<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Malshikare, Hrushikesh</style></author><author><style face="normal" font="default" size="100%">Priyakumar, U. Deva</style></author><author><style face="normal" font="default" size="100%">Chatterjee, Prathit</style></author><author><style face="normal" font="default" size="100%">Sengupta, Durba</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mechanistic principles of antimicrobial peptides uncovered by charge density-based machine learning</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">62</style></volume><pages><style face="normal" font="default" size="100%">PMID 9610838</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Antimicrobial peptides (AMPs) are emerging as potent alternatives to conventional antibiotics, yet their diverse nature due to divergent mechanisms of action hinders rational design. Here, we present an electrostatics-stratified computational framework that uncovers key physicochemical principles governing AMP activity. Experimentally validated peptides were grouped by average charge per residue (i.e., the charge/length of the peptide) and analyzed through integrated sequence-, structure-, and chemistry-based descriptors. Distinct molecular signatures emerged across electrostatic regimes: low-charge/length peptides rely on amphipathic organization via structural compactness, whereas the intermediate-charge/length peptides exhibit balanced hydrophobicity and electrostatics. The high-charge peptides couple strong cationic attraction with lipophilicity and tryptophan anchoring to mainly disrupt membranes. Interestingly, hydrophobic moment, which is a measure of the amphipathicity, is found to be important in all three classes of AMPs. This study identifies distinguishing features of AMP sub-groups and suggests design guidelines for developing selective and potent next-generation AMPs.&lt;/p&gt;
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	Foreign&lt;/p&gt;
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	4.2&lt;/p&gt;
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