INTRODUCTION/OBJECTIVE:The development of novel peptide-based therapeutics offers a promising strategy to overcome the limitations associated with conventional antibacterial drugs. This study aimed to design and synthesize a new series of lipidated pentapeptide derivatives containing unusual amino acids and to evaluate their antibacterial and antifungal potential. METHODS:A series of lipidated pentapeptides incorporating unconventional amino acids was designed and synthesized to enhance structural diversity, membrane interaction, amphiphilicity, and resistance to enzymatic degradation. Lipophilic moieties were introduced to improve peptide stability and biological performance. The synthesized compounds were characterized using standard analytical techniques and evaluated for their antibacterial and antifungal activities against selected Gram-positive and Gram-negative bacterial strains and pathogenic fungi. RESULTS:Several lipidated pentapeptide derivatives exhibited promising antibacterial activity against both Gram-positive and Gram-negative bacteria. In addition, notable antifungal activity was observed against pathogenic fungal strains. The results demonstrated that lipidation significantly enhanced the antimicrobial efficacy of the peptides. Among these peptide derivatives, compound 6a exhibited antibacterial activity against E. coli with MIC = 150 μg/mL, whereas compound 6b showed activity against S. aureus with MIC = 250 μg/mL. Compound 6c demonstrated the strongest antifungal activity against Candida albicans (MIC = 40 μg/mL), while compound 6e showed activity against Aspergillus niger (MIC = 80 μg/mL). DISCUSSION:The findings highlight peptide lipidation as an effective structural modification strategy to improve membrane interaction, bioactivity, and enzymatic stability of antimicrobial peptides. The incorporation of unusual amino acids further contributed to enhanced resistance against degradation, supporting their therapeutic potential. CONCLUSION:This study demonstrates that lipidated pentapeptide derivatives represent promising candidates for next-generation antimicrobial agents. Peptide lipidation emerges as a valuable approach for developing stable and potent peptide-based therapies to combat bacterial and fungal infections.
Abstract: Changes to the metabolic pathways of cancer cells present a plethora of possibilities for the therapeutic targeting of tumor cell metabolism. These alterations primarily involve the expression and regulation of proteins. Despite ongoing advancements and new targets, improving targeted drug delivery to cancer cells remains an area of active exploration. Mitochondria, the dynamic organelles central to cell survival and death, have become a promising target in cancer therapy due to their crucial role in cellular metabolism and metastasis. Differences between healthy and cancerous mitochondria, such as membrane potential, energy production, and genetic mutations, offer a unique opportunity for selective therapeutic targeting. Approaches to target the mitochondria of tumor cells have focused on metabolic inhibitors, photosensitizers, mitochondria-homing peptides, and functionalized nanoparticles. Compared to traditional drug delivery methods, peptide-functionalized nanoparticles provide greater stability, improved cellular uptake and retention, superior targeting, and remarkable flexibility in controlling the structure and function of designed conjugates. Peptide conjugation further enhances the biocompatibility and bioavailability of nanotherapeutics, delivering treatments that are not only more effective but also less toxic, and the ability to overcome drug resistance makes them a highly promising approach. This review highlights the recent progress in the development of mitochondria-homing peptides and peptide-functionalized nanoparticles, as well as peptide-based drug nanocarrier delivery methods, which show promising abilities to enhance the specific targeting and delivery of therapeutic drugs to cancer cells.
Background/Aim: Studies on Antimicrobial Peptides (AMPs) have shown their potential to inhibit cancer cell proliferation and induce cancer cell death. These discoveries raise the question of whether such anticancer properties can be enhanced using peptide modification methods. Therefore, this study aims to determine whether modifications to AMPs derived from aquatic sources can enhance their anticancer properties. Materials and Methods: A review of studies published from 2014 to 2024 was conducted using Google Scholar and ScienceDirect databases, with keywords and Boolean operators. Results: A total of 9 studies met the inclusion criteria. The reported methods of modification in these studies included peptide modifications, nanoencapsulation, and amino acid sequence scrambling. Among these studies, most reported increased stability, selectivity, and cytotoxicity towards cancer cells, while also reducing cytotoxicity towards normal human tissues Discussion: The findings suggest that peptide modification may improve anticancer activity by enhancing peptide stability, cellular uptake, delivery efficiency, and cancer-cell selectivity. However, the included studies varied in peptide sequence, modification method, cancer cell model, and evaluation indicators; therefore, the findings should be interpreted as potential evidence rather than definitive proof. Conclusion: These findings highlight the potential of peptide modifications in enhancing anticancer activity, underscoring the need for further research to optimize cancer treatment strategies.
