, N. C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.130955 · Cited by 244

Direct Visualization of Membrane Leakage Induced by the Antibiotic Peptides: Maculatin, Citropin, and Aurein

Ambroggio, E. E., Separovic, F., Bowie, J. H., Fidelio, G. D., & Bagatolli, L. A. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.066589 · Cited by 241

Unexpected Relationships between Structure and Function in α,β-Peptides: Antimicrobial Foldamers with Heterogeneous Backbones

Schmitt, M. A., Weisblum, B., & Gellman, S. H. (2004) · Journal of the American Chemical Society · doi:10.1021/ja048546z · Cited by 232

Controlled Depolymerization: Stimuli-Responsive Self-Immolative Polymers

Peterson, G. I., Larsen, M. B., & Boydston, A. J. (2012) · Macromolecules · doi:10.1021/ma300817v · Cited by 220

Stimuli-responsive dendrimers in drug delivery

Wang, H., Huang, Q., Chang, H., Xiao, J., & Cheng, Y. (2016) · Biomaterials Science · doi:10.1039/c5bm00532a · Cited by 219

Bioactivation of Self-Immolative Dendritic Prodrugs by Catalytic Antibody 38C2

Shamis, M., Lode, H. N., & Shabat, D. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039052p · Cited by 218

Guanylated Polymethacrylates: A Class of Potent Antimicrobial Polymers with Low Hemolytic Activity

Locock, K. E. S., Michl, T. D., Valentin, J. D. P., Vasilev, K. A., Hayball, J. D., Qu, Y., Traven, A., Griesser, H. J., Meagher, L., & Häußler, M. (2013) · Biomacromolecules · doi:10.1021/bm401128r · Cited by 216

Antimicrobial Metallopolymers and Their Bioconjugates with Conventional Antibiotics against Multidrug-Resistant Bacteria

Zhang, J., Chen, Y. P., Miller, K. P., Ganewatta, M. S., Bam, M., Yan, Y., Nagarkatti, M., Decho, A. W., & Tang, C. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5011338 · Cited by 216

Snorkeling of lysine side chains in transmembrane helices: how easy can it get?

Strandberg, E., & Killian, J. A. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00475-7 · Cited by 210

Recent Developments in Antimicrobial Polymers: A Review

Santos, M., Fonseca, A., Mendonça, P., Branco, R., Serra, A., Morais, P., & Coelho, J. (2016) · Materials · doi:10.3390/ma9070599 · Cited by 210

Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation

Wilmes, M., Cammue, B. P. A., Sahl, H.-G., & Thevissen, K. (2011) · Natural Product Reports · doi:10.1039/c1np00022e · Cited by 207

Cationic Spacer Arm Design Strategy for Control of Antimicrobial Activity and Conformation of Amphiphilic Methacrylate Random Copolymers

Palermo, E. F., Vemparala, S., & Kuroda, K. (2012) · Biomacromolecules · doi:10.1021/bm300342u · Cited by 198

Block versus Random Amphiphilic Copolymers as Antibacterial Agents

Oda, Y., Kanaoka, S., Sato, T., Aoshima, S., & Kuroda, K. (2011) · Biomacromolecules · doi:10.1021/bm200780r · Cited by 198

Rationally designed dual functional block copolymers for bottlebrush-like coatings: In vitro and in vivo antimicrobial, antibiofilm, and antifouling properties

Gao, Q., Yu, M., Su, Y., Xie, M., Zhao, X., Li, P., & Ma, P. X. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.01.061 · Cited by 188

Sequence Requirements and an Optimization Strategy for Short Antimicrobial Peptides

Hilpert, K., Elliott, M. R., Volkmer-Engert, R., Henklein, P., Donini, O., Zhou, Q., Winkler, D. F. H., & Hancock, R. E. W. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.08.014 · Cited by 183

Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids. Evidence for the snorkel hypothesis.

