Interest in natural biopreservatives has increased significantly due to growing consumer demand for safer and more environmentally friendly food preservation strategies. Antimicrobial peptides (AMPs), naturally occurring molecules (typically <10 kDa), have emerged as a promising alternative to synthetic chemical preservatives. Found in bacteria, fungi, plants, and animals, including humans, AMPs play a crucial role in innate immune defense. Their antibacterial and antioxidant effects enable them to prevent microbial spoilage and extend the shelf life of food, reducing the need for artificial additives. AMPs are biodegradable and environmentally friendly, and they specifically target harmful microorganisms, minimizing disruption to beneficial microorganisms. Despite their promising properties, challenges such as stability, cost and potential sensory impairment limit their wide application. Recent advances, such as encapsulation techniques and nanotechnology, have shown remarkable potential to improve the stability and functionality of AMPs in complex food systems. In addition, AMPs derived from edible mushrooms represent a sustainable and natural approach to food preservation and could offer effective solutions against foodborne pathogens and oxidative spoilage. This review examines the structural features, mechanisms of action and practical applications of AMPs in food protection, with a particular focus on their innovative integration with nanotechnology to address current food safety challenges.

Peptide-based vaccines offer a modular and readily manufacturable platform for both prophylactic and therapeutic immunization. However, their broader translation has been constrained by the limited capacity to predict protective immunity directly from sequence-level features. Recent advances in systems vaccinology and high-throughput immune profiling have substantially expanded the experimental evidence, while generative artificial intelligence now enables de novo design of peptide immunogens and multi-epitope antigens under precisely controlled constraints. This review approaches how these complementary developments are transforming peptide vaccine research, moving beyond classical reverse vaccinology and conventional epitope prediction toward integrated, data-driven design frameworks. We discuss key generative model architectures and conditioning strategies aligned with vaccine objectives, including approaches that account for structural presentation, antigen processing and population-level human leukocyte antigen (HLA) diversity. Central to this perspective is the requirement for rigorous experimental validation and for strengthening the computational–experimental feedback loop through iterative in vitro and in vivo testing informed by systems-level immune readouts. We highlight representative applications spanning infectious diseases, cancer immunotherapy and vector-borne vaccinology, and we outline major technical and translational challenges that must be addressed to enable robust real-world deployment. Finally, we propose future directions for precision peptide vaccinology, emphasizing standardized functional benchmarks, the development of richer curated datasets linking sequence space to immune outcomes, and the early incorporation of formulation and delivery constraints into generative design pipelines.

Acanthamoeba infections are hindered by limitations including prolonged treatment duration, cytotoxicity, limited efficacy against the resistant cystic stage, and a high rate of recurrence. Antimicrobial peptides (AMPs) demonstrate broad-spectrum antimicrobial activity, rapid mechanism of action, low potential for inducing resistance, and efficacy against both trophozoite and cyst forms, highlighting their potential as promising alternatives in the treatment of these infections. Herein, we report the amoebicidal activity of various peptides derived from cathelicidins and piscidins against Acanthamoeba castellanii Neff. Afterwards, the impact of the most effective peptide on the clinical features of a clinical strain of Acanthamoeba castellanii was evaluated using a fluorescence imaging system. Peptide OH_KR34 was the most active against A. castellanii Neff with an IC₅₀ values of 2.00 ± 0.58 µM. OH_KR34 was able to inhibit the clinical strain of A. castellanii (L10) with an IC₅₀ of 5.75 ± 0.30 μM. We demonstrated that the peptide OH_KR34 (related to OH-CATH) induces cytoskeletal damage and trigger apoptosis-like process by disrupting cell membrane permeability, mitochondrial dysfunction and DNA fragmentation. This antimicrobial peptide could therefore offer a potential target to develop new anti-parasitic drugs.