Ever since the first monumental discovery in 1921, peptide science has evolved into the field of therapeutic peptides (TPs), whose unique biochemical properties bridge the gaps associated with small molecules and biologics. Despite the fascinating therapeutic potential of TPs, such as lower immunogenicity, targeting specificity, binding affinity, favorable safety profiles, relatively easy synthesis, chemical flexibility, and diversity in physiological functions, the use of TPs in clinical settings is hampered by their shortcomings. Persistent issues such as poor oral bioavailability, susceptibility to enzymatic degradation, and short in vivo half-life limit their clinical application. This review provides a comprehensive overview of the evolving landscape of peptide therapeutics, with emphasis on innovative strategies to overcome the aforementioned challenges. Key advancements include peptide-drug conjugates (PDCs), peptide-nanoparticle conjugates (PNCs), synergistic peptide combinations, stimuli-responsive smart peptide systems, multifunctional peptides, as well as peptide-directed delivery of genetic products such as CRISPR technology and RNA therapeutics. In particular, the review focuses on the latest cutting-edge innovations in TP applications such as cancer theranostics, immunotherapy, gene delivery systems, and precision nanomedicine. Moreover, the integration of artificial intelligence (AI)-driven models in tumor diagnostics, treatment decisionmaking, peptide design, and peptide discovery has served as a pivotal advancement in the utilization of bioinformatic technologies for enhanced diagnostic precision and improved treatment efficiency through machine learning. Highlights of current advances and future directions in this review aim to provide research and translational insights into therapeutic peptide design, delivery, and nextgeneration peptide-based therapeutics.
Encapsulation technology is vital in food, pharmaceutical, and biomedical fields for protecting and delivering sensitive bioactive compounds. Proteins, due to their biocompatibility, biodegradability, and functional diversity, are increasingly used as carriers to enhance stability, bioavailability, and controlled release of bioactives. However, environmental factors such as pH, ionic strength, and enzymatic degradation can limit protein performance. This article reviews novel structural designs and modification strategies for protein-based delivery systems to improve encapsulation efficiency, stability, and targeted delivery of bioactive compounds. The study covers a range of protein architectures, including self-assembled nanostructures, protein nanoparticles, micelles, hydrogels, and hybrid protein-polymer systems. Techniques such as coacervation, crosslinking, and stimuli-responsive mechanisms are discussed to enhance delivery properties. Encapsulation efficiency, protection against degradation, controlled release, and bioavailability enhancement are analyzed. Novel protein structures, such as self-assembled nanocages and hybrid composites, demonstrated superior encapsulation and protection of bioactives against environmental and gastrointestinal degradation. Cross-linking and stimuli-responsive carriers enable targeted and controlled release. Encapsulation techniques such as spray drying, enzymatic cross-linking, and protein-polymer conjugation improve the mechanical and chemical stability of delivery systems. Codelivery platforms and surface functionalization further improve targeted absorption and therapeutic efficacy. Applications span the food, nutraceutical, pharmaceutical, and biomedical sectors, demonstrating promising results in enhancing the stability of functional ingredients, improving drug delivery, and advancing tissue engineering. Innovative protein-based delivery systems with tailored structural modifications offer enhanced encapsulation, protection, and controlled bioactive release, overcoming traditional limitations. Continued advancements in protein engineering and nanotechnology are crucial for optimizing these systems for clinical and industrial use, though challenges such as scalability and enzymatic degradation remain to be addressed.
