Current protein & peptide science最新文献

{"title":"Emerging Therapeutic Protein Targets of Inflammation: A Comprehensive Review.","authors":"Suman Sinha, Ram Kumar, Km Shainda","doi":"10.2174/0113892037500525261002120730","DOIUrl":"https://doi.org/10.2174/0113892037500525261002120730","url":null,"abstract":"<p><p>Conventional anti-inflammatory therapies, including nonsteroidal anti-inflammatory drugs (NSAIDs) and corticosteroids, remain the mainstay of treatment for inflammatory disorders. However, their long-term use is often limited by adverse effects, insufficient target specificity, and an inability to achieve sustained resolution of chronic inflammation. Advances in the understanding of inflammatory signalling pathways have led to the identification of several promising protein targets for the treatment of chronic inflammatory and autoimmune diseases. This review provides a comprehensive overview of emerging therapeutic protein targets whose dysregulation contributes to inflammation and neuroinflammation, highlighting their molecular mechanisms, therapeutic potential, and current clinical relevance. Key targets discussed include inflammasomes, the JAK-STAT pathway, the IL-17/IL-23 axis, specialized pro-resolving mediators (SPMs), the gut microbiota, epigenetic regulators, microRNAs, microglial activation, astrocyte dysfunction, the sphingosine-1- phosphate (S1P) signalling pathway, gasdermins, transient receptor potential (TRP) channels, and the complement system. Current therapeutic strategies targeting these pathways include smallmolecule inhibitors, monoclonal antibodies, and other emerging biologics designed to achieve selective immunomodulation. Collectively, these advances offer new opportunities for precision medicine by enabling more targeted control of inflammation while preserving essential host immune functions. Furthermore, the integration of multi-target therapeutic approaches, innovative drug delivery systems, and personalized treatment strategies is reshaping the future of anti-inflammatory therapy. Continued efforts to restore immune homeostasis without compromising protective immune responses will be critical for the development of safer and more effective treatments for inflammatory diseases.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149223531","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Preparation, Identification, and Anticoagulant and Antithrombotic Activities of Peptide-Rich Fractions from Crassostrea hongkongensis Hydrolysates.","authors":"Qilin Zhu, Suhua Chen, Fei Yang","doi":"10.2174/0113892037504835260915141342","DOIUrl":"https://doi.org/10.2174/0113892037504835260915141342","url":null,"abstract":"<p><strong>Objective: </strong>Oysters are abundant in protein and represent a promising raw material for producing bioactive peptides. This work aimed to isolate antithrombotic peptide-rich fractions from Crassostrea hongkongensis meat and evaluate their anticoagulant and antithrombotic effects via in vitro clotting assays and mouse in vivo experiments.</p><p><strong>Methods: </strong>Enzymatic hydrolysis was performed to prepare EC. Sequential ultrafiltration and dialysis were adopted to obtain graded fractions FEC1-FEC5. In vitro clotting time assays were conducted to screen active fractions. FEC5 was further purified by Sephadex G-15 gel filtration to yield four subfractions (F1-F4) with different molecular weight distributions. Chemical composition, molecular spectral features, and molecular weight distribution of EC, FEC5, and F2 were characterized using UV scanning, FTIR spectroscopy, and UHPLC-QTOF-MS. A carrageenan-induced mouse tail thrombosis model was established to evaluate the in vivo antithrombotic potency of FEC5, indicated by IR and PCTE.</p><p><strong>Results: </strong>Among all subfractions, F2 possessed the highest peptide content (90.17%) and prolonged in vitro clotting time to 401.92 s, with anticoagulant activity approaching that of HSPCG (p > 0.05). The high-dose FEC5 group exhibited in vivo antithrombotic activity, with an IR of 41.98% and a PCTE of 43.63%. These indicators were numerically higher than those of the APDG without statistical significance (p > 0.05). UHPLC-QTOF-MS analysis confirmed eight shared peptide components between FEC5 and F2 with defined molecular weights. Characteristic marker ions of FEC5 remained detectable after gel filtration, yet residual system impurities existed in F2, indicating that single-round Sephadex G-15 purification cannot completely remove small-molecule contaminants. Chromatography also altered component distribution and molecular aggregation states. Typical peptide absorption signals and phenylalanine characteristic UV absorption were observed in EC, FEC5, and F2, and FTIR spectra displayed characteristic amide A and amide I bands.