Mishra, V., Palgunachari, M. N., Segrest, J. P., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37266-6 · Cited by 179

Rational Design of Single-Chain Polymeric Nanoparticles That Kill Planktonic and Biofilm Bacteria

Nguyen, T., Lam, S. J., Ho, K. K. K., Kumar, N., Qiao, G. G., Egan, S., Boyer, C. A., & Wong, E. H. H. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00203 · Cited by 179

Role of Cationic Group Structure in Membrane Binding and Disruption by Amphiphilic Copolymers

Palermo, E. F., Lee, D.-K., Ramamoorthy, A., & Kuroda, K. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp1083357 · Cited by 174

Biologically active polycations, 4. Synthesis and antimicrobial activity of poly(trialkylvinylbenzylammonium chloride)s

Ikeda, T., Tazuke, S., & Suzuki, Y. (1984) · Die Makromolekulare Chemie · doi:10.1002/macp.1984.021850503 · Cited by 173

Bacterial Membranes as Predictors of Antimicrobial Potency

Epand, R. M., Rotem, S., Mor, A., Berno, B., & Epand, R. F. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8062327 · Cited by 172

Dual Mechanism of Bacterial Lethality for a Cationic Sequence-Random Copolymer that Mimics Host-Defense Antimicrobial Peptides

Epand, R. F., Mowery, B. P., Lee, S. E., Stahl, S. S., Lehrer, R. I., Gellman, S. H., & Epand, R. M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.047 · Cited by 171

Multiple Orientation of Melittin inside a Single Lipid Bilayer Determined by Combined Vibrational Spectroscopic Studies

Chen, X., Wang, J., Boughton, A. P., Kristalyn, C. B., & Chen, Z. (2007) · Journal of the American Chemical Society · doi:10.1021/ja067446l · Cited by 170

“Doubly Selective” Antimicrobial Polymers: How Do They Differentiate between Bacteria?

Lienkamp, K., Kumar, K., Som, A., Nüsslein, K., & Tew, G. N. (2009) · Chemistry – A European Journal · doi:10.1002/chem.200802558 · Cited by 169

Biocidal Activity of Polystyrenes That Are Cationic by Virtue of Protonation

Gelman, M. A., Weisblum, B., Lynn, D. M., & Gellman, S. H. (2004) · Organic Letters · doi:10.1021/ol036341+ · Cited by 164

A Cascade Biodegradable Polymer Based on Alternating Cyclization and Elimination Reactions

DeWit, M. A., & Gillies, E. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja905343x · Cited by 162

Amplified release through the stimulus triggered degradation of self-immolative oligomers, dendrimers, and linear polymers

Wong, A. D., DeWit, M. A., & Gillies, E. R. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.09.012 · Cited by 160

Antibacterial and Hemolytic Activities of Quaternary Pyridinium Functionalized Polynorbornenes

Eren, T., Som, A., Rennie, J. R., Nelson, C. F., Urgina, Y., Nüsslein, K., Coughlin, E. B., & Tew, G. N. (2008) · Macromolecular Chemistry and Physics · doi:10.1002/macp.200700418 · Cited by 160

Synthetic Mimics of Antimicrobial Peptides—A Versatile Ring‐Opening Metathesis Polymerization Based Platform for the Synthesis of Selective Antibacterial and Cell‐Penetrating Polymers

Lienkamp, K., & Tew, G. N. (2009) · Chemistry – A European Journal · doi:10.1002/chem.200900049 · Cited by 159

Biodegradable Broad-Spectrum Antimicrobial Polycarbonates: Investigating the Role of Chemical Structure on Activity and Selectivity

Chin, W., Yang, C., Ng, V. W. L., Huang, Y., Cheng, J., Tong, Y. W., Coady, D. J., Fan, W., Hedrick, J. L., & Yang, Y. Y. (2013) · Macromolecules · doi:10.1021/ma4019685 · Cited by 159

Investigating the Effect of Increasing Charge Density on the Hemolytic Activity of Synthetic Antimicrobial Polymers

AL‐Badri, Z. M., Som, A., Lyon, S. K., Nelson, C. F., Nüsslein, K. R., & Tew, G. N. (2008) · Biomacromolecules · doi:10.1021/bm800569x · Cited by 156

Kinetics of Pore Formation by an Antimicrobial Peptide, Magainin 2, in Phospholipid Bilayers