INTRODUCTION:Diabetes mellitus is a chronic metabolic disorder that is frequently complicated by impaired wound healing, resulting in diabetic foot ulcers, amputations, and long-term disability. Conventional wound management strategies often fail due to persistent inflammation, oxidative stress, vascular dysfunction, and neuropathy. Recent advances in nanotechnology and biomarker research have emerged as promising approaches to improve diabetic wound healing outcomes. METHODS:A comprehensive literature review was conducted using PubMed, ScienceDirect, Elsevier, Web of Science, and Google Scholar to identify relevant studies published up to January 2025. Peerreviewed original research articles and reviews were screened using keywords related to diabetic wound healing, nanotherapeutics, nanoparticles, biomarkers, tissue engineering, and clinical translation. RESULTS:Nanotherapeutic systems, including metallic nanoparticles, polymeric nanoparticles, nanofibres, lipid-based carriers, hydrogels, and bioengineered exosomes, have demonstrated antimicrobial, pro-angiogenic, anti-inflammatory, and antioxidant effects in preclinical and clinical studies. These systems promote accelerated wound closure, enhance collagen deposition, improve angiogenesis, and reduce the inflammatory burden. Additionally, emerging biomarkers, such as microRNAs, cytokines, and angiogenic factors, provide valuable insights into wound progression, therapeutic response, and tissue regeneration. The integration of biomarker monitoring with nanocarrier-based delivery systems supports a personalised and adaptive wound care strategy. DISCUSSION:The combined application of nanotherapeutics and biomarker-based diagnostics addresses key pathological barriers in diabetic wound healing and offers improved therapeutic precision. However, translational challenges remain, including biosafety concerns, long-term toxicity, regulatory complexities, and variability in clinical outcomes. CONCLUSION:Nanotechnology-based therapeutics integrated with biomarker-driven assessment represent a promising and evolving paradigm for DM wound management, with the potential to enhance healing efficiency and support personalised treatment approaches; further large-scale clinical validation is warranted.
Inteins are self-excising protein elements that catalyze their own removal from host polypeptides and mediate the ligation of the surrounding exteins, generating mature and functional proteins without the requirement for external cofactors or energy sources. Since their discovery, inteins have attracted considerable interest due to their unique catalytic mechanisms, structural diversity, and broad applicability. Extensive progress in deciphering the molecular basis of cis- and trans-splicing inteins has facilitated the rational design and engineering of improved variants with enhanced efficiency, controllability, and substrate tolerance. These advances have significantly expanded their practical utility. Distinctive features such as compact architecture, high fidelity of splicing, orthogonal activity, minimal cytotoxicity, and irreversible function position inteins as powerful molecular tools in biotechnology and biomedicine. Their applications are increasingly diverse, ranging from fundamental protein engineering tasks such as protein purification, site-specific modification, and selenoprotein production to more translational uses, including microbial drug targeting, intein-based biosensing, targeted gene delivery, and therapeutic gene editing. In addition, conditional inteins, engineered to respond to environmental or molecular cues, are opening new avenues in synthetic biology and biomedicine, enabling precise control over protein function in complex cellular contexts. This review provides a comprehensive overview of intein biology, classification, and mechanistic insights, followed by a discussion of recent developments in their biotechnological and biomedical applications. Particular attention is given to challenges that continue to limit broader adoption, such as incomplete splicing, extein compatibility issues, and context-dependent efficiency. Finally, we highlight emerging opportunities in the field, including the computational design of orthogonal intein libraries, integration with high-throughput screening methods, and the incorporation of artificial intelligence to accelerate intein engineering and application discovery. Collectively, these developments underscore the transformative potential of inteins as versatile molecular tools poised to impact diverse areas of life sciences and therapeutic innovation.