</p><p><strong>Discussion: </strong>The peptide-rich fractions from Crassostrea hongkongensis, especially FEC5, show obvious anticoagulant and antithrombotic effects in vitro and in vivo. FEC5 exhibited dosedependent activity, with its efficacy numerically close to aspirin, and high concentrations of FEC5 achieved anticoagulant activity comparable to heparin sodium in vitro. Further exploration is required to reveal its underlying action mechanisms.</p><p><strong>Conclusion: </strong>FEC5 exerted dose-dependent anticoagulant and antithrombotic effects in vitro and in vivo. Further purification effectively improved the activity of its subfraction F2. The peptide-rich fractions from Crassostrea hongkongensis have potential for developing marine antithrombotic functional food ingredients.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149164990","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative Evaluation of Surfactants and Stabilizers in Preventing Protein Aggregation in Insulin Formulations.","authors":"Asif Sayyad, Bandoo Chatale, Vinod Mokale","doi":"10.2174/0113892037484972260921041034","DOIUrl":"https://doi.org/10.2174/0113892037484972260921041034","url":null,"abstract":"<p><strong>Introduction: </strong>Protein aggregation is an issue that affects the stability and effectiveness of biopharmaceutical products. Proteins easily undergoes denaturation, due to mechanical agitation and prolonged storage times. Although polysorbates have been extensively used to stabilize proteins, there is still room to identify other highly effective additives. This research aimed to compare the efficacy of hydroxypropyl-β-cyclodextrin (HP-β-CD) in preventing protein aggregation in recombinant human insulin with polysorbate 20 (PS-20), polysorbate 80 (PS-80), and Poloxamer 188 (P188).</p><p><strong>Methods: </strong>Recombinant human insulin formulations with the addition of PS-20, PS-80, P188, or HP-β-CD, or the absence of any additive (control group), were prepared. The prepared samples were subjected to mechanical stress through shaking at 100 rpm for 24 hours. Thereafter, a sixmonth accelerated stability test was performed at 25±2°C/65±5% RH. Protein aggregation and particle formation were measured using size-exclusion high-performance liquid chromatography (SEHPLC) to detect HMWP, dynamic light scattering (DLS) for submicron aggregate size, and light obscuration (LO) of subvisible particles.</p><p><strong>Results: </strong>Mechanical agitation caused protein aggregation in all formulations; however, the degree of aggregation depended on the stabilizer used. HP-β-CD showed the highest stabilization activity, with only a 1.2% increase in HMWP level, whereas the non-stabilized control increased by 12.3%. LO analysis showed that formulations containing HP-β-CD had the least subvisible particles. In addition, DLS analysis showed no changes in aggregate size. Accelerated stability study results showed even better performance of HP-β-CD, with HMWP levels ranging from 2.60% to 2.64% over six months of storage, exceeding the performance of PS-20, PS-80, and P188.</p><p><strong>Discussion: </strong>The stabilization effect exerted by HP-β-CD could be assumed due to its capacity to decrease protein unfolding and prevent aggregation by the interfacial stress. Compared with the other surfactants, HP-β-CD provided better protection against mechanical and storage-related degradation of the protein while limiting particle formation.</p><p><strong>Conclusion: </strong>Under the conditions of agitation and storage stress, the use of HP-β-CD provides more efficient stabilization of recombinant human insulin as compared with polysorbate surfactants and Poloxamer 188.