{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T04:22:41Z","timestamp":1772252561833,"version":"3.50.1"},"reference-count":33,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2019,2,10]],"date-time":"2019-02-10T00:00:00Z","timestamp":1549756800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Department of Biotechnology , Ministry of Science and Technology","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Data"],"abstract":"<jats:p>Antimicrobial peptides are ubiquitous molecules that form the innate immune system of organisms across all kingdoms of life. Despite their prevalence and early origins, they continue to remain potent natural antimicrobial agents. Antimicrobial peptides are therefore promising drug candidates in the face of overwhelming multi-drug resistance to conventional antibiotics. Over the past few decades, thousands of antimicrobial peptides have been characterized in vitro, and their efficacy data are now available in a multitude of public databases. Computational antimicrobial peptide design attempts typically use such data. However, utilizing heterogenous data aggregated from different sources presents significant drawbacks. In this report, we present a uniform dataset containing 20 antimicrobial peptides assayed against 30 organisms of Gram-negative, Gram-positive, mycobacterial, and fungal origin. We also present circular dichroism spectra for all antimicrobial peptides. We draw simple inferences from this data, and we discuss what characteristics are essential for antimicrobial peptide efficacy. We expect our uniform dataset to be useful for future projects involving computational antimicrobial peptide design.<\/jats:p>","DOI":"10.3390\/data4010027","type":"journal-article","created":{"date-parts":[[2019,2,12]],"date-time":"2019-02-12T03:18:20Z","timestamp":1549941500000},"page":"27","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["A Uniform In Vitro Efficacy Dataset to Guide Antimicrobial Peptide Design"],"prefix":"10.3390","volume":"4","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8468-9834","authenticated-orcid":false,"given":"Deepesh","family":"Nagarajan","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India"}]},{"given":"Tushar","family":"Nagarajan","sequence":"additional","affiliation":[{"name":"Department of Computer Science, University of Texas, Austin, TX 78751, USA"}]},{"given":"Neha","family":"Nanajkar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India"}]},{"given":"Nagasuma","family":"Chandra","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India"},{"name":"Centre for Biosystems Science and Engineering, Indian Institute of Science, Bangalore 560012, India"}]}],"member":"1968","published-online":{"date-parts":[[2019,2,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/nbt.2572","article-title":"Antimicrobial peptides stage a comeback","volume":"31","author":"Fox","year":"2013","journal-title":"Nat. Biotechnol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/S2213-2600(14)70061-X","article-title":"Assessment of the worldwide burden of critical illness: The intensive care over nations (ICON) audit","volume":"2","author":"Vincent","year":"2014","journal-title":"Lancet Respir. Med."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"D590","DOI":"10.1093\/nar\/gkh025","article-title":"APD: The antimicrobial peptide database","volume":"32","author":"Wang","year":"2004","journal-title":"Nucl. Acids Res."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1615\/CritRevImmunol.v20.i5.40","article-title":"Cationic antimicrobial peptides and their multifunctional role in the immune system","volume":"20","author":"Scott","year":"2000","journal-title":"Crit. Rev. Immunol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/S0021-9258(18)73041-X","article-title":"Bactericidal fractions from an aerobic sporulating bacillus","volume":"136","author":"Hotchkiss","year":"1940","journal-title":"J. Biol. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"585","DOI":"10.2174\/138920309789630589","article-title":"Anionic antimicrobial peptides from eukaryotic organisms","volume":"10","author":"Harris","year":"2009","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"11361","DOI":"10.1021\/bi960016v","article-title":"An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation","volume":"35","author":"Matsuzaki","year":"1996","journal-title":"Biochemistry"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1002\/jss.400020504","article-title":"A molecular model of membrane excitability","volume":"2","author":"Baumann","year":"1974","journal-title":"J. Supramol. Struct."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1002\/bip.10260","article-title":"Mode of action of membrane active antimicrobial peptides","volume":"66","author":"Shai","year":"2002","journal-title":"Pept. Sci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1074\/jbc.M117.805499","article-title":"Computational antimicrobial peptide design and evaluation against multidrug-resistant clinical isolates of bacteria","volume":"293","author":"Nagarajan","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2998","DOI":"10.1021\/bi00126a022","article-title":"Binding of tachyplesin I to DNA revealed by footprinting analysis: Significant contribution of secondary structure to DNA binding and implication for biological action","volume":"31","author":"Yonezawa","year":"1992","journal-title":"Biochemistry"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1574-6968.1998.tb12896.x","article-title":"Mechanism of antimicrobial action of indolicidin","volume":"160","author":"Subbalakshmi","year":"1998","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1128\/AAC.46.3.605-614.2002","article-title":"Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli","volume":"46","author":"Patrzykat","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"E1409","DOI":"10.1073\/pnas.1319900111","article-title":"Small cationic antimicrobial peptides delocalize peripheral membrane proteins","volume":"111","author":"Wenzel","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1128\/IAI.69.3.1402-1408.2001","article-title":"Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease","volume":"69","author":"Gusman","year":"2001","journal-title":"Infect. Immun."