Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics.

Packing behaviour of two predominant anionic phospholipids of bacterial cytoplasmic membranes

Prossnigg, F., Hickel, A., Pabst, G., & Lohner, K. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.04.004 · Cited by 41

Experimental concepts for linking the biological activities of antimicrobial peptides to their molecular modes of action

Malanović, N., Marx, L., Blondelle, S. E., Pabst, G., & Semeraro, E. F. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183275 · Cited by 40

Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayers

Salay, L. C., Ferreira, M., Oliveira, O. N., Nakaie, C. R., & Schreier, S. (2012) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2012.05.002 · Cited by 39

Membrane curvature stress and antibacterial activity of lactoferricin derivatives

Zweytick, D., Tumer, S., Blondelle, S. E., & Lohner, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.176 · Cited by 39

Antimicrobial activity, membrane interaction and structural features of short arginine-rich antimicrobial peptides

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N-acylated Peptides Derived from Human Lactoferricin Perturb Organization of Cardiolipin and Phosphatidylethanolamine in Cell Membranes and Induce Defects in Escherichia coli Cell Division

Zweytick, D., Japelj, B., Mileykovskaya, E., Zorko, M. S., Dowhan, W., Blondelle, S. E., Riedl, S., Jerala, R., & Lohner, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090228 · Cited by 38

Antimicrobial Peptides for Plant Disease Control. From Discovery to Application

Montesinos, E., Badosa, E., Cabrefiga, J., Planas, M., Feliu, L., & Bardajı́, E. (2012) · ACS symposium series · doi:10.1021/bk-2012-1095.ch012 · Cited by 38

Interaction of LL-37 human cathelicidin peptide with a model microbial-like lipid membrane

Majewska, M., Zamlynny, V., Pieta, I. S., Nowakowski, R., & Pięta, P. (2021) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2021.107842 · Cited by 37

Membrane perturbing activities and structural properties of the frog-skin derived peptide Esculentin-1a(1-21)NH2 and its Diastereomer Esc(1-21)-1c: Correlation with their antipseudomonal and cytotoxic activity

Loffredo, M. R., Ghosh, A., Harmouche, N., Casciaro, B., Luca, V., Bortolotti, A., Cappiello, F., Stella, L., Bhunia, A., Bechinger, B., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.09.009 · Cited by 37

The antibiotic peptaibol alamethicin from Trichoderma permeabilises Arabidopsis root apical meristem and epidermis but is antagonised by cellulase-induced resistance to alamethicin

Dotson, B. R., Soltan, D., Schmidt, J., Areskoug, M., Rabe, K., Swart, C., Widell, S., & Rasmusson, A. G. (2018) · BMC Plant Biology · doi:10.1186/s12870-018-1370-x · Cited by 37

Avengers against cancer: A new era of nano-biomaterial-based therapeutics

Kumar, N., Fazal, S., Miyako, E., Matsumura, K., & Rajan, R. (2021) · Materials Today · doi:10.1016/j.mattod.2021.09.020 · Cited by 36

Differential Scanning Calorimetry Studies of Phospholipid Membranes: The Interdigitated Gel Phase

Eric, A., & Phoebe, K. (2013) · InTech eBooks · doi:10.5772/51882 · Cited by 36

Antiplasmodial Activity of Lauryl-Lysine Oligomers

Radzishevsky, I. S., Krugliak, M., Ginsburg, H., & Mor, A. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01288-06 · Cited by 36

Update of Peptides with Antibacterial Activity

Vila‐Farrés, X., Giralt, E., & Vilà, J. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712804485818 · Cited by 34

Structure and Thermotropic Behavior of the Staphylococcus aureus Lipid Lysyl-Dipalmitoylphosphatidylglycerol

Danner, S., Pabst, G., Lohner, K., & Hickel, A. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.123422 · Cited by 34

Mammary Gland Expression of Antibacterial Peptide Genes to Inhibit Bacterial Pathogens Causing Mastitis