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149134678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Advances in Antimicrobial Peptides: Design, Mechanism, and Clinical Application-A Critical Review.","authors":"Shesham Kumari, Ranjeet Kumar, Manish Singh, Dharmendra Kumar","doi":"10.2174/0113892037467494260912090514","DOIUrl":"https://doi.org/10.2174/0113892037467494260912090514","url":null,"abstract":"<p><p>The global antimicrobial resistance (AMR) crisis, projected to cause 10 million deaths annually by 2050, necessitates innovative therapeutic strategies beyond traditional antibiotics. Antimicrobial peptides (AMPs), fundamental components of innate immunity, have emerged as compelling candidates owing to their broad-spectrum activity and mechanism of action, which challenges conventional resistance development. This review critically synthesizes the latest advances in the field, where the transition from natural discovery to rational engineering is of paramount importance. This review explores how computational design, artificial intelligence, and peptidomimetics can generate next-generation AMPs with enhanced stability and reduced toxicity. Furthermore, we dissected their multifaceted mechanisms, which extend beyond membrane disruption to include immunomodulation and intracellular targeting. However, the clinical pipeline reveals significant hurdles, with recent late-stage failures of candidates such as murepavadin and surotomycin, underscoring persistent challenges in systemic toxicity and pharmacokinetics. Looking ahead, we assess promising strategies to overcome these barriers, including AMP-antibiotic synergies and targeted delivery systems. This review aims to provide a realistic and forward-looking analysis of the design principles, mechanistic complexity, and translational potential of AMPs, framing their role in future antimicrobial strategies.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149105290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Xianling Gubao Capsule for Osteoporosis: A Review of Active Components and Underlying Mechanisms.","authors":"Ailing Fang, Ziling Tang, Hao Zeng, Ye He, Zhigang Zhou, Jing Wang, Zuocheng Qiu","doi":"10.2174/0113892037479962260908094129","DOIUrl":"https://doi.org/10.2174/0113892037479962260908094129","url":null,"abstract":"<p><p>Osteoporosis is a metabolic bone disorder that poses a serious threat to the health of middle- aged and elderly individuals. Xianling Gubao Capsule is a clinical medication used to treat osteoporosis, comprising six Chinese medicinal herbs: Epimedii Folium, Dipsaci Radix, Psoraleae Fructus, Rehmanniae Radix, Salviae Miltiorrhizae Radix Et Rhizoma, and Anemarrhenae Rhizoma. This article reviews the research progress on the active constituents and pharmacological mechanisms of treating osteoporosis in this capsule. Network pharmacology and mass spectrometry have identified flavonoids (e.g., Icariin), coumarins (e.g., Psoralen), and saponins(e.g., Timosaponin BII) as the major active constituents. Regarding the mechanism of treating osteoporosis, this capsule promotes osteoblast differentiation by activating pathways such as Wnt/β-catenin and p38 MAPK, regulates the OPG/RANKL/RANK pathway to inhibit osteoclast activity, and exerts effects by modulating estrogen metabolic homeostasis. Despite these advances, the complete repertoire of active constituents and the detailed multi‑component synergy remain incompletely understood. Future work must deepen the analysis of multi-component synergistic networks, explore emerging signaling pathways, such as the histamine pathway mediated by histidine decarboxylase, and resolve safety concerns to provide robust support for its precise clinical application.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149105411","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural and Functional Mechanisms of Human Serum Albumin in Drug Binding and Transport: Implications for Albumin-Based Nanocarrier Design - A Systematic Review.","authors":"Anurag Negi, Shikha Baghel Chauhan, Chirag Jain, Indu Singh","doi":"10.2174/0113892037473412260828073005","DOIUrl":"https://doi.org/10.2174/0113892037473412260828073005","url":null,"abstract":"<p><strong>Objective: </strong>Albumin is a widely used nanoparticle drug delivery system due to its biocompatibility, stability, and inherent targeting capabilities. The aim of this systematic review is to highlight the structural and functional role of albumin in drug binding, stability, and targeting, with particular emphasis on the therapeutic implications.</p><p><strong>Methods: </strong>A comprehensive search of electronic databases, including PubMed, Scopus, Web of Science, and Google Scholar, was conducted according to the PRISMA guidelines. Relevant literature was screened based on predetermined criteria for inclusion and exclusion. Data were extracted and synthesized qualitatively.