Phosphodiesterase type 5 inhibitors (PDE5-Is) have emerged as potential therapeutic agents for neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), and multiple sclerosis (MS). Originally developed for cardiovascular disorders, PDE5-Is have gained significant attention for their neuroprotective effects due to their ability to modulate intracellular signaling pathways. These inhibitors exert their effects by increasing nitric oxide synthase expression, elevating cyclic guanosine monophosphate (cGMP) levels, and activating protein kinase G (PKG), leading to improved synaptic plasticity, neuronal survival, and cognitive enhancement. By targeting these molecular pathways, PDE5-Is help regulate neuroinflammation, oxidative stress, mitochondrial dysfunction, and neuronal apoptosis, which are key pathological features of neurodegenerative disorders. Several preclinical studies have demonstrated that PDE5-Is can reduce neuroinflammation, enhance neurogenesis, and improve mental performance in animal models of AD, PD, and MS. Additionally, these agents have shown promise in mitigating β-amyloid and tau pathology in AD, improving dopamine signalling in PD, and exerting immunomodulatory effects in MS. Furthermore, emerging research suggests that PDE5-Is may protect against neuronal cell death and improve cognitive function following cerebral ischemia by enhancing cerebral blood flow, reducing excitotoxicity, and promoting neurovascular coupling. Despite these promising findings, the clinical translation of PDE5-Is for neurodegenerative diseases remains in its early stages. Challenges, such as blood-brain barrier permeability, optimal dosing strategies, and long-term safety, must be addressed through further research. Nevertheless, given their multifaceted mechanisms of action, PDE5-Is represent a novel and exciting therapeutic approach that warrants deeper investigation in both preclinical and clinical settings for the treatment of neurodegenerative diseases.
Food Protein-derived Amyloid Fibrils (FPAFs) are rapidly gaining attention for their unique functional properties, offering new ways to improve texture and stability in plant-based and clean-label foods. These nanofibrils show superior gelling, emulsifying, and water-binding properties, supporting sustainable food innovation. However, the safety of FPAFs remains a topic of debate. In vitro gastrointestinal models show that fibrils from β-lactoglobulin and lysozyme are degraded into non-amyloidogenic oligopeptides during digestion, with no residual β-sheet-rich fragments left to induce further amyloid formation. In contrast, certain amyloid fibrils derived from legumes resist digestive enzymes and exhibit cytotoxicity in human epithelial cells at high concentrations. The presence of heat-stable amyloid A (AA) fibrils in animal-based products, such as foie gras, raises theoretical concerns about transmissible amyloidosis, especially in individuals with chronic inflammation. Most food-grade fibrils lack the pathogenic structures seen in disease-related amyloids, yet their potential to trigger protein misfolding or bypass intestinal barriers is under ongoing investigation. This review critically evaluates the dual nature of food protein-derived amyloid fibrils by integrating their functional advantages with emerging safety concerns. Future research must explore real food matrix effects, long-term exposure, and relevant biomarkers to clarify the safety of FPAFs. With strict regulation and comprehensive risk evaluation, FPAFs could sustainably transform food textures while minimizing potential health concerns.
BACKGROUND:The peptide Phα1β, derived from the venom of Phoneutria nigriventer, has been extensively investigated for its antinociceptive properties, primarily associated with modulation of ion channels and inflammatory pathways. However, its effects on oxidative stress and immune cell function remain incompletely understood. OBJECTIVE:This study aimed to investigate the effects of recombinant Phα1β (rPhα1β) on Reactive Oxygen Species (ROS) production and inflammatory mediator release in human immune cells. METHODS:Human neutrophils were isolated and stimulated to evaluate ROS production using a luminol-dependent chemiluminescence assay. The involvement of the protein kinase C (PKC) pathway was assessed using pharmacological modulators, including phorbol dibutyrate (PDB) and calphostin C. Cytokine levels were measured to determine the impact of rPhα1β on inflammatory responses. RESULTS:rPhα1β significantly reduced ROS production in human neutrophils. This effect was comparable to that observed with PKC inhibition and was reversed by PKC activation, suggesting modulation of the PKC/NADPH oxidase axis. In parallel, rPhα1β markedly decreased IL-6 levels, while exerting minimal effects on IL-4 and IL-10. Additionally, modulation of CCR5-related signaling was observed, indicating a potential effect on chemokine-mediated inflammatory pathways. CONCLUSION:These findings demonstrate that rPhα1β acts as a modulator of oxidative stress and inflammatory signaling in human immune cells. Its ability to reduce ROS production and selectively inhibit pro-inflammatory mediators suggests a mechanism involving the PKC/NADPH oxidase pathway. This study expands the current understanding of venom-derived peptides and highlights rPhα1β as a promising candidate for targeting redox-dependent inflammatory processes.