Zhang, J. X., Zhang, S. F., Wang, T. D., Guo, X., & Hu, R. (2007) · Journal of Dairy Science · doi:10.3168/jds.2007-0301 · Cited by 33

A novel antifungal peptide designed from the primary structure of a natural antimicrobial peptide purified from Argopecten purpuratus hemocytes

Arenas, G., Guzmán, F., Cárdenas, C., Mercado, L. A., & Marshall, S. H. (2009) · Peptides · doi:10.1016/j.peptides.2009.05.019 · Cited by 33

Analysis of membrane interactions of antibiotic peptides using ITC and biosensor measurements

Al-Kaddah, S., Reder-Christ, K., Klocek, G., Wiedemann, I., Brunschweiger, M., & Bendas, G. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.09.002 · Cited by 32

Biophysical approaches for exploring lipopeptide-lipid interactions

Munusamy, S., Condé, R., Bertrand, B., & Muñóz-Garay, C. (2020) · Biochimie · doi:10.1016/j.biochi.2020.01.009 · Cited by 31

Insights from Micro-second Atomistic Simulations of Melittin in Thin Lipid Bilayers

Upadhyay, S. K., Wang, Y., Zhao, T., & Ulmschneider, J. P. (2015) · The Journal of Membrane Biology · doi:10.1007/s00232-015-9807-8 · Cited by 31

Membrane Interacting Peptides: From Killers to Helpers

Dufourc, É. J., Buchoux, S., Toupé, J., Sani, M., Jean-Francois, F. L., Khemtémourian, L., Grélard, A., Courrèges, C., Laguerre, M. S., Elezgaray, J., et al. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312804142138 · Cited by 30

Antimicrobial activity of the antibacterial peptide PMAP-36 and its analogues

Zhou, J., Liu, Y., Shen, T., Chen, L., Zhang, C., Cai, K., Liao, C., & Wang, C. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.103712 · Cited by 30

Membrane-targeted synergistic activity of docosahexaenoic acid and lysozyme against Pseudomonas aeruginosa

Martinez, J. G., Waldon, M., Huang, Q., Alvarez, S., Oren, A., Sandoval, N., Du, M., Zhou, F., Zenz, A., Lohner, K., et al. (2008) · Biochemical Journal · doi:10.1042/bj20081505 · Cited by 30

Conformational behavior of temporin A and temporin L in aqueous solution: A computational/experimental study

D’Abramo, M., Rinaldi, A. C., Bozzi, A., Amadei, A., Mignogna, G., Nola, A. D., & Aschi, M. (2005) · Biopolymers · doi:10.1002/bip.20404 · Cited by 29

Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region

Voegele, A., Subrini, O., Sapay, N., Ladant, D., & Chenal, A. (2017) · Toxins · doi:10.3390/toxins9110369 · Cited by 31

Headgroup structure and fatty acid chain length of the acidic phospholipids modulate the interaction of membrane mimetic vesicles with the antimicrobial peptide protegrin‐1

Jing, W., Prenner, E. J., Vogel, H. J., Waring, A. J., Lehrer, R. I., & Lohner, K. (2005) · Journal of Peptide Science · doi:10.1002/psc.702 · Cited by 29

Interaction of a novel antimicrobial peptide isolated from the venom of solitary bee Colletes daviesanus with phospholipid vesicles and Escherichia coli cells

Čujová, S., Bednářová, L., Slaninová, J., Straka, J., & Čeřovský, V. (2014) · Journal of Peptide Science · doi:10.1002/psc.2681 · Cited by 28

Reversible Liposome Association Induced by LAH4: A Peptide with Potent Antimicrobial and Nucleic Acid Transfection Activities

Marquette, A., Lorber, B., & Bechinger, B. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.02.042 · Cited by 28

Interactions of oritavancin, a new semi-synthetic lipoglycopeptide, with lipids extracted from Staphylococcus aureus

Domènech, Ò., Dufrêne, Y. F., Françoise Van Bambeke, A., Tukens, P. M., & Mingeot‐Leclercq, M. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.06.011 · Cited by 28