</p><p><strong>Results: </strong>A total of 4,754 records were retrieved, and 76 studies were included in this review after the screening and assessment of their eligibility. The results showed that albumin plays a role in the stabilization of nanoparticles via steric and electrostatic interactions, improves the encapsulation efficiency of drugs, and increases the systemic circulation of nanoparticles. The targeting mechanisms of albumin, including the mechanisms of gp60-mediated transcytosis and SPARC-mediated tumor retention, have also been effective in the improvement of drug delivery and efficacy.</p><p><strong>Discussion: </strong>From the results, it is evident that albumin plays a critical role in the improvement of nanoparticle formulations compared to synthetic stabilizers.</p><p><strong>Conclusion: </strong>From the results of this review, it is evident that albumin nanoparticles have a great future in the improvement of drug targeting and delivery.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148966926","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, Synthesis, and Biological Evaluation of Lipidated Pentapeptide Derivatives Containing Unnatural Amino Acids.","authors":"Sunil Tivari, Pooja Bhanderi, Dharmesh Katariya, Vijay Khedkar, Ranjan Khunt","doi":"10.2174/0113892037480421260816205356","DOIUrl":"https://doi.org/10.2174/0113892037480421260816205356","url":null,"abstract":"<p><strong>Introduction/objective: </strong>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.</p><p><strong>Methods: </strong>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.</p><p><strong>Results: </strong>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).</p><p><strong>Discussion: </strong>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.</p><p><strong>Conclusion: </strong>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.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148905218","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mini Review of Modified Aquatic Antimicrobial Peptides with Anticancer Properties.","authors":"Arnold Ang, Li Ting Lee, Ahmed Abdulkareem Najm, Rui Rui Wong, Ibrahim Mahmood, Muhammad Yasin, Wamidh Talib, Shazrul Fazry, Douglas Law","doi":"10.2174/0113892037492863260811110405","DOIUrl":"https://doi.org/10.2174/0113892037492863260811110405","url":null,"abstract":"<p><strong>Background/aim: </strong>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.</p><p><strong>Materials and methods: </strong>A review of studies published from 2014 to 2024 was conducted using Google Scholar and ScienceDirect databases, with keywords and Boolean operators.</p><p><strong>Results: </strong>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.</p><p><strong>Discussion: </strong>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.</p><p><strong>Conclusion: </strong>These findings highlight the potential of peptide modifications in enhancing anticancer activity, underscoring the need for further research to optimize cancer treatment strategies.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148891182","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural Transitions of β-lactoglobulin Aggregates Observed Under Controlled Heat Treatment.","authors":"Miraclin Prasanna A, Priyankar Sen","doi":"10.2174/0113892037474248260716172451","DOIUrl":"https://doi.org/10.2174/0113892037474248260716172451","url":null,"abstract":"<p><strong>Introduction: </strong>β-Lactoglobulin (β-Lg), the major whey protein in bovine milk, readily undergoes structural transitions leading to amyloid fibril formation under acidic conditions and elevated temperatures. This study investigated the influence of different thermal treatment conditions on the aggregation and fibrillation behavior of β-Lg at pH 2.</p><p><strong>Methods: </strong>β-Lg solutions were subjected to three different thermal conditions: stepwise heating from 35o C to 90o C for 12h (Sample A), cyclic heating and cooling from 35o C to 90o C for 24h (Sample B), and constant heating at 90o C for 24h (Sample F). Untreated β-Lg served as the control (Sample M). Structural and morphological changes induced by these treatments were characterized by using intrinsic tryptophan fluorescence spectroscopy, Thioflavin T (ThT) fluorescence assay, circular dichroism (CD) spectroscopy, Fourier-transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FE-SEM) and atomic force microscopy (AFM).