Microalga nannochloropsis gaditana as a sustainable source of bioactive peptides: a proteomic and in silico approach
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The impact of the world’s growing population on food systems and the role of dietary patterns in the managing of non-communicable diseases underscore the need to explore sustainable and dietary protein sources. Although microalgae have stood out as alternative sources of proteins and bioactive peptides, some species such as Nannochloropsis gaditana remain unexplored. This study aimed to characterize N. gaditana’s proteome and evaluate its potential as a source of bioactive by using an in silico approach. A total of 1955 proteins were identified and classified into functional groups of cellular component, molecular function, and biological process. In silico gastrointestinal digestion of identified proteins demonstrated that 202 hydrophobic and low molecular size-peptides with potential bioactivity were released. Of them, 27 exhibited theorical antioxidant, antihypertensive, antidiabetic, antiinflammatory, and/or antimicrobial activities. Seven of 27 peptide showed ≥20% intestinal absorption, suggesting potential systemic effects, while the rest could act at local level. Molecular docking demonstrated strong affinities with key enzymes such as MPO, ACE, and DPPIV. Resistance to the digestion, capacity to be absorbed and multifunctionality were demonstrated for peptide FIPGL. This study highlights N. gaditana's potential as a sustainable source of novel potential bioactive peptides with promising local and systemic biological effects.
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Paterson et al. (2025) performed an in silico assay to predict the absorption and distribution of bioactive peptides from Nannochloropsis gaditana.
“To predict the absorption and distribution of bioactive peptides from Nannochloropsis gaditana, Paterson et al. (2025) performed an in silico assay.”
From Microalgae biotechnology and its role in sustainable and healthy food design (2025) · cites this paper as Paterson et al., 2025
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Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · see citing works
Daina, A., Michielin, O., & Zoete, V. (2017) · Scientific Reports · doi:10.1038/srep42717 · Cited by 18,367 · see citing works
Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (1997) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(96)00423-1 · Cited by 11,484 · see citing works
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,930 · see citing works
Commercial Applications of Microalgae
Spolaore, P., Joannis-Cassan, C., Duran, E., & Isambert, A. (2006) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.101.87 · Cited by 4,285 · see citing works
Molecular Docking and Structure-Based Drug Design Strategies
Ferreira, L. L. G., dos Santos, R. N., Oliva, G., & Andricopulo, A. D. (2015) · Molecules · doi:10.3390/molecules200713384 · Cited by 2,645 · see citing works
Berman, H. M., Battistuz, T., Bhat, T. N., Bluhm, W. F., Bourne, P. E., Burkhardt, K., Feng, Z., Gilliland, G. L., Iype, L. E., Jain, S. C., et al. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902003451 · Cited by 2,578 · see citing works
Martin, Y. C. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0492002 · Cited by 1,042 · see citing works
BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities
Minkiewicz, P., Iwaniak, A., & Darewicz, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235978 · Cited by 958 · see citing works
Management and Prevention Strategies for Non-communicable Diseases (NCDs) and Their Risk Factors
Budrevičiūtė, A., Damiati, S., Sabir, D. K., Önder, K., Schuller‐Götzburg, P., Plakys, G., Katileviciute, A., Khoja, S. M., & Kodzius, R. (2020) · Frontiers in Public Health · doi:10.3389/fpubh.2020.574111 · Cited by 955 · see citing works
Crystal structure of the human angiotensin-converting enzyme–lisinopril complex
NATESH, R., Schwager, S. L. U., Sturrock, E. D., & Acharya, K. R. (2003) · Nature · doi:10.1038/nature01370 · Cited by 891 · see citing works
Cheung, H. S., Wang, F. L., Ondetti, M. A., Sabo, E. F., & Cushman, D. W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86187-2 · Cited by 746 · see citing works
Bioactive Peptides: Synthesis, Sources, Applications, and Proposed Mechanisms of Action
Akbarian, M., Khani, A., Eghbalpour, S., & Uversky, V. N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031445 · Cited by 639 · see citing works
Mooney, C., Haslam, N. J., Pollastri, G., & Shields, D. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045012 · Cited by 629 · see citing works
A review of high value-added molecules production by microalgae in light of the classification
Levasseur, W., Perré, P., & Pozzobon, V. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107545 · Cited by 551 · see citing works
Simple Method of Calculating Octanol/Water Partition Coefficient.
