Green seaweed Ulva lactuca, a potential source of bioactive peptides revealed by in silico analysis
Open accessAbstract
The green seaweed Ulva lactuca is found in coastal areas. Potential bioactive peptides have a wide range of uses, including antibacterial, antifungal, antiviral, alpha-amylase inhibitory, antiamnestic, ACE inhibitory, immunomodulatory, anticancer, antioxidative, contracting, anti-inflammatory, and more. This study's major goal was to use in-silico methods to reveal the availability and abundance of putative bioactive peptides in the RuBisCO protein of Ulva lactuca seaweed. The protein sequence was obtained using the UniProtKB database. The peptide sequences were produced by using the BIOPEP-UWM enzyme activity tool. The peptides were ranked using PeptideRanker, and the toxicity profile was assessed using ToxinPred. For the first time, the current in-silico investigation depicts the pharmacological characteristics of Ulva lactuca by focusing on the RuBisCO protein. Numerous bioactive peptides with inhibitory activity against the angiotensin-I converting enzyme (ACE), dipeptidyl peptidase IV, antioxidant, dipeptidyl peptidase III, renin, antithrombotic, antiamnestic, α-glucosidase, anti-inflammatory, hypolipidemic activity, and ion flow regulation were produced by the in-silico proteolysis of rubisco using 18 proteases. Based on the cutoff score >0.75, pancreatic elastase liberated the most bioactive peptide sequences from the rubisco compared to other proteases. Additionally, PeptideRanker's findings showed that a number of di-, tri-, and/or polypeptides produced from the RuBisCO have a great deal of potential to be used as bioactive peptides. These studies open up new opportunities for these bioactive peptides in the fields of pharmacy, medicine, the food sector, and marine biotechnology.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Several algal peptides exert anti-obesity effects through activation of AMPK, including peptides derived from Limnospira platensis, Auxenochlorella pyrenoidosa, and Ulva lactuca.
“Several algal peptides have been identified to exert anti-obesity effects through the activation of AMP-activated protein kinase (AMPK). Notably, peptides derived from Limnospira platensis, Auxenochlorella pyrenoidosa, and the macroalgae Ulva lactuca have demonstrated such activity [115,119].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [119]
Section 3.2 and the discussion following Table 4 (page unavailable) report an in-silico prediction of a hypolipidemic peptide from Ulva lactuca that activates AMPK. They do not demonstrate an anti-obesity effect; this paper also does not provide evidence for the other two algae named in the citing sentence. (LLM, conf=0.89)
Experimental — accuracy not yet measuredIn silico-directed approaches have gained increasing popularity in recent studies of algal proteins (e.g. Limnospira platensis, Chlorella vulgaris, and Ulva lactuca) to guide discovery faster and maximize specificity of peptide selection.
“Such in silico-directed approaches have gained increasing popularity in recent studies of algal proteins (e.g. Limnospira platensis, Chlorella vulgaris, and Ulva lactuca) to guide the discovery process faster and maximize the specificity of peptide selection [119,214,215].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [119]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
In Silico Approach for Predicting Toxicity of Peptides and Proteins
Gupta, S., Kapoor, P., Chaudhary, K., Gautam, A., Kumar, R., & Raghava, G. P. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073957 · Cited by 2,026 · see citing works