Matsuzaki, K., Murase, O., & Miyajima, K. (1995) · Biochemistry · doi:10.1021/bi00039a009 · Cited by 154

Synthetic mimics of antimicrobial peptides

Som, A., Vemparala, S., Ivanov, I. N., & Tew, G. N. (2008) · Biopolymers · doi:10.1002/bip.20970 · Cited by 152

Polyglyoxylates: A Versatile Class of Triggerable Self-Immolative Polymers from Readily Accessible Monomers

Fan, B., Trant, J. F., Wong, A. D., & Gillies, E. R. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504727u · Cited by 152

Antimicrobial Polycarbonates: Investigating the Impact of Nitrogen-Containing Heterocycles as Quaternizing Agents

Ng, V. W. L., Tan, J. P. K., Leong, J., Voo, Z. X., Hedrick, J. L., & Yang, Y. Y. (2014) · Macromolecules · doi:10.1021/ma402641p · Cited by 148

Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights

Ramamoorthy, A. (2009) · Solid State Nuclear Magnetic Resonance · doi:10.1016/j.ssnmr.2009.03.003 · Cited by 147

Synthetic Random Copolymers as a Molecular Platform To Mimic Host-Defense Antimicrobial Peptides

Takahashi, H., Caputo, G. A., Vemparala, S., & Kuroda, K. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00114 · Cited by 143

Isolation of an ovine pulmonary surfactant-associated anionic peptide bactericidal for Pasteurella haemolytica.

Brogden, K. A., Lucca, A. J. D., Bland, J. M., & Elliott, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.412 · Cited by 138

Synthetic Antimicrobial Oligomers Induce a Composition-Dependent Topological Transition in Membranes

Yang, L., Gordon, V. D., Mishra, A., Som, A., Purdy, K. R., Davis, M. A., Tew, G. N., & Wong, G. C. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072310o · Cited by 134

Comparison of Facially Amphiphilic versus Segregated Monomers in the Design of Antibacterial Copolymers

Gabriel, G. J., Maegerlein, J. A., Nelson, C. F., Dabkowski, J. M., Eren, T., Nüsslein, K. R., & Tew, G. N. (2008) · Chemistry - A European Journal · doi:10.1002/chem.200801233 · Cited by 134

Design of Synthetic Antimicrobial Peptides Based on Sequence Analogy and Amphipathicity

Tossi, A., Tarantino, C., & Romeo, D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0549a.x · Cited by 133

Hemocompatibility of hydrophilic antimicrobial copolymers of alkylated 4-vinylpyridine

Allison, B. C., Applegate, B. M., & Youngblood, J. P. (2007) · Biomacromolecules · doi:10.1021/bm7004627 · Cited by 129

Hydrophilic Modifications of an Amphiphilic Polynorbornene and the Effects on its Hemolytic and Antibacterial Activity

Colak, S., Nelson, C. F., Nüsslein, K. R., & Tew, G. N. (2009) · Biomacromolecules · doi:10.1021/bm801129y · Cited by 128

Antibacterial Studies of Cationic Polymers with Alternating, Random, and Uniform Backbones

Song, A., Walker, S. G., Parker, K. A., & Sampson, N. S. (2011) · ACS Chemical Biology · doi:10.1021/cb100413w · Cited by 123

Sequence Control as a Powerful Tool for Improving the Selectivity of Antimicrobial Polymers

Kuroki, A., Sangwan, P., Qu, Y., Peltier, R., Sánchez-Cano, C., Moat, J., Dowson, C. G., Williams, E. G. L., Locock, K. E. S., Hartlieb, M., et al. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b14996 · Cited by 123

M olecular Design, Structures, and Activity of Antimicrobial Peptide‐ M imetic Polymers

Takahashi, H., Palermo, E. F., Yasuhara, K., Caputo, G. A., & Kuroda, K. (2013) · Macromolecular Bioscience · doi:10.1002/mabi.201300126 · Cited by 121

Ternary Nylon-3 Copolymers as Host-Defense Peptide Mimics: Beyond Hydrophobic and Cationic Subunits