MORIGUCHI, I., Hirono, S., Qian, L. I. U., Nakagome, I., & MATSUSHITA, Y. (1992) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.40.127 · Cited by 536 · see citing works
Bennett, J. M., Reeves, G., Billman, G. E., & Sturmberg, J. P. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00316 · Cited by 531 · see citing works
De novo peptide sequencing by deep learning
Tran, N. H., Zhang, X., Xin, L., Shan, B., & Li, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705691114 · Cited by 437 · see citing works
Sheih, I., Wu, T., & Fang, T. J. (2009) · Bioresource Technology · doi:10.1016/j.biortech.2009.02.014 · Cited by 397 · see citing works
Deep learning enables de novo peptide sequencing from data-independent-acquisition mass spectrometry
Tran, N. H., Qiao, R., Xin, L., Chen, X., Liu, C., Zhang, X., Shan, B., Ghodsi, A., & Li, M. (2018) · Nature Methods · doi:10.1038/s41592-018-0260-3 · Cited by 375 · see citing works
Millward, D. J., Layman, D. K., Tomé, D., & Schaafsma, G. (2008) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/87.5.1576s · Cited by 359 · see citing works
CAMPR4: a database of natural and synthetic antimicrobial peptides
Gawde, U., Chakraborty, S., Waghu, F. H., Barai, R. S., Khanderkar, A., Indraguru, R., Shirsat, T., & Idicula‐Thomas, S. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac933 · Cited by 282 · see citing works
Comparison of Reliability of log P Values for Drugs Calculated by Several Methods.
MORIGUCHI, I., Hirono, S., Nakagome, I., & Hirano, H. (1994) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.42.976 · Cited by 280 · see citing works
Saito, Y., Wanezaki, K., Kawato, A., & Imayasu, S. (1994) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.58.1767 · Cited by 240 · see citing works
SPIDER: SOFTWARE FOR PROTEIN IDENTIFICATION FROM SEQUENCE TAGS WITH DE NOVO SEQUENCING ERROR
Han, Y., Ma, B., & Zhang, K. (2005) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720005001247 · Cited by 216 · see citing works
Vo, T.-S., Ryu, B., & Kim, S.-K. (2013) · Journal of Functional Foods · doi:10.1016/j.jff.2013.05.001 · Cited by 209 · cited 1× · see citing works
“Similarly, N. oculata has been reported to generate protein hydrolyzates and peptides with angiotensin-converting enzyme (ACE)-1-inhibitory, antithrombotic, and calcium/calmodulin-dependent kinase II (CAMKII)-inhibitory activities [17,18].”
An in silico platform for predicting, screening and designing of antihypertensive peptides
Kumar, R., Chaudhary, K., Chauhan, J. S., Nagpal, G., Kumar, R., Sharma, M., & Raghava, G. P. S. (2015) · Scientific Reports · doi:10.1038/srep12512 · Cited by 193 · see citing works
Khatun, M. S., Hasan, M. M., & Kurata, H. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00129 · Cited by 184 · see citing works
Wu, J., Aluko, R. E., & Nakai, S. (2006) · QSAR & Combinatorial Science · doi:10.1002/qsar.200630005 · Cited by 175 · see citing works
Functional properties of the biomass of three microalgal species
Guil-Guerrero, J. L., Navarro-Juárez, R., López-Martı́nez, J. C., Campra-Madrid, P., & Rebolloso-Fuentes, M. (2004) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2004.02.014 · Cited by 173 · see citing works
Angiotensin-Converting Enzyme Inhibitors
Peng, H., Carretero, O. A., Vuljaj, N., Liao, T., Motivala, A. A., Peterson, E. L., & Rhaleb, N. (2005) · Circulation · doi:10.1161/circulationaha.104.528695 · Cited by 161 · see citing works
Exploring the Potential of Bioactive Peptides: From Natural Sources to Therapeutics
Purohit, K., Reddy, N., & Sunna, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031391 · Cited by 160 · see citing works
Complete De Novo Assembly of Monoclonal Antibody Sequences