Cyclic Nucleotide Phosphodiesterases: Molecular Regulation to Clinical Use
Bender, A. T., & Beavo, J. A. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.3.5 · Cited by 1,787 · see citing works
Oxidative stress and the use of antioxidants in diabetes: Linking basic science to clinical practice
Johansen, J. S., Harris, A. K., Rychly, D. J., & Ergul, A. (2005) · Cardiovascular Diabetology · doi:10.1186/1475-2840-4-5 · Cited by 1,003 · 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
The most abundant protein in the world
Ellis, R. J. (1979) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(79)90212-3 · Cited by 675 · see citing works
Smith, H. S. (2009) · Mayo Clinic Proceedings · doi:10.1016/s0025-6196(11)60750-7 · Cited by 666 · 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
Linnaeus was right all along:UlvaandEnteromorphaare not distinct genera
Hayden, H. S., Blomster, J., Maggs, C. A., Silva, P. C., Stanhope, M. J., & Waaland, J. R. (2003) · European Journal of Phycology · doi:10.1080/1364253031000136321 · Cited by 588 · see citing works
Dipeptidyl peptidase‐4 inhibitors in the treatment of type 2 diabetes: a comparative review
Deacon, C. F. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01306.x · Cited by 528 · see citing works
Nielsen, S. D.-H., Beverly, R. L., Qu, Y., & Dallas, D. C. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.04.056 · Cited by 496 · see citing works
The world's largest macroalgal bloom in the Yellow Sea, China: Formation and implications
Liu, D., Keesing, J. K., He, P., Wang, Z., Shi, Y., & Wang, Y. (2013) · Estuarine Coastal and Shelf Science · doi:10.1016/j.ecss.2013.05.021 · Cited by 455 · see citing works
Bioenergy potential of Ulva lactuca: Biomass yield, methane production and combustion
Bruhn, A., Dahl, J., Nielsen, H. B., Nikolaisen, L., Rasmussen, M. B., Markager, S., Olesen, B., Arias, C. A., & Jensen, P. D. (2010) · Bioresource Technology · doi:10.1016/j.biortech.2010.10.010 · Cited by 443 · see citing works
Functional ingredients from algae for foods and nutraceuticals
Domínguez, H. (2013) · doi:10.1533/9780857098689 · Cited by 387 · see citing works
Admassu, H., Gasmalla, M. A. A., Yang, R., & Zhao, W. (2018) · Journal of Food Science · doi:10.1111/1750-3841.14011 · Cited by 293 · see citing works
Angiotensin-converting enzyme 2 (ACE2) mediates influenza H7N9 virus-induced acute lung injury
Yang, P., Gu, H., Zhao, Z., Wang, W., Cao, B., Lai, C., Yang, X., Zhang, L., Duan, Y., Zhang, S., et al. (2014) · Scientific Reports · doi:10.1038/srep07027 · Cited by 283 · see citing works
The green seaweed Ulva: a model system to study morphogenesis
Wichard, T., Charrier, B., Mineur, F., Bothwell, J. H. F., Clerck, O. D., & Coates, J. C. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00072 · Cited by 256 · see citing works
Kayser, H., & Meisel, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00207-4 · Cited by 203 · see citing works
Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway
Turner, G. C., Du, F., & Varshavsky, A. J. (2000) · Nature · doi:10.1038/35014629 · Cited by 202 · see citing works
O'Brien, E. T., Barton, J., Nussberger, J., Mulcahy, D., Jensen, C., Dicker, P., & Stanton, A. V. (2006) · Hypertension · doi:10.1161/01.hyp.0000253780.36691.4f · Cited by 198 · see citing works
Palmieri, V. O., Grattagliano, I., Portincasa, P., & Palasciano, G. (2006) · The Journal of Nutrition · doi:10.1093/jn/136.12.3022 · Cited by 197 · see citing works
R ubisco: still the most abundant protein of Earth?
Raven, J. A. (2013) · New Phytologist · doi:10.1111/nph.12197 · Cited by 181 · see citing works
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect.