The endoplasmic reticulum (ER) is essential for protein synthesis, folding, maturation, transport, and calcium storage in mammalian cells. Perturbations in ER homeostasis, caused by stressors such as hypoxia, oxidative stress, or infection result in the accumulation of unfolded or misfolded proteins, triggering ER stress. To restore equilibrium, cells activate the unfolded protein response (UPR), a conserved adaptive mechanism mediated by three major ER transmembrane anchored stress sensors: IRE1, PERK, and ATF6. These sensors coordinate translational attenuation, chaperone upregulation, protein degradation, and lipid synthesis to mitigate ER stress and sustain cell survival. However, chronic or dysregulation UPR can induce apoptosis, inflammation, or autophagy. Viruses exploit ER stress and UPR pathway to promote their replication, immune evasion, and persistent infection, highlighting the dual role of the UPR in both host defense and viral survival. A comprehensive understanding of viral modulation of the UPR may reveal novel therapeutic opportunities, offering potential antiviral strategies by targeting host stress response pathways. This review explores how viruses use the UPR to control cell stress and metabolic pathways, and thereby enhance replication and progeny formation, or undergo cell death.
BACKGROUND:Epitope immunodominance describes the phenomenon whereby some antigenic epitopes preferentially elicit immune responses, whereas other epitopes remain subdominant or immunologically silent. Epitope immunodominance hierarchies are the result of coordinated molecular, structural, and cellular mechanisms. These hierarchies emerge from selective immune recognition processes that balance effective immunity and self-tolerance mechanisms. OBJECTIVE:The aim of this study is to describe the molecular, structural, and cellular parameters that mediate epitope immunodominance in antigens. In addition, it details how central and peripheral tolerance mechanisms influence epitope selection and immunodominance hierarchies in T- and B-cell responses. CONCLUSION:Epitope immunodominance arises from molecular and structural characteristics, including the nature of the antigen, the level of protein structure, host genetic factors, and immune regulatory mechanisms. Epitope immunodominance hierarchies depend on multiple factors, including the structural accessibility of epitopes, the epitope density, the distinctive binding affinities of antigen-derived peptides to MHC molecules, the availability of T cells able to recognize peptide-MHC complexes, the molecular stability of conformational epitopes recognized by BCRs, and the efficiency of antigen processing by antigen-presenting cells. Collectively, these factors focus immune recognition, determining whether specific epitopes dominate the immune response or remain immunologically silent.
Calcitonin gene-related peptide (CGRP), a neuropeptide with α and β isoforms, is a pivotal regulator connecting the neural, immune, and gastrointestinal systems. This comprehensive analysis delineates the evidence-based mechanistic roles of CGRP within the microbiome-gut-brain axis, focusing on its bidirectional modulation of enteric and central nervous system pathways. Both α- and β-CGRP are widely expressed in sensory and enteric neurons, where they govern vasodilation, intestinal motility, secretion, and mucosal homeostasis. CGRP-mediated signaling integrates gut microbiota-derived cues with central neurocircuitry, influencing visceral sensitivity, immune activation, and behavioral states such as anxiety and satiety. Furthermore, CGRP interacts with major neurotransmitter systems-including serotonin (5-HT), histamine, dopamine, and glutamatethereby linking peripheral microbial activity to central pain and emotional processing. We discuss isoform-specific and receptor-level mechanisms (e.g., CLR/RAMP1) as evidence permits and highlight gaps in translating preclinical findings to human physiology. Although CGRP has significant roles in other systems, such as in metabolism and pancreatic function, these are beyond the scope of this review, which focuses specifically on the neuro-immune-gastrointestinal interface. Collectively, CGRP emerges as a critical neuroendocrine mediator in coordinating communication across the microbiota-gut-brain axis. A deeper understanding of its spatiotemporal dynamics and isoformspecific functions will be crucial for the development of targeted therapeutic strategies for CGRPrelated disorders affecting both neurological and gastrointestinal systems.