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"2539","DOI":"10.4049\/jimmunol.0901813","article-title":"Synthetic cationic peptide IDR-1002 provides protection against bacterial infections through chemokine induction and enhanced leukocyte recruitment","volume":"184","author":"Nijnik","year":"2010","journal-title":"J. Immunol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"947","DOI":"10.4049\/jimmunol.163.2.947","article-title":"Neutrophil defensins induce histamine secretion from mast cells: Mechanisms of action","volume":"163","author":"Befus","year":"1999","journal-title":"J. Immunol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1172\/JCI17545","article-title":"An angiogenic role for the human peptide antibiotic LL-37\/hCAP-18","volume":"111","author":"Koczulla","year":"2003","journal-title":"J. Clin. Investig."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1128\/AAC.43.4.782","article-title":"In vitro antibacterial properties of pexiganan, an analog of magainin","volume":"43","author":"Ge","year":"1999","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"12688","DOI":"10.1021\/bi00165a020","article-title":"Design of model amphipathic peptides having potent antimicrobial activities","volume":"31","author":"Blondelle","year":"1992","journal-title":"Biochemistry"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2511","DOI":"10.1128\/AAC.02218-12","article-title":"Rational design of engineered cationic antimicrobial peptides consisting exclusively of arginine and tryptophan, and their activity against multidrug-resistant pathogens","volume":"57","author":"Deslouches","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1128\/AAC.49.1.316-322.2005","article-title":"De novo generation of cationic antimicrobial peptides: Influence of length and tryptophan substitution on antimicrobial activity","volume":"49","author":"Deslouches","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2204","DOI":"10.1016\/j.biomaterials.2010.11.054","article-title":"Synthetic cationic amphiphilic \u03b1-helical peptides as antimicrobial agents","volume":"32","author":"Wiradharma","year":"2011","journal-title":"Biomaterials"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1111\/j.1747-0285.2010.01044.x","article-title":"Optimization of antibacterial peptides by genetic algorithms and cheminformatics","volume":"77","author":"Fjell","year":"2011","journal-title":"Chem. Biol. Drug Des."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Maccari, G., Di Luca, M., Nifos\u00ed, R., Cardarelli, F., Signore, G., Boccardi, C., and Bifone, A. (2013). Antimicrobial peptides design by evolutionary multiobjective optimization. PLoS Comput. Biol., 9.","DOI":"10.1371\/journal.pcbi.1003212"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1038\/nature05233","article-title":"A linguistic model for the rational design of antimicrobial peptides","volume":"443","author":"Loose","year":"2006","journal-title":"Nature"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.ijantimicag.2011.12.003","article-title":"YADAMP: Yet another database of antimicrobial peptides","volume":"39","author":"Piotto","year":"2012","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"D774","DOI":"10.1093\/nar\/gkp1021","article-title":"CAMP: A useful resource for research on antimicrobial peptides","volume":"38","author":"Thomas","year":"2010","journal-title":"Nucl. Acids Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"24482","DOI":"10.1038\/srep24482","article-title":"DRAMP: A comprehensive data repository of antimicrobial peptides","volume":"6","author":"Fan","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1038\/nprot.2007.521","article-title":"Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances","volume":"3","author":"Wiegand","year":"2008","journal-title":"Nat. Protoc."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1023\/A:1018698002314","article-title":"Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an \u03b1-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol\/water solution","volume":"9","author":"Gesell","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbapap.2003.09.004","article-title":"Antimicrobial peptides from ranid frogs: Taxonomic and phylogenetic markers and a potential source of new therapeutic agents","volume":"1696","author":"Conlon","year":"2004","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Data"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2306-5729\/4\/1\/27\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T12:30:58Z","timestamp":1760185858000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2306-5729\/4\/1\/27"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,2,10]]},"references-count":33,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2019,3]]}},"alternative-id":["data4010027"],"URL":"https:\/\/doi.org\/10.3390\/data4010027","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/463588","asserted-by":"object"}]},"ISSN":["2306-5729"],"issn-type":[{"value":"2306-5729","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,2,10]]}}}