Yoshimoto, T., Kunio, K. A. D. O., Matsubara, F., KORIYAMA, N., Kaneto, H., & Tsuru, D. (1987) · Journal of Pharmacobio-Dynamics · doi:10.1248/bpb1978.10.730 · Cited by 173 · see citing works
A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate
Zhao, Y., Li, B., Dong, S., Liu, Z., Zhao, X. Q., Wang, J., & Zeng, M. (2009) · Peptides · doi:10.1016/j.peptides.2009.03.002 · Cited by 170 · see citing works
Rennex, D., Hemmings, B. A., Hofsteenge, J., & Stone, S. R. (1991) · Biochemistry · doi:10.1021/bi00222a025 · Cited by 153 · see citing works
Potential harmful effects of discontinuing ACE-inhibitors and ARBs in COVID-19 patients
Rossi, G. P., Sanga, V., & Barton, M. (2020) · eLife · doi:10.7554/elife.57278 · Cited by 147 · see citing works
Sun, S., Xu, X., Sun, X., Zhang, X., Chen, X., & Xu, N. (2019) · Marine Drugs · doi:10.3390/md17030179 · Cited by 140 · see citing works
Cermeño, M., Kleekayai, T., Amigo‐Benavent, M., Harnedy‐Rothwell, P. A., & Fitzgerald, R. J. (2020) · Electrophoresis · doi:10.1002/elps.202000153 · Cited by 139 · see citing works
Chakrabarti, S., & Wu, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117492 · Cited by 122 · see citing works
Kirkendale, L. A., Saunders, G. W., & Winberg, P. C. (2012) · Journal of Phycology · doi:10.1111/jpy.12016 · Cited by 114 · see citing works
Green tide formed by free-floating Ulva spp. at Yatsu tidal flat, Japan
Yabe, T., Ishii, Y., Amano, Y., Koga, T., Hayashi, S., Nohara, S., & Tatsumoto, H. (2009) · Limnology · doi:10.1007/s10201-009-0278-4 · Cited by 113 · see citing works
How Brittany and Florida coasts cope with green tides
Charlier, R. H., Morand, P., & Finkl, C. W. (2008) · International Journal of Environmental Studies · doi:10.1080/00207230701791448 · Cited by 104 · see citing works
Udenigwe, C. C., Gong, M., & Wu, S. (2013) · Process Biochemistry · doi:10.1016/j.procbio.2013.08.013 · Cited by 101 · see citing works
Evaluation of Marine Alga Ulva lactuca L. as A Source of Natural Preservative Ingredient
El‐Baky, H. H. A., & El-Baz, F. K. (2008) · Cited by 100 · 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
Species of Ulva (Ulvophyceae, Chlorophyta) as indicators of salinity
Rybak, A. S. (2017) · Ecological Indicators · doi:10.1016/j.ecolind.2017.10.061 · Cited by 83 · see citing works
García‐Vaquero, M., Mora, L., & Hayes, M. (2019) · Marine Drugs · doi:10.3390/md17040204 · Cited by 82 · see citing works
Agrawal, H., Joshi, R., & Gupta, M. (2017) · LWT · doi:10.1016/j.lwt.2017.06.036 · Cited by 81 · see citing works
Post-Proline Cleaving Enzyme (Prolyl Endoeptidase) from Bovine Brain1
Yoshimoto, T., NISHIMURA, T., Kita, T., & Tsuru, D. (1983) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a134463 · Cited by 80 · see citing works
Lee, D., Lee, E.-S., Alam, M. M., Jang, J.-H., Lee, H.-S., Oh, H., Kim, Y., Manzoor, Z., Koh, Y., Kang, D.-G., et al. (2015) · Metabolism · doi:10.1016/j.metabol.2015.10.002 · Cited by 70 · see citing works
Self-citationStructure and function of a novel antioxidant peptide from the skin of tropical frogs
Barbosa, É. A., Oliveira, A. L. S., Plácido, A., Socodato, R., Portugal, C. C., Mafud, A. C., Ombredane, A. S., Moreira, D. C., Vale, N., Bessa, L. J., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.11.001 · Cited by 64 · see citing works
Pigments and minor compounds in algae