Chakraborty, S., Liu, R., Hayouka, Z., Chen, X., Ehrhardt, J., Lu, Q., Burke, E. G., Yang, Y., Weisblum, B., Wong, G. C. L., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja507576a · Cited by 119

Continuous Head-to-Tail Depolymerization: An Emerging Concept for Imparting Amplified Responses to Stimuli-Responsive Materials

Phillips, S. T., & DiLauro, A. M. (2014) · ACS Macro Letters · doi:10.1021/mz5000784 · Cited by 116

Design and Synthesis of Self-Degradable Antibacterial Polymers by Simultaneous Chain- and Step-Growth Radical Copolymerization

Mizutani, M., Palermo, E. F., Thoma, L. M., et al. (2012) · Biomacromolecules · doi:10.1021/bm300254s · Cited by 115

Cationic Methacrylate Polymers as Topical Antimicrobial Agents against Staphylococcus aureus Nasal Colonization

Thoma, L. M., Boles, B. R., & Kuroda, K. (2014) · Biomacromolecules · doi:10.1021/bm500557d · Cited by 114

Synthesis and characterization of non-leaching biocidal polyurethanes

Grapski, J. A., & Cooper, S. L. (2001) · Biomaterials · doi:10.1016/s0142-9612(00)00412-9 · Cited by 109

Modulating Antimicrobial Activity and Mammalian Cell Biocompatibility with Glucosamine-Functionalized Star Polymers

Wong, E. H. H., Khin, M. M., Ravikumar, V., Si, Z., Rice, S. A., & Chan‐Park, M. B. E. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.5b01766 · Cited by 109

Structure and Mode of Action of Microplusin, a Copper II-chelating Antimicrobial Peptide from the Cattle Tick Rhipicephalus (Boophilus) microplus

da Silva, F. D., Rezende, C. A. M., Rossi, D. C. P., Esteves, E., Dyszy, F. H., Schreier, S., Gueiros‐Filho, F. J., de Campos, C. B. L., Pires, J. R., & Daffre, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016410 · Cited by 105

Amphipathic antibacterial agents using cationic methacrylic polymers with natural rosin as pendant group

Chen, Y., Wilbon, P. A., Chen, Y. P., Zhou, J., Nagarkatti, M., Wang, C., Chu, F., Decho, A. W., & Tang, C. (2012) · RSC Advances · doi:10.1039/c2ra21675b · Cited by 100

Self‐Powered Microscale Pumps Based on Analyte‐Initiated Depolymerization Reactions

Zhang, H., Yeung, K., Robbins, J. S., Pavlick, R. A., Wu, M., Liu, R., Sen, A., & Phillips, S. T. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201107787 · Cited by 97

Effect of glycounits on the antimicrobial properties and toxicity behavior of polymers based on quaternized DMAEMA

Álvarez‐Paino, M., Muñoz‐Bonilla, A., López, F., Gómez-Garcés, J. L., Heuts, J. P. A., & Fernández‐García, M. (2014) · Biomacromolecules · doi:10.1021/bm5014876 · Cited by 97

Lipid Segregation Explains Selective Toxicity of a Series of Fragments Derived from the Human Cathelicidin LL-37

Epand, R. F., Wang, G., Berno, B., & Epand, R. M. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00321-09 · Cited by 94

The effects of polymer topology and chain length on the antimicrobial activity and hemocompatibility of amphiphilic ternary copolymers

Namivandi‐Zangeneh, R., Kwan, R. J., Nguyen, T., Yeow, J., Byrne, F. L., Oehlers, S. H., Wong, E. H. H., & Boyer, C. A. (2017) · Polymer Chemistry · doi:10.1039/c7py01069a · Cited by 94

Polycarbonates with Potent and Selective Antimicrobial Activity toward Gram-Positive Bacteria

Nimmagadda, A., Liu, X., Teng, P., Su, M., Li, Y., Qiao, Q., Khadka, N. K., Sun, X., Pan, J., Xu, H., et al. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.6b01385 · Cited by 93

Side Chain Degradable Cationic–Amphiphilic Polymers with Tunable Hydrophobicity Show in Vivo Activity