Tran, N. H., Rahman, M. Z., He, L., Xin, L., Shan, B., & Li, M. (2016) · Scientific Reports · doi:10.1038/srep31730 · Cited by 158 · see citing works
Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor
Lan, V. T. T., Ito, K., Ohno, M., Motoyama, T., Ito, S., & Kawarasaki, Y. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.11.131 · Cited by 150 · see citing works
Application Progress of Bioactive Compounds in Microalgae on Pharmaceutical and Cosmetics
Zhuang, D., He, N., Khoo, K. S., Ng, E.-P., Chew, K. W., & Ling, T. C. (2022) · Chemosphere · doi:10.1016/j.chemosphere.2021.132932 · Cited by 142 · see citing works
Microalgae proteins as sustainable ingredients in novel foods: recent developments and challenges
Mosibo, O. K., Ferrentino, G., & Udenigwe, C. C. (2024) · Foods · doi:10.3390/foods13050733 · Cited by 140 · see citing works
Separation, antitumor activities, and encapsulation of polypeptide from Chlorella pyrenoidosa
Wang, X., & Zhang, X. (2013) · Biotechnology Progress · doi:10.1002/btpr.1725 · Cited by 133 · see citing works
He, W., Su, G., Sun‐Waterhouse, D., Waterhouse, G. I. N., Zhao, M., & Yang, L. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.08.057 · Cited by 131 · see citing works
Luna‐Vital, D. A., Weiss, M., & de Mejı́a, E. G. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700362 · Cited by 114 · see citing works
The Biochemistry and Effectiveness of Antioxidants in Food, Fruits, and Marine Algae
Pruteanu, L.-L., Bailey, D. S., Grădinaru, A. C., & Jäntschi, L. (2023) · Antioxidants · doi:10.3390/antiox12040860 · Cited by 114 · see citing works
Microalgal Proteins and Bioactives for Food, Feed, and Other Applications
Lucáková, S., Brányiková, I., & Hayes, M. (2022) · Applied Sciences · doi:10.3390/app12094402 · Cited by 110 · see citing works
Myeloperoxidase: Growing importance in cancer pathogenesis and potential drug target
Valadez-Cosmes, P., Raftopoulou, S., Mihalič, Z. N., Marsche, G., & Kargl, J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108052 · Cited by 104 · see citing works
Paterson, S., Gómez‐Cortés, P., de la Fuente, M. Á., & Hernández‐Ledesma, B. (2023) · Nutrients · doi:10.3390/nu15020477 · Cited by 103 · see citing works
Self-citationMajumder, K., Chakrabarti, S., Morton, J. S., Panahi, S., Kaufman, S., Davidge, S. T., & Wu, J. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2014.12.028 · Cited by 102 · see citing works
Charoenkwan, P., Nantasenamat, C., Hasan, M. M., Moni, M. A., Lió, P., Manavalan, B., & Shoombuatong, W. (2021) · Methods · doi:10.1016/j.ymeth.2021.12.001 · Cited by 102 · see citing works
Essential and toxic elements in commercial microalgal food supplements
Rzymski, P., Budzulak, J., Niedzielski, P., Klimaszyk, P., Proch, J., Kozak, L., & Poniedziałek, B. (2018) · Journal of Applied Phycology · doi:10.1007/s10811-018-1681-1 · Cited by 97 · see citing works
Alonso, R., Pisa, D., Marina, A., Morato, E., Rábano, A., Rodal, I., & Carrasco, L. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.11084 · Cited by 95 · see citing works
Pereira, H., Silva, J., Santos, T., Gangadhar, K. N., Raposo, A., Nunes, C., Coimbra, M. A., Gouveia, L., Barreira, L. A., & Varela, J. C. S. (2019) · Molecules · doi:10.3390/molecules24173192 · Cited by 94 · see citing works
Wang, Z., & Zhang, X. (2016) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.7815 · Cited by 92 · see citing works
Ji, D., Xu, M., Udenigwe, C. C., & Agyei, D. (2020) · Current Research in Food Science · doi:10.1016/j.crfs.2020.03.001 · Cited by 89 · see citing works
Qin, D., Jiao, L., Wang, R., Zhao, Y. C., Hao, Y., & Liang, G. (2023) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2023.106591 · Cited by 87 · see citing works