</p><p><strong>Results: </strong>Spectroscopic and microscopic analyses revealed that stepwise heating (Sample A) promoted amyloid fibril formation, whereas constant heating (Sample F) resulted in extensive aggregation and the development of highly ordered β-sheet-rich fibrillar structures. In contrast, cyclic heating and cooling (Sample B) produced reduced fibril formation, partial retention of native β-Lg structural changes, and distinct aggregate morphologies. Fluorescence, CD, FTIR, and microscopic analyses consistently indicate that Sample F represents the most advanced fibrillar state, while Sample B remained in a partially unfolded and hydrated state with limited changes in the structure.</p><p><strong>Discussion: </strong>The observed differences in aggregation and fibrillation behavior demonstrated that thermal treatment strongly influences the balance between structural rearrangement and irreversible protein aggregation. Controlled thermal cycling appears to modulate the aggregation pathway by stabilizing intermediate conformational states and limiting the formation of highly ordered amyloid assemblies.</p><p><strong>Conclusion: </strong>The method of heating plays a critical role in determining the structural change of βLg. While prolonged heating promotes extensive fibrillation and aggregation, controlled heatingcooling cycles reduce the extent of amyloid formation and preserve partially native-like structural characteristics. These findings provide valuable insights into the thermal regulation of β-Lg aggregation and may contribute to the development of processing strategies for controlling protein selfassembly in food and biomaterial applications.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148600092","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploring Neurological Disorder Therapeutics: The Progress and Future Prospects of Proteins and Peptides Derived from Blue Foods.","authors":"Mahima Chaudhary, Tushar Verma, Ravi Pratap Singh, Pramod Kumar Sharma, Dharmendra Kumar","doi":"10.2174/0113892037464157260629092418","DOIUrl":"https://doi.org/10.2174/0113892037464157260629092418","url":null,"abstract":"<p><strong>Introduction: </strong>Neurological illnesses continue to be a major global health challenge and require novel and safe therapeutic strategies. Blue foods like marine fish, algae, and invertebrates consist of many bioactive proteins/peptides that might provide multiple benefits for maintenance of a healthy brain, including neuroprotection, reduction of inflammation, and reduction of oxidative stress. This review looks at both recent advances made with blue food bio-molecules and their potential future roles in therapeutic targeting for neurological disorders.</p><p><strong>Methods: </strong>This study is designed as a narrative review, aiming to comprehensively summarize and critically analyze existing literature on marine-derived bioactive peptides and their neuroprotective potential. Literature searches were conducted from January 2009 to March 2025 using PubMed and other biomedical databases.</p><p><strong>Results: </strong>Available preclinical evidence suggests that marine-derived proteins and peptides may exert neuroprotective effects through multiple mechanisms, including activation of antioxidant defense pathways via Nrf2-mediated signaling, modulation of NF-κB-associated neuroinflammatory responses, regulation of serotonergic and dopaminergic neurotransmission, and attenuation of amyloid-β aggregation. Experimental studies conducted in animal models have reported improvements in cognitive performance, reductions in oxidative stress biomarkers, and decreased production of pro-inflammatory cytokines following administration of marine protein hydrolysates.</p><p><strong>Discussion and conclusion: </strong>Clinical translation of marine-derived bioactive peptides remains challenging due to the following factors: standardization of extraction, bioavailability, batch-to-batch variability, allergenic potency, and complex regulatory requirements. Ongoing new approaches using nano-formulation, synthetic biology, and Artificial Intelligence (AI) in the discovery of peptides hold the promise of enhancing their stability, targeting, and scalability. However, in order to validate the therapeutic utility of these approaches, it will require large, well-designed clinical studies.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2026-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148396214","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}