Pulmonary Collectins Selectively Permeabilize Model Bacterial Membranes Containing Rough Lipopolysaccharide

Kuzmenko, A. I., Wu, H., & McCormack, F. X. (2006) · Biochemistry · doi:10.1021/bi0522652 · Cited by 27

Effects of Aib residues insertion on the structural–functional properties of the frog skin-derived peptide esculentin-1a(1–21)NH2

Biondi, B., Casciaro, B., Grazia, A. D., Cappiello, F., Luca, V., Crisma, M., & Mangoni, M. L. (2016) · Amino Acids · doi:10.1007/s00726-016-2341-x · Cited by 27

Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data

Langham-Putrow, A., Waring, A. J., & Kaznessis, Y. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-11 · Cited by 27

Enhanced leishmanicidal activity of cryptopeptide chimeras from the active N1 domain of bovine lactoferrin

Silva, T., Abengózar, M. Á., Fernández‐Reyes, M., Andreu, D., Nazmi, K., Bolscher, J. G. M., Bastos, M., & Rivas, L. (2012) · Amino Acids · doi:10.1007/s00726-012-1304-0 · Cited by 26

Improved model systems for bacterial membranes from differing species: Theimportance of varying composition in PE/PG/cardiolipin ternary mixtures

Lopes, S. C. D. N., Neves, C., Eaton, P. J., & Gameiro, P. (2012) · Molecular Membrane Biology · doi:10.3109/09687688.2012.700491 · Cited by 26

In vitro leishmanicidal activity of antimicrobial peptide KDEL against Leishmania tarentolae

Cao, L., Jiang, W., Cao, S., Zhao, P., Liu, J., Dong, H. Y., Guo, Y., Liu, Q., & Gong, P. (2019) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmz128 · Cited by 24

A Fourier Transformation based Method to Mine Peptide Space for Antimicrobial Activity

Nagarajan, V., Kaushik, N., Murali, B., Zhang, C., Lakhera, S., Elasri, M. O., & Deng, Y. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-s2-s2 · Cited by 24

A natural peptide and its variants derived from the processing of infectious pancreatic necrosis virus (IPNV) displaying enhanced antimicrobial activity: A novel alternative for the control of bacterial diseases

Claudio, J., Guzmán, F., Cárdenas, C., Alberício, F., & Marshall, S. H. (2011) · Peptides · doi:10.1016/j.peptides.2011.01.026 · Cited by 23

Computational Design of Biologically Active Anticancer Peptides and Their Interactions with Heterogeneous POPC/POPS Lipid Membranes

Singh, M., Kumar, V., Sikka, K., Thakur, R. K., Harioudh, M. K., Mishra, D. P., Ghosh, J. K., & Siddiqi, M. I. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00348 · Cited by 23

Antimicrobial activity of peptides derived from human ß‐amyloid precursor protein

Papareddy, P., Mörgelin, M., Walse, B., Schmidtchen, A., & Malmsten, M. (2012) · Journal of Peptide Science · doi:10.1002/psc.1439 · Cited by 22

Divorcing folding from function: How acylation affects the membrane-perturbing properties of an antimicrobial peptide

Vad, B. S., Thomsen, L. A., Bertelsen, K., Franzmann, M., Pedersen, J. M., Nielsen, S. B., Vosegaard, T., Valnickova, Z., Skrydstrup, T., Enghild, J. J., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.006 · Cited by 22

Dermaseptin 01 as antimicrobial peptide with rich biotechnological potential: study of peptide interaction with membranes containing Leishmania amazonensis lipid‐rich extract and membrane models

Salay, L. C., Nobre, T. M., Colhone, M. C., Zaniquelli, M. E. D., Ciancaglini, P., Stábeli, R. G., Leite, J. R. S. A., & Zucolotto, V. (2011) · Journal of Peptide Science · doi:10.1002/psc.1392 · Cited by 22

Antibiotics

Vardanyan, R., & Hruby, V. I. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-411492-0.00030-4 · Cited by 23