García‐Vaquero, M., Mora, L., & Hayes, M. (2019) · Marine Drugs · doi:10.3390/md17040204 · Cited by 82 · see citing works
The Structure, Functions and Potential Medicinal Effects of Chlorophylls Derived from Microalgae
Sun, D., Wu, S., Li, X., Ge, B., Zhou, C., Yan, X., Ruan, R. R., & Cheng, P. (2024) · Marine Drugs · doi:10.3390/md22020065 · Cited by 81 · see citing works
Chronakis, I. S., & Madsen, M. (2011) · Elsevier eBooks · doi:10.1533/9780857093639.353 · Cited by 79 · see citing works
Salelles, L., Floury, J., & Feunteun, S. L. (2021) · Food & Function · doi:10.1039/d1fo02453a · Cited by 77 · see citing works
Conventional and in silico approaches to select promising food-derived bioactive peptides: A review
Peredo-Lovillo, A. G., Hernández‐Mendoza, A., Vallejo‐Córdoba, B., & Romero‐Luna, H. E. (2021) · Food Chemistry X · doi:10.1016/j.fochx.2021.100183 · Cited by 76 · see citing works
Li, Y., Li, B., He, J., & Qian, P. (2011) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2011.05.011 · Cited by 75 · see citing works
Floret, C., Monnet, A., Micard, V., Walrand, S., & Michon, C. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1956426 · Cited by 75 · see citing works
Cai, Y., Zhai, L., Fang, X., Wu, K., Liu, Y., Cui, X., Wang, Y., Yu, Z., Ruan, R. R., Liu, T., et al. (2022) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-022-02204-z · Cited by 72 · see citing works
Cavonius, L. R., Albers, E., & Undeland, I. (2016) · Food & Function · doi:10.1039/c5fo01144b · Cited by 59 · see citing works
Li, Y., Aiello, G., Fassi, E. M. A., Boschin, G., Bartolomei, M., Bollati, C., Roda, G., Arnoldi, A., Grazioso, G., & Lammi, C. (2021) · Nutrients · doi:10.3390/nu13051624 · Cited by 59 · see citing works
Senadheera, T. R. L., Hossain, A., Dave, D., & Shahidi, F. (2022) · Marine Drugs · doi:10.3390/md20100610 · Cited by 58 · see citing works
Ferreira, M., Teixeira, C., Abreu, H., Silva, J., Costas, B., Kiron, V., & Valente, L. M. P. (2021) · Journal of Applied Phycology · doi:10.1007/s10811-021-02549-2 · Cited by 56 · see citing works
Bioactive Peptides: An Understanding from Current Screening Methodology
Nong, N. T. P., & Hsu, J. (2022) · Processes · doi:10.3390/pr10061114 · Cited by 54 · see citing works
Vizcaíno, A. J., Sáez, M. I., Martínez, T. F., Acién, F. G., & Alarcón, F. J. (2018) · Algal Research · doi:10.1016/j.algal.2018.11.018 · Cited by 52 · see citing works
Rapid Peptides Generator: fast and efficient in silico protein digestion
Maillet, N. (2019) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqz004 · Cited by 51 · see citing works
Protein quality, nutrition and health
Calvez, J., Azzout‐Marniche, D., & Tomé, D. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1406618 · Cited by 51 · see citing works
Pei, Y., Cai, S., Ryu, B., Zhou, C., Hong, P., & Qian, Z. (2022) · Journal of Functional Foods · doi:10.1016/j.jff.2022.105061 · Cited by 45 · see citing works
Medina, C., Rubilar, M., Shene, C., Torres, S., & Verdugo, M. (2015) · Journal of Biobased Materials and Bioenergy · doi:10.1166/jbmb.2015.1534 · Cited by 42 · see citing works
Evaluation of the Multifunctionality of Soybean Proteins and Peptides in Immune Cell Models
Paterson, S., Fernández‐Tomé, S., Galvez, A. F., & Hernández‐Ledesma, B. (2023) · Nutrients · doi:10.3390/nu15051220 · Cited by 42 · see citing works
Self-citationDu, C., Gong, H., Zhao, H., & Wang, P. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.139587 · Cited by 41 · see citing works
Proteomic and Transcriptomic Patterns during Lipid Remodeling in Nannochloropsis gaditana