Uppu, D. S. S. M., Samaddar, S., Hoque, J., Konai, M. M., Krishnamoorthy, P., Shome, B. R., & Haldar, J. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.6b01057 · Cited by 92

Characterization of Nonbiological Antimicrobial Polymers in Aqueous Solution and at Water−Lipid Interfaces from All-Atom Molecular Dynamics

Ivanov, I. N., Vemparala, S., Pophristic, V., Kuroda, K., DeGrado, W. F., McCammon, J. A., & Klein, M. L. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0564665 · Cited by 91

RAFT-derived antimicrobial polymethacrylates: elucidating the impact of end-groups on activity and cytotoxicity

Michl, T. D., Locock, K. E. S., Stevens, N. E., Hayball, J. D., Vasilev, K. A., Postma, A., Qu, Y., Traven, A., Häußler, M., Meagher, L., et al. (2014) · Polymer Chemistry · doi:10.1039/c4py00652f · Cited by 90

Self-immolative nanoparticles for simultaneous delivery of microRNA and targeting of polyamine metabolism in combination cancer therapy

Xie, Y., Stewart, T. M., Wang, Y., Yu, F., Li, J., Marton, L. J., Casero, R. A., & Oupický, D. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.12.017 · Cited by 90

Cell Selectivity and Mechanism of Action of Antimicrobial Model Peptides Containing Peptoid Residues

Song, Y. M., Park, Y., Lim, S. S., Yang, S., Woo, E., Park, I., Lee, J. S., Kim, J. I., Hahm, K., Kim, Y., et al. (2005) · Biochemistry · doi:10.1021/bi050765p · Cited by 87

Learning from Host-Defense Peptides: Cationic, Amphipathic Peptoids with Potent Anticancer Activity

Huang, W., Seo, J., Willingham, S. B., Czyzewski, A. M., Gonzalgo, M. L., Weissman, I. L., & Barron, A. E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090397 · Cited by 84

A Critical Evaluation of Random Copolymer Mimesis of Homogeneous Antimicrobial Peptides

Hu, K., Schmidt, N. W., Zhu, R., Jiang, Y., Lai, G. H., Wei, G., Palermo, E. F., Kuroda, K., Wong, G. C. L., & Yang, L. (2013) · Macromolecules · doi:10.1021/ma302577e · Cited by 77

Antibacterial low molecular weight cationic polymers: dissecting the contribution of hydrophobicity, chain length and charge to activity

Grace, J. L., Huang, J. X., Cheah, S.-E., Truong, N. P., Cooper, M. A., Li, J., Davis, T. P., Quinn, J. F., Velkov, T., & Whittaker, M. R. (2016) · RSC Advances · doi:10.1039/c5ra24361k · Cited by 77

Antimicrobial Peptide Mimicking Primary Amine and Guanidine Containing Methacrylamide Copolymers Prepared by Raft Polymerization

Exley, S. E., Paslay, L. C., Sahukhal, G. S., Abel, B. A., Brown, T. D., McCormick, C. L., Heinhorst, S., Koul, V., Choudhary, V., Elasri, M. O., et al. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b01162 · Cited by 76

Revealing the Lytic Mechanism of the Antimicrobial Peptide Gomesin by Observing Giant Unilamellar Vesicles

Domingues, T. M., Riske, K. A., & Miranda, A. (2010) · Langmuir · doi:10.1021/la100662a · Cited by 75

A reduction sensitive cascade biodegradable linear polymer

DeWit, M. A., Beaton, A., & Gillies, E. R. (2010) · Journal of Polymer Science Part A Polymer Chemistry · doi:10.1002/pola.24180 · Cited by 72

Helical cationic antimicrobial peptide length and its impact on membrane disruption

Juba, M. L., Porter, D. K., Williams, E. H., Rodriguez, C. A., Barksdale, S. M., & Bishop, B. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.01.007 · Cited by 70

Rapid and Reliable Detection of Antimicrobial Peptide Penetration into Gram-Negative Bacteria Based on Fluorescence Quenching