Functionalization of Bacterial Cellulose with the Antimicrobial Peptide KR-12 via Chimerical Cellulose-Binding Peptides

van Zyl, E. M., & Coburn, J. M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031462 · Cited by 21

Determining the Mode of Action Involved in the Antimicrobial Activity of Synthetic Peptides: A Solid-State NMR and FTIR Study

Lorin, A., Noël, M., Provencher, M.-È., Turcotte, V., Cardinal, S., Lagüe, P., Voyer, N., & Auger, M. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.08.055 · Cited by 21

Blood Compatibility—An Important but Often Forgotten Aspect of the Characterization of Antimicrobial Peptides for Clinical Application

Harm, S., Lohner, K., Fichtinger, U., Schildböck, C., Zottl, J., & Hartmann, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215426 · Cited by 21

New Insights into the Translocation Route of Enrofloxacin and Its Metalloantibiotics

Ribeiro, C., Lopes, S. C. D. N., & Gameiro, P. (2011) · The Journal of Membrane Biology · doi:10.1007/s00232-011-9368-4 · Cited by 21

Panurgines, novel antimicrobial peptides from the venom of communal bee Panurgus calcaratus (Hymenoptera: Andrenidae)

Čujová, S., Slaninová, J., Monincová, L., Fučı́k, V., Bednářová, L., Štokrová, J., Hovorka, O., Vobůrka, Z., Straka, J., & Čeřovský, V. (2013) · Amino Acids · doi:10.1007/s00726-013-1482-4 · Cited by 21

Antimicrobial peptide interactions with bacterial cell membranes

Khavani, M., Mehranfar, A., & Mofrad, M. R. K. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2304683 · Cited by 20

Staphyloxanthin Photolysis Potentiates Low Concentration Silver Nanoparticles in Eradication of Methicillin-Resistant Staphylococcus aureus

Jusuf, S., Hui, J., Dong, P., & Cheng, J. (2020) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.9b10209 · Cited by 20

Bilayer lipid composition modulates the activity of dermaseptins, polycationic antimicrobial peptides

Duclohier, H. (2006) · European Biophysics Journal · doi:10.1007/s00249-006-0047-9 · Cited by 20

Molecular Dynamics Studies on the Bacterial Membrane Pore Formation by Small Molecule Antimicrobial Agents

Daison, F. A., Kumar, N., Balakrishnan, S., Venugopal, K., Elango, S., & Sokkar, P. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c01049 · Cited by 19

Adsorption of the antimicrobial peptide arenicin and its linear derivative to model membranes – A maximum insertion pressure study

Travkova, O. G., & Brezesinski, G. (2013) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.01.010 · Cited by 19

Synergies with and Resistance to Membrane-Active Peptides

Kmeck, A., Tancer, R. J., Ventura, C. R., & Wiedman, G. R. (2020) · Antibiotics · doi:10.3390/antibiotics9090620 · Cited by 19

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function

Reiß, K., & Bhakdi, S. (2012) · Medical Microbiology and Immunology · doi:10.1007/s00430-012-0260-3 · Cited by 16

Antimicrobial C3a –Biology, Biophysics, and Evolution

Malmsten, M., & Schmidtchen, A. (2007) · Springer eBooks · doi:10.1007/978-0-387-71767-8_11 · Cited by 18

Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells

Weghuber, J., Aichinger, M. C., Brameshuber, M. O., Wieser, S., Ruprecht, V., Plochberger, B., Madl, J., Hörner, A., Reipert, S., Lohner, K., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.06.007 · Cited by 17

Membrane structure and interactions of a short Lycotoxin I analogue

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Revisiting Peptide Amphiphilicity for Membrane Pore Formation

Lorin, A., Noël, M., Provencher, M.-È., Turcotte, V., Masson, C., Cardinal, S., Lagüe, P., Voyer, N., & Auger, M. (2011) · Biochemistry · doi:10.1021/bi201335t · Cited by 16

A PiggyBac mediated approach for lactoferricin gene transfer in bovine mammary epithelial stem cells for management of bovine mastitis