Kraan, S. (2013) · Elsevier eBooks · doi:10.1533/9780857098689.1.205 · Cited by 60 · see citing works
Cian, R. E., Hernández‐Chirlaque, C., Gámez‐Belmonte, R., Drago, S. R., de Medina, F. S., & Martínez‐Augustin, O. (2018) · Marine Drugs · doi:10.3390/md16070235 · Cited by 53 · see citing works
Wang, Z., Cui, Y., Liu, P., Zhao, Y., Wang, L., Liu, Y., & Xie, J. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b05026 · Cited by 52 · see citing works
Ringseis, R., Matthes, B., Lehmann, V., Becker, K., Schöps, R., Ulbrich‐Hofmann, R., & Eder, K. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.10.005 · Cited by 46 · see citing works
Smith, H. S. (2009) · Mayo Clinic Proceedings · doi:10.4065/84.7.613 · Cited by 44 · see citing works
In Silico Assessment of the Potential of Patatin as a Precursor of Bioactive Peptides
Fu, Y., Wu, W., Zhu, M., & Xiao, Z. (2015) · Journal of Food Biochemistry · doi:10.1111/jfbc.12213 · Cited by 40 · see citing works
Seaweed Proteins as a Source of Bioactive Peptides
Alboofetileh, M., Hamzeh, A., & Abdollahi, M. (2021) · Current Pharmaceutical Design · doi:10.2174/1381612827666210208153249 · Cited by 34 · see citing works
Kęska, P., Stadnik, J., Bąk, O., & Borowski, P. (2019) · Nutrients · doi:10.3390/nu11102537 · Cited by 28 · see citing works
Structure-Function of Prolyl Oligopeptidase and its Role in Neurological Disorders
Polgár, L. (2002) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/1568015023357860 · Cited by 26 · see citing works
Villares, R., Puente, X. A., & Carballeira, A. (1999) · Cited by 22 · see citing works
In Silico Analysis of Bioactive Peptides in Invasive Sea Grass Halophila stipulacea
Çavaş, Ç. K., Pérez‐Sánchez, H., Ozupek, N. M., & Çavaş, L. (2019) · Cells · doi:10.3390/cells8060557 · Cited by 22 · see citing works
Glu–Phe from onion (Allium Cepa L.) attenuates lipogenesis in hepatocytes
Lee, Y. G., Cho, J., Hwang, E. J., Jeon, T., & Moon, J. (2017) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2017.1303358 · Cited by 13 · see citing works
Hamit, C. S., Nam, K., & Abeyrathne, E. D. N. S. (2022) · Applied Phycology · doi:10.1080/26388081.2022.2063758 · Cited by 9 · see citing works
Liapina, L. A., Grigor'eva, M. E., Andreeva, L. A., & Miasoedov, N. F. (2010) · PubMed · Cited by 3 · see citing works
Prospect of Marine Bioactive Peptides as DPP4 Inhibitor
Alam, M. M. (2022) · Oceanography & Fisheries Open access Journal · doi:10.19080/ofoaj.2022.14.555896 · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 5
- Apaydin G, Aylikci V, Cengiz E, Saydam M, Kup N, Tirasoglu E. Analysis of metal contents of seaweed (Ulva lactuca) from istanbul, Turkey by EDXRF. Turk J Fish Aquat Sci 2010;10(2). https://doi.org/10.4194/trjfas.2010.0209. · DOI
- Ziganshin R, Svieryaev VI, Vaskovsky V, Mikhaleva II, Ivanov VT, Kokoz YM, Alekseev AE, Korystova AF, Sukhova GS, Emel'ianova TG. Bioactive peptides isolated from the brain of hibernating ground squirrel. Bioorg Khim 1994;20(8-9): 899-918.
- Md Morshedul A. Therapeutic potential of marine bioactive compounds against SARS-CoV2 infection. CPQ Medicine 2020;11(1):1-18.
- Md Morshedul A. Essence of antioxidants in aging science: NRF2, a true fact. CPQ Medicine 2019;5(5):1-5.
- Md Morshedul A. Possibility of NRF2 activation as a priming tool against SARS- COV2 infection. CPQ Medicine 2020;10(2):1-5.