Hulatt, C. J., Smolina, I., Dowle, A., Kopp, M., Vasanth, G. K., Hoarau, G. G., Wijffels, R. H., & Kiron, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186946 · Cited by 38 · see citing works
Fernández‐Acero, F. J., Amil‐Ruíz, F., Durán‐Peña, M. J., Carrasco-Reinado, R., Fajardo, C., Guarnizo, P., Fuentes-Almagro, C. A., & Vallejo, R. A. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.10.015 · Cited by 33 · see citing works
Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase‐III homologue
Dhanda, S., Singh, J., & Singh, H. (2007) · Cell Biochemistry and Function · doi:10.1002/cbf.1448 · Cited by 32 · see citing works
Hayes, M., Mora, L., & Lucáková, S. (2022) · Biomolecules · doi:10.3390/biom12121806 · Cited by 32 · see citing works
Antioxidant activity of peptide-based angiotensin converting enzyme inhibitors
Bhuyan, B. J., & Mugesh, G. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob06533a · Cited by 30 · see citing works
Structural Basis of Bioactivity of Food Peptides in Promoting Metabolic Health
Yao, S., Agyei, D., & Udenigwe, C. C. (2018) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2017.12.002 · Cited by 30 · see citing works
Zinc Finger Protein LipR Represses Docosahexaenoic Acid and Lipid Biosynthesis in Schizochytrium sp.
Xiao, H., Liu, Y., & Chen, Z. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.02063-21 · Cited by 29 · see citing works
Xie, W., Li, X., Xu, H., Chen, F., Cheng, K., Liu, H., & Liu, B. (2023) · Marine Drugs · doi:10.3390/md21100519 · Cited by 29 · see citing works
Sanchiz, Á., Morato, E., Rastrojo, A., Camacho, E., la Fuente, S. G., Marina, A., Aguado, B., & Requena, J. M. (2020) · Genes · doi:10.3390/genes11091036 · Cited by 27 · see citing works
Wang, Z., Fan, H.-B., Bao, X., & Wu, J. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c04211 · Cited by 26 · see citing works
Villaseñor, V. M., Enríquez-Vara, J. N., Urías-Silva, J. E., Lugo-Cervantes, E. D. C., Luna‐Vital, D. A., & Mojica, L. (2022) · Food Research International · doi:10.1016/j.foodres.2022.112048 · Cited by 24 · see citing works
Fernando, R. C., Sun, X., & Rupasinghe, H. P. V. (2024) · Macromol—A Journal of Macromolecular Research · doi:10.3390/macromol4030035 · Cited by 22 · see citing works
Hayes, M., Bastiaens, L., Gouveia, L., Gkelis, S., Skomedal, H., Skjånes, K., Murray, P., García‐Vaquero, M., HOŞOĞLU, M. İ., Dodd, J., et al. (2018) · doi:10.1002/9781119385332.ch12 · Cited by 21 · see citing works
Ashtiani, F.-R., Jalili, H., Rahaie, M., Sedighi, M., & Amrane, A. (2020) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2020.11.006 · Cited by 21 · see citing works
Naqash, S. Y., & Nazeer, R. A. (2011) · Amino Acids · doi:10.1007/s00726-011-1084-y · Cited by 16 · see citing works
In SilicoProteome Cleavage Reveals Iterative Digestion Strategy for High Sequence Coverage
Meyer, J. G. (2014) · ISRN Computational Biology · doi:10.1155/2014/960902 · Cited by 12 · see citing works
Кручинин, А. Г., Bolshakova, E. I., & Barkovskaya, I. A. (2023) · Fermentation · doi:10.3390/fermentation9040380 · Cited by 12 · see citing works
Using In Silico Approach for Metabolomic and Toxicity Prediction of Alternariol
Marin, D. E., & Țăranu, I. (2023) · Toxins · doi:10.3390/toxins15070421 · Cited by 12 · see citing works
Spotlight on Plant Bromodomain Proteins
Bardani, E., Kallemi, P., Tselika, M., Κατσαρού, Κ., & Kalantidis, K. (2023) · Biology · doi:10.3390/biology12081076 · Cited by 12 · see citing works
Pedroni, L., Perugino, F., Galaverna, G., Dall’Asta, C., & Dellafiora, L. (2022) · Nutrients · doi:10.3390/nu14214680 · Cited by 11 · see citing works
Rashid, M. H. U., Yi, E. K. J., Amin, N. D. M., & Ismail, M. N. (2023) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04783-5 · Cited by 11 · see citing works