Sharma, N., Huynh, D. L., Kim, S. W., Ghosh, M., Sodhi, S. S., Singh, A. K., Kim, N. E., Lee, S., Hussain, K., Oh, S. J., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.22210 · Cited by 16

Scorpion Venom: New Promise in the Treatment of Cancer

Rave, L. J. G., Muñoz-Bravo, A. X., Sierra-Castrillo, J., Marín, L. M. R., & Pereira, C. C. (2019) · Acta Biológica Colombiana · doi:10.15446/abc.v24n2.71512 · Cited by 16

Use of X-ray scattering to aid the design and delivery of membrane-active drugs

Pabst, G., Zweytick, D., Prassl, R., & Lohner, K. (2012) · European Biophysics Journal · doi:10.1007/s00249-012-0821-9 · Cited by 14

The antimicrobial peptide Magainin-2 interacts with BamA impairing folding of E. coli membrane proteins

Somma, A. D., Canè, C., Moretta, A., Illiano, A., Pinto, G., Cavasso, D., Amoresano, A., Paduano, L., & Duilio, A. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.1013788 · Cited by 13

Structural Basis for Antimicrobial Activity of Lasiocepsin

Monincová, L., Buděšı́nský, M., Čujová, S., Čeřovský, V., & Veverka, V. (2013) · ChemBioChem · doi:10.1002/cbic.201300509 · Cited by 13

Crabrolin, a natural antimicrobial peptide: structural properties

Aschi, M., Bozzi, A., Luzi, C., Bouchemal, N., & Sette, M. (2017) · Journal of Peptide Science · doi:10.1002/psc.3013 · Cited by 13

Structural characterization and biological activity of Crabrolin peptide isoforms with different positive charge

Aschi, M., Perini, N., Bouchemal, N., Luzi, C., Savarin, P., Migliore, L., Bozzi, A., & Sette, M. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.183055 · Cited by 13

The potential for antimicrobial peptides to improve fish health in aquaculture

Falcó, A., Martínez‐López, A., Coll, J.-L., & Estepa, A. (2012) · Elsevier eBooks · doi:10.1533/9780857095732.3.457 · Cited by 12

The Equilibrium of Bacterial Microecosystem: Probiotics, Pathogenic Bacteria, and Natural Antimicrobial Substances in Semen

Miao, X., Zhao, Y., Zhu, L. D., Zeng, Y., Yang, C., Zhang, R., Lund, A. K., & Zhang, M. (2024) · Microorganisms · doi:10.3390/microorganisms12112253 · Cited by 11

Recombinant Active Peptides and their Therapeutic Functions

Ajingi, Y. S., Rukying, N., Aroonsri, A., & Jongruja, N. (2021) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201022666210702123934 · Cited by 12

Antimicrobial Activity of the Antibacterial Peptide PMAP-GI24 and Its Analogs

Liu, Y., Yan, Z., Chai, J., Zhou, J., & Wang, C. (2020) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-020-10026-6 · Cited by 10

Computational screening of antimicrobial peptides for Acinetobacter baumannii

Majumder, A., Biswal, M. R., & Prakash, M. K. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219693 · Cited by 10

Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: a vibrational study

Morales, M. C. S., Juárez, A. C., Montich, G. G., & Álvarez, R. M. S. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.03.009 · Cited by 10

Direct Functional Protein Delivery with a Peptide into Neonatal and Adult Mammalian Inner Ear In Vivo

Zhang, K., Cheng, X., Zhao, L., Huang, M., Tao, Y., Zhang, H., Rosenholm, J. M., Zhuang, M., Chen, Z., Chen, B., et al. (2020) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2020.06.023 · Cited by 9

Antiplasmodial Properties of Acyl-Lysyl Oligomers in Culture and Animal Models of Malaria

Zaknoon, F., Wein, S., Krugliak, M., Meir, O., Rotem, S., Ginsburg, H., Vial, H. J., & Mor, A. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00129-11 · Cited by 9

Elucidating the anticancer activities of guanidinium-functionalized amphiphilic random copolymers by varying the structure and composition in the hydrophobic monomer

