http://worldascience.com/journals/index.php/wassn <p>WAS<strong style="font-size: 0.875rem;"> Science Nature (WASSN) (<a class="is_text" href="https://portal.issn.org/resource/ISSN/2766-7715#">ISSN: 2766-7715</a>) </strong><span style="font-size: 0.875rem;"> is a comprehensive <strong>PEER-REVIEWED</strong> journal aiming to proceed science-society interactions. <strong>The open access</strong> strategy offers increased vulnerability of the research and help in dissemination of research results, as well. We believe that all accurate scientific results have to be published and disseminated by being freely accessible to all.</span></p> <h3><span style="color: #0000ff;">AIMS &amp; SCOPE</span></h3> <p>WAS Science Nature (WASSN) journal publishes multidisciplinary and interdisciplinary <strong>peer-reviewed</strong> research. WASSN accepts research in all subject areas of science, medicine, engineering, technology, social sciences and humanities. The submitted manuscripts are evaluated on the basis of high ethical standards, accurate methodology, scientific and perceived novelty.</p> <h3><span style="color: #0000ff;">Types of articles: </span></h3> <p><em><strong>Original research</strong></em> that contributes to the base of scientific knowledge, including interdisciplinary, replication studies, and negative or null results.<br /><em><strong>Systematic reviews</strong></em> whose methods ensure the comprehensive and unbiased sampling of existing literature.<br /><em><strong>Qualitative research</strong></em> that adheres to appropriate study design and reporting guidelines.<br /><em><strong>Other submissions </strong></em>that describes methods, software, databases, or other tools that if they follow the appropriate reporting guidelines.</p> <h3><span style="color: #0000ff;">Open Access Statement</span></h3> <p>WASSN is a peer-reviewed open-access journal. This implies that every content is available for free. Without previous permission from the author or publisher, users or institutions may read, download, copy, distribute, print, search, or link to the full texts of the articles or use them for any other legal purpose. </p> <p> </p> en-US [email protected] (World Advanced Science Edior ) [email protected] (Technical Support Contact) Fri, 10 Jul 2026 00:00:00 +0200 OJS 3.3.0.3 http://blogs.law.harvard.edu/tech/rss 60 http://worldascience.com/journals/index.php/wassn/article/view/51 <p><strong>Background:</strong> The rapid escalation of antimicrobial resistance (AMR), particularly among the "ESKAPE" pathogens, presents an existential threat to global clinical medicine. Because conventional small-molecule antibiotics are highly vulnerable to resistance acquisition via single-nucleotide polymorphisms or horizontal gene transfer, there is an urgent need to engineer next-generation therapeutics with resilient, biophysical modes of action. Antimicrobial peptides (AMPs) derived from the Class Insecta represent an evolutionary goldmine, offering robust host-defense platforms shaped by survival in pathogen-dense ecological niches.</p> <p><strong>Objective:</strong> This review addresses a historical fragmentation in literature by providing a translation-focused synthesis that comprehensively bridges upstream molecular regulatory networks with downstream pharmacological performance and modern formulation engineering.</p> <p><strong>Methods/Structure:</strong> The manuscript structurally classifies the four primary families of insect AMPs—linear $\alpha$-helical cecropins, disulfide-stabilized cysteine-rich defensins, intracellular-targeting proline-rich peptides (PrAMPs), and macromolecular glycine-rich proteins (e.g., diptericins, attacins)—and correlates their unique structural topography with specific, multi-target mechanisms of action. Furthermore, it maps the underlying upstream activation pathways, including the Toll, Immune Deficiency (Imd), and JAK-STAT cascades, while examining complementary humoral factors and antioxidant defense systems.</p> <p><strong>Results &amp; Discussion:</strong> While insect-derived AMPs exhibit exceptional <em>in vitro</em> potency, direct direct lysis mechanisms often cross-react with eukaryotic membranes, leading to mammalian cytotoxicity and hemolytic vulnerabilities. Moreover, native linear peptides suffer from rapid proteolytic degradation by host proteases, resulting in a short plasma half-life. This review evaluates how these challenges, alongside high chemical manufacturing costs and emerging microbial countermeasures (e.g., membrane remodeling, active efflux networks), have historically blocked clinical translation.</p> <p><strong>Conclusion &amp; Future Directions:</strong> To resolve these bottlenecks, we highlight cutting-edge 2026 strategies, emphasizing how artificial intelligence (AI)-driven generative and predictive modeling accelerates the <em>de novo</em> design of synthetic peptides with optimized therapeutic indices. Concurrently, we detail the implementation of chemical modifications (peptidomimetics, D-amino acid substitutions, cyclization, PEGylation) and advanced nanocarrier delivery frameworks (liposomes, nanoparticles, hydrogels) to systematically shield sequences from degradation, eliminate host toxicity, and chart a definitive regulatory roadmap toward successful clinical translation.</p> AlaaEddeen Seufi, M. Hamza, Sherifa H. Ahmed, Mona S. Azab, Mossad A. Salama, Shayma Mahmoud, Hanan T. Hamza, Fatma H. Galal Copyright (c) 2026 WAS Science Nature (WASSN) ISSN: 2766-7715 https://creativecommons.org/licenses/by-nc/4.0 http://worldascience.com/journals/index.php/wassn/article/view/51 Fri, 10 Jul 2026 00:00:00 +0200