BACKGROUND:Diabetes, a chronic metabolic disorder, is associated with severe health complications, including impaired wound healing, affecting approximately 25% of diabetic individuals worldwide. Factors such as neuropathy, chronic vascular diseases, retinopathy, infections, and non-traumatic lower limb amputations contribute to the incidence and severity of diabetic wounds. OBJECTIVE:To explore the pathophysiology of diabetic wounds, the role of insulin in wound healing, and the efficacy of advanced drug delivery systems-particularly insulin-based topical formulations- in improving healing outcomes. METHODS:This review examines the impact of physiological factors, including oxidative stress, chronic inflammation, impaired angiogenesis, and hyperglycemia, on diabetic wounds. It also analyzes the role of topical insulin delivered via transferosomes entrapped in organogels in enhancing localized treatment, sustained drug release, and patient adherence. RESULTS:Insulin resistance significantly impairs wound healing by promoting oxidative stress, inflammation, and impaired angiogenesis, thereby complicating treatment. Advanced drug delivery systems, particularly insulin-based topical formulations, improve glucose regulation, enhance tissue repair, and reduce inflammation. Technologies such as transferosomes ensure sustained drug release, enhance drug efficacy, and minimize complications, resulting in superior healing outcomes compared to traditional methods. CONCLUSION:Transferosome-based organogel delivery systems incorporating insulin offer promising therapeutic approaches for diabetic wound management. By addressing specific healing challenges through targeted delivery, deeper tissue penetration, and sustained drug release, these systems improve patient adherence and quality of life, significantly enhancing healing outcomes compared to conventional treatments.
The rise of antimicrobial resistance (AMR) has emerged as a critical global health concern, undermining the effectiveness of conventional antibiotics and complicating the treatment of infectious diseases. As a result, there is an urgent need to explore alternative therapeutic strategies. Antimicrobial peptides (AMPs) offer a promising solution due to their ability to target microbial membranes and essential cellular functions, exhibiting potent activity even against resistant strains. However, translating AMPs into clinical use is challenging due to issues, such as enzymatic degradation, short half-life, systemic toxicity, and poor pharmacokinetic profiles. To address these barriers, innovative delivery technologies have been developed. Systems such as nanoparticles, hydrogels, polymeric carriers, and microneedle arrays are being explored to enhance AMP stability, bioavailability, and targeted action. Additionally, advancements in peptide modification, combination therapies, and stimuli-responsive platforms are further enhancing their therapeutic potential. This review outlines the latest advancements in AMP delivery strategies aimed at counteracting AMR. It highlights key developments, identifies ongoing challenges, and proposes directions for future research. Emphasizing a multidisciplinary approach, the study underscores the transformative role of AMP-based systems in the next generation of antimicrobial therapies.
Choriocarcinoma, a rare yet highly aggressive gestational trophoblastic neoplasia, is uniquely responsive to chemotherapy. The serum marker β-human chorionic gonadotropin (βhCG) has long been central to its diagnosis and monitoring, but not without limitations. Persistent false positives, poor specificity for residual disease or resistance, and slow detection of relapse are a few to mention. Advances in precision oncology have introduced novel biomarkers, such as ctDNA, circulating tumor cells (CTCs), exosomes, miRNAs, and exosomal miRNAs, that promise improved specificity, early relapse detection, and personalized monitoring. This review encapsulates the current landscape of emerging biomarkers in choriocarcinoma, categorizes them by methodological class and clinical utility, discusses integration challenges, and outlines future research directions toward multi-marker precision diagnostics.