Vakhrusheva, T. V., Av, S., Moroz, G. D., Kostevich, V. A., Gorbunov, N., Smirnov, I. P., Grafskaia, E. N., Latsis, I. A., Panasenko, O. M., & Lazarev, V. N. (2022) · Antioxidants · doi:10.3390/antiox11122419 · Cited by 10 · see citing works
NgAP2a Targets KCS Gene to Promote Lipid Accumulation in Nannochloropsis gaditana
Lin, Y., Li, Y., Wu, X., Xu, W., Zhang, Z., Zhu, H., & Zhou, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910305 · Cited by 6 · see citing works
Proteomic Analysis of the Major Alkali-Soluble Inca Peanut (Plukenetia volubilis) Proteins
Torres-Sánchez, E., Morato, E., Hernández‐Ledesma, B., & Gutiérrez, L. (2024) · Foods · doi:10.3390/foods13203275 · Cited by 6 · see citing works
Self-citationBioactive peptides released from microalgae during gastrointestinal digestion
Zaky, A. A., Paterson, S., Gómez‐Cortés, P., & Hernández‐Ledesma, B. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19141-1.00012-1 · Cited by 5 · see citing works
Self-citationWang, R., Li, J., Zhang, F., & Miao, X. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c05511 · Cited by 3 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [25]Official Methods of Analysis, 22nd Edition (2023)—Aoac International Available online: https://www.aoac.org/official-methods-of-analysis/ (accessed on 23 February 2024)
- [68]Heda R. Toro F. Tombazzi C.R. Physiology, Pepsin StatPearls Treasure Island, FL, USA 2023 30725690
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Prates, J. A. M. (2025) · Foods · doi:10.3390/foods14091524 · Cited by 45 · see citing works
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Schneider, A. T., Machado, R. L. S., Dutra, D. A., Machado, E. F., Dias, R. R., Deprá, M. C., Zepka, L. Q., & Jacob-Lopes, E. (2025) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2025.1716473 · Cited by 15 · see citing works
Rodríguez-Cabello, F., Rodríguez, L., Guzmán, F., Carrasco, B., Sanzana, S., Trostchansky, A., Palomo, I. F., & Eduardo Fuentes, Q. (2026) · Chemosensors · doi:10.3390/chemosensors14020030 · Cited by 11 · see citing works
Heredia-Martínez, L. G., Gutiérrez-Diánez, A. M., & Díaz‐Santos, E. (2025) · Phycology · doi:10.3390/phycology5020019 · Cited by 7 · see citing works
Fang, Y., Alahyaribeik, S., Hazaveh, M. N., Keung, P. C. C., Nie, L., Grootaert, C., Camp, J. V., & Mirzaei, M. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2599498 · Cited by 7 · see citing works
Tripathy, S., Rout, S., Das, R. S., Tiwari, B. K., García‐Vaquero, M., & Srivastav, P. P. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.108285 · Cited by 7 · see citing works
The pivotal role of omics technologies in the production of third and fourth generation biodiesel
Ijoma, G. N., Mannie, T., Lokwe, G. N., Ogola, H. J. O., Kalu, C. M., & Tekere, M. (2025) · Biofuels · doi:10.1080/17597269.2025.2564504 · Cited by 5 · see citing works
Recent insight about Biotechnological Applications of Functional Seafoods in Pharmaceutical Industry
Taş, S., Döndaş, N. Y., Bulut, S. D., Arslan, B. N., Tamer, M. A., Abed, N. E., Rathod, N. B., Kudre, T. G., Zhang, Z., Döndaş, H. A., et al. (2025) · Food Reviews International · doi:10.1080/87559129.2025.2526681 · Cited by 4 · see citing works
Pino, D., Castro-Varela, P., Morales, E., & Rubilar, M. (2025) · Algal Research · doi:10.1016/j.algal.2025.104414 · Cited by 4 · see citing works
Algal metabolites as emerging anti-virulence therapeutics against Pseudomonas aeruginosa
Chakraborty, A., Bhattacharya, D., Pandit, S., Gill, H. S., Rajeev, M., Lahiri, D., & Nag, M. (2025) · Archives of Microbiology · doi:10.1007/s00203-025-04614-7 · Cited by 3 · see citing works