Benincasa, M., Pacor, S., Gennaro, R., & Scocchi, M. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01620-08 · Cited by 68

Self‐Activation in De Novo Designed Mimics of Cell‐Penetrating Peptides

Som, A., Tezgel, A. Ö., Gabriel, G. J., & Tew, G. N. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201101535 · Cited by 67

Antibacterial Activity of Geminized Amphiphilic Cationic Homopolymers

Wang, H., Shi, X., Yu, D., Zhang, J., Yang, G., Cui, Y., Sun, K., Wang, J., & Yan, H. (2015) · Langmuir · doi:10.1021/acs.langmuir.5b03182 · Cited by 63

Cationic Poly(benzyl ether)s as Self-Immolative Antimicrobial Polymers

Ergene, C., & Palermo, E. F. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b01062 · Cited by 63

High Efficiency Antimicrobial Thiazolium and Triazolium Side-Chain Polymethacrylates Obtained by Controlled Alkylation of the Corresponding Azole Derivatives

Tejero, R., López, D., López, F., Gómez-Garcés, J. L., & Fernández‐García, M. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b00427 · Cited by 62

Polymer Composites – Polyolefin Fractionation – Polymeric Peptidomimetics – Collagens

Abe, A., Kausch, H., Möller, M., & Pasch, H. (2013) · Advances in polymer science · doi:10.1007/978-3-642-34330-8 · Cited by 61

Cationic amphiphilic non-hemolytic polyacrylates with superior antibacterial activity

Punia, A., He, E., Lee, K., Banerjee, P., & Yang, N. (2014) · Chemical Communications · doi:10.1039/c4cc01583e · Cited by 61

Developments in antimicrobial polymers

Ren, W., Cheng, W., Wang, G., & Liu, Y. (2016) · Journal of Polymer Science Part A Polymer Chemistry · doi:10.1002/pola.28446 · Cited by 60

Fatty Acid Comprising Lysine Conjugates: Anti-MRSA Agents That Display In Vivo Efficacy by Disrupting Biofilms with No Resistance Development

Konai, M. M., & Haldar, J. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00055 · Cited by 60

Biodegradable Antimicrobial Polycarbonates with In Vivo Efficacy against Multidrug‐Resistant MRSA Systemic Infection

Cheng, J., Chin, W., Dong, H., Xu, L., Zhong, G., Huang, Y., Li, L., Xu, K., Wu, M., Hedrick, J. L., et al. (2015) · Advanced Healthcare Materials · doi:10.1002/adhm.201500471 · Cited by 58

Insight into the Mechanism of Antimicrobial Poly(phenylene ethynylene) Polyelectrolytes: Interactions with Phosphatidylglycerol Lipid Membranes†Langmuir 25th Year: Molecular and macromolecular self-assemblies

Ding, L., Chi, E. Y., Chemburu, S., Ji, E., Schanze, K. S., López, G. P., & Whitten, D. G. (2009) · Langmuir · doi:10.1021/la901457t · Cited by 58

Nonhemolytic and Antibacterial Acrylic Copolymers with Hexamethyleneamine and Poly(ethylene glycol) Side Chains

Punia, A., Mancuso, A., Banerjee, P., & Yang, N. (2015) · ACS Macro Letters · doi:10.1021/acsmacrolett.5b00102 · Cited by 56

Bactericidal Peptidomimetic Polyurethanes with Remarkable Selectivity against Escherichia coli

Mankoci, S., Kaiser, R. L., Sahai, N., Barton, H. A., & Joy, A. (2017) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.7b00309 · Cited by 50

Orientation, Dynamics, and Lipid Interaction of an Antimicrobial Arylamide Investigated by 19 F and 31 P Solid-State NMR Spectroscopy

Su, Y., DeGrado, W. F., & Hong, M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103658h · Cited by 48

Nontoxic Cationic Coumarin Polyester Coatings Prevent Pseudomonas aeruginosa Biofilm Formation

Chamsaz, E. A., Mankoci, S., Barton, H. A., & Joy, A. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b12610 · Cited by 48

Self‐Immolative Poly(4,5‐dichlorophthalaldehyde) and its Applications in Multi‐Stimuli‐Responsive Macroscopic Plastics

DiLauro, A. M., Lewis, G. G., & Phillips, S. T. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201501320 · Cited by 46

Bactericidal cationic peptides involved in bacterial antagonism and host defence.