Cited by
Sorted by citations
Ali, M. Q., Azhar, M. A., Munaim, M. S. A., Ruslan, N. F., Alsubhi, L. M., Noormazlinah, A., & Noman, A. E. (2024) · Discover Food · doi:10.1007/s44187-024-00173-w · Cited by 22 · see citing works
Taraszkiewicz, A., Sinkiewicz, I., Sommer, A., & Staroszczyk, H. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2170973 · Cited by 22 · see citing works
Dhaouafi, J., Romdhani, M., Deracinois, B., Flahaut, C., Nedjar, N., & Balti, R. (2024) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2024.103211 · Cited by 18 · see citing works
Wang, L., Wang, L., Liu, X., Lin, X., Tao, F., & Zhang, W. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2449596 · Cited by 18 · see citing works
Kang, Y.-A., Kim, Y., Jin, S.-K., & Choi, H. (2023) · Marine Drugs · doi:10.3390/md21090469 · Cited by 15 · see citing works
Ghelichi, S., Hajfathalian, M., Helalat, S. H., Svensson, B., & Jacobsen, C. (2025) · Marine Drugs · doi:10.3390/md23100392 · Cited by 13 · see citing works
Shannon, E., & Hayes, M. (2025) · Foods · doi:10.3390/foods14020284 · Cited by 12 · see citing works
Uses of Papaya Leaf and Seaweed Supplementations for Controlling Glucose Homeostasis in Diabetes
Nyakundi, B. B., & Yang, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076846 · Cited by 15 · see citing works
Investigation of Anticancer Peptides Derived from Arca Species Using In Silico Analysis
Wu, J., Zhang, X., Jin, Y., Zhang, M., Yu, R., Song, L., Liu, F., & Zhu, J. (2025) · Molecules · doi:10.3390/molecules30071640 · 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
Hong, Q., Wu, H., Jia, X., Yang, Y., Yong, J., Xing, Q., & Liu, Z. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.107939 · Cited by 6 · see citing works
Dhaouafi, J., Romdhani, M., Deracinois, B., Flahaut, C., Balti, R., & Nedjar, N. (2024) · Waste and Biomass Valorization · doi:10.1007/s12649-024-02715-w · Cited by 6 · see citing works
Budiyanto, F., Sari, M., Widyaningrum, S. R., Putra, A. B. N., Palupi, K. D., Rachman, F., Untari, F., Handayani, T., & Rasyid, A. (2025) · Algal Research · doi:10.1016/j.algal.2025.104181 · Cited by 6 · see citing works
Khaliq, M., Noor, Z., Moazzam, M., Saeed, F., Tul-Zohra, K., Tariq, E., Muhammad Shahbaz, H., & Khaliq, K. (2026) · Annals of Medicine · doi:10.1080/07853890.2026.2637282 · Cited by 4 · see citing works
“Such in silico-directed approaches have gained increasing popularity in recent studies of algal proteins (e.g. Limnospira platensis , Chlorella vulgaris , and Ulva lactuca ) to guide the discovery process faster and maximize the specificity of peptide selection [119,214,215].”