Tay, J., Zhao, Y., Hedrick, J. L., & Yang, Y. Y. (2021) · Theranostics · doi:10.7150/thno.60711 · Cited by 9

LFchimera: a synthetic mimic of the two antimicrobial domains of bovine lactoferrin

Ligtenberg, A. J. M., Bikker, F. J., & Bolscher, J. G. M. (2021) · Biochemistry and Cell Biology · doi:10.1139/bcb-2020-0285 · Cited by 9

Antimicrobial agents

Musumeci, T., & Puglisi, G. (2013) · Elsevier eBooks · doi:10.1533/9781908818348.305 · Cited by 9

The potential of AFM in studying the role of the nanoscale amphipathic nature of (lipo)-peptides interacting with lipid bilayers

Mescola, A., Ragazzini, G., Facci, P., & Alessandrini, A. (2022) · Nanotechnology · doi:10.1088/1361-6528/ac80c9 · Cited by 8

Electrochemical and AFM study of the interaction of recombinant human cathelicidin LL-37 with various supported bilayer lipid membranes

Gál, M., Sokolová, R., Naumowicz, M., Hı́veš, J., & Krahulec, J. (2018) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2018.01.019 · Cited by 8

One Drug Multiple Targets: An Approach To Predict Drug Efficacies on Bacterial Strains Differing in Membrane Composition

Majumder, A., Biswal, M. R., & Prakash, M. K. (2019) · ACS Omega · doi:10.1021/acsomega.8b02862 · Cited by 8

Expanding therapeutic strategies for intracellular bacterial infections through conjugates of apoptotic body–antimicrobial peptides

Marín, V. N., Buccini, D. F., Arboleda, J. W., Cardoso, M. H. E. S., & Franco, O. L. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.103444 · Cited by 7

Modifying Membranotropic Action of Antimicrobial Peptide Gramicidin S by Star-like Polyacrylamide and Lipid Composition of Nanocontainers

Ващенко, О. В., Berest, V. P., Sviechnikova, L. V., Kutsevol, N. V., Kasian, N. A., Sofronov, D. S., & Skorokhod, O. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168691 · Cited by 9

In vitro antibacterial activities of the methanol extract of Ziziphus mucronata Willd . subsp. mucronata Willd.

Olajuyigbe, O. O., & Afolayan, A. J. (2011) · Journal of Medicinal Plants Research · doi:10.5897/jmpr.9000732 · Cited by 7

Evaluation of iso-α-acid and β-acid extracts from hops (Humulus lupulus L.) on fermentation by rumen microbes in dual-flow continuous culture fermenters

Salfer, I. J., Fessenden, S. W., & Stern, M. D. (2019) · Animal Feed Science and Technology · doi:10.1016/j.anifeedsci.2019.114385 · Cited by 7

Evaluation of proline-rich antimicrobial peptides as potential lead structures for novel antimycotics against Cryptococcus neoformans

Brakel, A., Grochow, T., Fritsche, S., Knappe, D., Krizsan, A., Fietz, S. A., Alber, G., Hoffmann, R., & Müller, U. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1328890 · Cited by 7

Lead Informed Artificial Intelligence Mining of Antitubercular Host Defense Peptides

Biswas, D., Benson, S., Matunis, A. R., Gebretsadik, G., Wertz, A., StPierre, B. J., Schacht, N. A., Yan, Y., Gebremichael, H. Y., Wong, P. K., et al. (2025) · Biomacromolecules · doi:10.1021/acs.biomac.5c00244 · Cited by 6

Immunoliposomes: A Multipurpose Strategy in Breast Cancer Targeted Therapy

Barrajón‐Catalán, E., Maria, P., Falcó, A., Saceda, M., Catania, A., & Micol, V. (2011) · InTech eBooks · doi:10.5772/23998 · Cited by 6

Influence of First‐Line Antibiotics on the Antibacterial Activities of Acetone Stem Bark Extract of Acacia mearnsii De Wild. against Drug‐Resistant Bacterial Isolates

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