Hg, S. (1985) · PubMed · Cited by 45

Hydrophilic Phage-Mimicking Membrane Active Antimicrobials Reveal Nanostructure-Dependent Activity and Selectivity

Jiang, Y., Zheng, W., Kuang, L., Ma, H., & Liang, H. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00076 · Cited by 45

Enhancement of Cationic Antimicrobial Materials via Cholesterol Incorporation

Coady, D. J., Ong, Z. Y., Lee, P. S., Venkataraman, S., Chin, W., Engler, A. C., Yang, Y. Y., & Hedrick, J. L. (2013) · Advanced Healthcare Materials · doi:10.1002/adhm.201300554 · Cited by 44

Investigating the effects of L- to D-amino acid substitution and deamidation on the activity and membrane interactions of antimicrobial peptide anoplin

Won, A. M., Khan, M., Gustin, S., Akpawu, A., Seebun, D., Avis, T. J., Leung, B. O., Hitchcock, A. P., & Ianoul, A. I. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.11.010 · Cited by 37

Rational Design of Membrane‐Pore‐Forming Peptides

Pillong, M., Hiss, J. A., Schneider, P., Lin, Y., Posselt, G., Pfeiffer, B., Blatter, M., Müller, A. T., Bachler, S., Neuhaus, C. S., et al. (2017) · Small · doi:10.1002/smll.201701316 · Cited by 34

Roles of Salt and Conformation in the Biological and Physicochemical Behavior of Protegrin-1 and Designed Analogues: Correlation of Antimicrobial, Hemolytic, and Lipid Bilayer-Perturbing Activities

Lai, J. R., Epand, R. F., Weisblum, B., Epand, R. M., & Gellman, S. H. (2006) · Biochemistry · doi:10.1021/bi0617759 · Cited by 30

Pro-Antimicrobial Networks via Degradable Acetals (PANDAs) Using Thiol–Ene Photopolymerization

Amato, D. N., Amato, D. V., Mavrodi, O. V., Martin, W. B., Swilley, S. N., Parsons, K. H., Mavrodi, D. V., & Patton, D. L. (2017) · ACS Macro Letters · doi:10.1021/acsmacrolett.7b00009 · Cited by 29

Effect of Relative Arrangement of Cationic and Lipophilic Moieties on Hemolytic and Antibacterial Activities of PEGylated Polyacrylates

Punia, A., Lee, K., He, E., Mukherjee, S., Mancuso, A., Banerjee, P., & Yang, N. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161023867 · Cited by 20

Influence of lipid composition of model membranes on methacrylate antimicrobial polymer–membrane interactions

Baul, U., & Vemparala, S. (2017) · Soft Matter · doi:10.1039/c7sm01211j · Cited by 15

Structure–property relationships of antibacterial amphiphilic polymers derived from 2-aminoethyl acrylate

Punia, A., Debata, P. R., Banerjee, P., & Yang, N. (2015) · RSC Advances · doi:10.1039/c5ra17875d · Cited by 11

Polymers against Microorganisms: On the Race to Efficient Antimicrobial Materials

Rodríguez‐Hernández, J., & Rodríguez-Hernández (2016) · Cited by 10

Chemical Approaches to Prepare Antimicrobial Polymers

Rodríguez‐Hernández, J. (2016) · Springer eBooks · doi:10.1007/978-3-319-47961-3_3 · Cited by 2

Sanitizing agents for virus inactivation and disinfection

Lin, Q., Lim, J. Y. C., Xue, K., Yew, P. Y. M., Owh, C., Chee, P. L., & Loh, X. J. (2020) · VIEW · doi:10.1002/viw2.16 · Cited by 271

Unleashing the power of polymeric nanoparticles—Creative triumph against antibiotic resistance: A review

Naik, G. A. R. R., Roy, A. A., Mutalik, S., & Dhas, N. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134977 · Cited by 47