Majchrzak, M., Paterson, S., Gómez‐Cortés, P., Silván, J. M., Martínez-Rodríguez, A. J., & Hernández‐Ledesma, B. (2025) · Molecules · doi:10.3390/molecules30244669 · Cited by 1 · see citing works
Self-citationSaini, J. K., Narwal, S., Singh, J., Dhingra, A. K., Dushyant, Singh, G., & Grewal, N. (2026) · Protein and Peptide Letters · doi:10.2174/0109298665438727260217054757 · Cited by 1 · see citing works
Characterization of a novel thermostable α-amylase from Calothrix sp. using in silico approaches
de Sousa, A. C. L. F., dos Santos, L. Q., Xavier, G. A., Aguiar, D. C. F., Siqueira, A. S., & Gonçalves, E. C. (2025) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2025.109124
Romdhani, M., Dhaouafi, J., Deracinois, B., Flahaut, C., Nedjar, N., & Balti, R. (2025) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2025.103694
Liu, K., He, Y., Li, S., Tao, H., Liang, W., Huang, J., Jiang, C., Farag, M. A., Song, L., & Gao, F. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148392
Hofmann, A., Atamaniuk, I., & Kuchta, K. (2025) · Royal Society of Chemistry eBooks · doi:10.1039/9781837678198-00186
Algae and microbial proteins for alternative proteins: Untapped molecular resources
Spínola, M. P., Martins, C. F., & Prates, J. A. M. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.08.003
Paterson, S., Majchrzak, M., Andrés-Gaspar, M., Hernández‐Ledesma, B., Gómez‐Cortés, P., Arranz, E., & Fernández‐Tomé, S. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7411193
Self-citationFan, Z., Sun, T., Teng, D. H. A., Du, H., Yang, K., Wang, C., Ma, J., & Wang, P. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27188255
Zhuang, Y., Li, G., Cao, W., Lin, H., Chen, Z., Gao, J., Zhu, G., & Zheng, H. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.110164
Possibility of recovering bioactives from side streams of omega-3 oil extraction from microalgae
Sabbanwar, P., Han, Y., & Halim, R. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45519-3.00014-5
- Authors
- Paterson, S., Alonso-Pintre, L., Morato-López, E., González de la Fuente, S., Gómez-Cortés, P., & Hernández-Ledesma, B.
- Affiliations
- Instituto de Investigación en Ciencias de la Alimentación (ES)
- Proteomics Core Facility, Centro de Biología Molecular Severo Ochoa (CBM), CSIC-Universidad Autónoma de Madrid, Nicolás Cabrera 1, 28049 Madrid, Spain
- Biocomputational Core Facility, Centro de Biología Molecular Severo Ochoa (CBM), CSIC-Universidad Autónoma de Madrid, Nicolás Cabrera 1, 28049 Madrid, Spain
- Department of Bioactivity and Food Analysis, Institute of Food Science Research (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera 9, 28049 Madrid, Spain
- ORCID
- Venue
- Foods
- Publisher
- MDPI AG
- Published
- 2025-01-14
- Volume
- 14
- Issue
- 2
- Pages
- 252
- ISSN
- 2304-8158 (ISSN-L)
- PMC
- PMC11765504
- OpenAlex
- W4406357381
- Cited by
- 20
- References
- 96
- Citations by year
- 2026: 7 · 2025: 13
- FWCI
- 6.01
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Foods (publishedVersion, cc-by)
- Preprints.org (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- MICIU/AEI/10.13039/501100011033
- FEDER, EU
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Aquatic Science › Seaweed-derived Bioactive Compounds
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Keywords
- Nannochloropsis gaditana, microalgae, bioactive peptides, proteome, gastrointestinal digestion, antioxidant peptides, antihypertensive peptides, antidiabetic peptides, anti-inflammatory peptides, antimicrobial peptides, intestinal absorption, myeloperoxidase, ACE, dipeptidyl peptidase IV, alternative protein sources, non-communicable diseases
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