Nuclear medicine has revolutionized diagnostic and therapeutic strategies in oncology by offering molecular-level insights into tissue function-often detecting pathological changes before they manifest structurally. At the heart of this advancement lies the growing field of radiotheranostics, which combines targeted molecular imaging with precision radiotherapy. One of the most promising molecular targets in this field is the Gastrin-Releasing Peptide Receptor (GRPR), which is overexpressed in several solid tumors, including prostate cancer, breast cancer, and Gastrointestinal Stromal Tumors (GISTs). Among the GRPR-targeting radiopharmaceuticals, NeoB (formerly NeoBOMB1)-a radiolabeled GRPR antagonist-has emerged as a potent agent, enabling both diagnostic imaging ([67/68Ga]Ga-NeoB) and targeted radionuclide therapy ([177Lu] Lu-NeoB). This narrative review examines the current state of NeoB-based radiopharmaceuticals in cancer, with a focus on their diagnostic and therapeutic applications, primarily in prostate cancer, breast cancer, and Gastrointestinal Stromal Tumors (GIST), including preclinical and clinical studies published up to January 2025. Additionally, limitations and future directions are addressed. In diagnostic imaging, [68Ga]Ga-NeoB PET/CT demonstrated high detection rates for primary tumors and distant metastases in GRPR-positive cancers, with moderate accuracy for detecting lymph node metastases. In therapeutic studies, [177Lu] Lu-NeoB showed strong tumor uptake and significant antitumor activity in preclinical models, with no observed toxicity. One ongoing multicenter clinical trial, initiated in 2019, is assessing the safety and efficacy of [177Lu] Lu-NeoB in patients with advanced or metastatic cancers, including those with moderate renal impairment. Despite encouraging findings, several limitations remain. GRPR is physiologically expressed in normal tissues such as the pancreas and kidneys, leading to non-specific uptake and potential off-target radiation. Optimizing molecular structure, radionuclide selection, and dosing strategies is essential to reduce toxicity. Moreover, long-term efficacy and safety data in humans are still lacking, and further largescale clinical trials are needed to validate NeoB's clinical utility.
INTRODUCTION:The legume pod borer, Helicoverpa armigera, is a major biotic constraint to chickpea production, causing substantial global yield losses. The downstream signaling pathways underlying host-insect interactions remain largely unexplored, yet understanding these processes is crucial for developing pest-resilient cultivars. METHODS:A systems biology approach was employed to investigate the leaf proteome of 2 cultivated chickpea genotypes (JG 12 and JG 36) and 1 moderately tolerant wild genotype (ILWC 46) under simulated herbivory. This study aimed to elucidate molecular mechanisms underlying plant defense against insect attack. RESULTS:Proteomic profiling revealed 190-200, 170-210, and 170-200 total protein spots in ILWC 46, JG12, and JG 36, respectively. 76 Differentially Expressed Proteins (DEPs) were visually identified, of which 62 were selected for Mass Spectrometric (MS) analysis. ILWC 46 exhibited 22 DEPs (4 downregulated, 18 upregulated), JG 12 showed 23 DEPs (5 downregulated, 18 upregulated), and JG 36 had 17 DEPs (10 downregulated, 7 upregulated). Five proteins were common to JG 12 and JG 36. DISCUSSION:Genotype-specific proteomic changes suggest variable defense responses: predominant upregulation in ILWC 46 indicates enhanced metabolic activity under stress, whereas JG 36's downregulation implies reduced adaptability. Functional categorization showed modulation of photosynthesis, primary metabolism, and stress-related proteins, highlighting energy reallocation and activation of defense pathways sustaining stress tolerance differences among genotypes. CONCLUSION:This study provides a comprehensive proteomic perspective on chickpea defense responses to herbivory, highlighting candidate proteins and pathways for enhancing insect resistance in both cultivated and wild germplasm.
The oceans, covering over 70% of the Earth's surface, represent a vast and underexplored source of proteins and bioactive peptides with unique structures and functionalities. This review comprehensively examines the production, properties, and food applications of these marine-derived compounds, with a specific focus on their structure-function relationships. We highlight that peptides derived from fish, algae, and shellfish by-products exhibit a wide range of bioactivities, including potent antioxidant, antimicrobial, antihypertensive, and anti-inflammatory effects. These healthpromoting properties are intrinsically linked to their amino acid sequences and structural features, such as molecular weight and specific configurations. While enzymatic hydrolysis is the primary method for their production, challenges in cost-effective large-scale purification persist. The review further details their successful application in functional foods to improve nutritional value, enhance shelf-life, and promote health. Finally, we conclude that to fully harness this potential, future efforts must prioritize sustainable sourcing, advanced extraction technologies, and robust clinical trials to bridge the gap between laboratory research and commercial application.