Nouri, M., Mousavi, Z. E., Parandi, E., & Goudarzi, M. (2025) · LWT · doi:10.1016/j.lwt.2025.118203 · Cited by 3 · see citing works
Amin, M. A., Chondra, U., & Alam, M. M. (2024) · Journal of Exploratory Research in Pharmacology · doi:10.14218/jerp.2023.00030 · Cited by 2 · see citing works
Self-citationJhoomuck, S. K., & Mund, P. (2025) · Journal of Drug Delivery and Therapeutics · doi:10.22270/jddt.v15i7.7216 · Cited by 2 · see citing works
Windarto, S., Herawati, V. E., Wijaya, Y. J., & Indriati, D. A. (2025) · Biotech Studies · doi:10.38042/biotechstudies.1756936 · Cited by 2 · see citing works
Araújo, J., Carvalho, A. C., Matias, A. C., Ribeiro, M. C., Soares, F., & Pousão‐Ferreira, P. (2025) · Fishes · doi:10.3390/fishes10090447 · Cited by 2 · see citing works
Berraquero‐García, C., García‐Moreno, P. J., Pérez‐Gálvez, R., Espejo-Carpio, F. J., & Guadix, E. M. (2025) · Journal of Insects as Food and Feed · doi:10.1163/23524588-00001304 · Cited by 1 · see citing works
Putra, N. R., Rizkiyah, D. N., Mukhaimin, I., Mamat, H., Aziz, A. H. A., & Airlangga, B. (2025) · Journal of Aquatic Food Product Technology · doi:10.1080/10498850.2025.2504909 · Cited by 1 · see citing works
In Silico Evaluation of Human α‐S1‐Casein, β‐Casein, and κ‐Casein as a Source of Bioactive Peptides
Zavala-Trejo, D. A., Aguilar‐Uscanga, B. R., Arreola, A. R., Quezada, E. G., & Solís-Pacheco, J. R. (2025) · Journal of Food Biochemistry · doi:10.1155/jfbc/1831514 · Cited by 1 · see citing works
Khan, A. M., Munna, M. M. R., Shoyshob, T. Z., Haque, M. R., & Hannan, M. A. (2026) · Journal of Food Biochemistry · doi:10.1155/jfbc/9116317 · Cited by 1 · see citing works
Account on the diversity and distribution of the genus Ulva from India
Kumar, Y. A. S., Mookkan, P., Yadav, S. K., & Savurirajan, M. (2024) · Regional Studies in Marine Science · doi:10.1016/j.rsma.2024.103634 · Cited by 1 · see citing works
Li, H., Cao, W., Wang, Z., Song, C., Chen, Z., Tan, M., Lin, H., & Gao, J. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4526961
Pharmacological Importance of Gracilariopsis Lemaniformis Seaweed
Alam, M. M. (2023) · Oceanography & Fisheries Open access Journal · doi:10.19080/ofoaj.2023.16.555927
Self-citationKumar, L. R. G., Tejpal, C. S., Anas, K. K., Vishnu, K. V., Mohanan, V., Pavithra, P. A., & Venkatesan, J. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4869402
Bioactivity and Biofunctionality Characterization of Algal Biomass
Echave, J., Barciela, P., Perez-Vazquez, A., Seyyedi-Mansour, S., Donn, P., Cassani, L., Prieto, M. A., Simal‐Gándara, J., Otero, P., & Fraga‐Corral, M. (2024) · Environmental science and engineering · doi:10.1007/978-981-97-2371-3_23
Nusaibah, N., Rhamadani, T. J., Arumsari, K., Siregar, A. N., Andayani, T. R., Maulid, D. Y., & Pangestika, W. (2024) · Jurnal Pengolahan Hasil Perikanan Indonesia · doi:10.17844/jphpi.v27i6.53338
In silico Evaluation of Potential Bioactive Peptides of Phycoerythrins from Selected Rhodophytes
Sharmin, K. N., White, W. L., & Lee, K. C. Y. (2025) · The Open Bioinformatics Journal · doi:10.2174/0118750362370187250307055547
Hong, Q., Wu, H., jia, X., Yang, Y., Xing, Q., & Liu, Z. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5349415
Wang, M.-J., Zhao, Z., Qiu, Y.-C., Zhang, Y., & Mu, Z.-S. (2025) · International Dairy Journal · doi:10.1016/j.idairyj.2025.106457
Thuraisingam, S. L., Heijink, I. H., Goh, B. H., & Yow, Y. (2025) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2025.100235
- Authors
- Amin, M. A., Chondra, U., Mostafa, E., & Alam, M. M.
- Affiliations
- Bangladesh Maritime University (BD)
- Corresponding author
- Alam, Md.Morshedul
- Venue
- Informatics in Medicine Unlocked
- Publisher
- Elsevier BV
- Published
- 2022
- Volume
- 33
- Pages
- 101099
- ISSN
- 2352-9148 (ISSN-L)
- OpenAlex
- W4297322800
- Cited by
- 33
- References
- 55
- Citations by year
- 2026: 3 · 2025: 17 · 2024: 8 · 2023: 5
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Informatics in Medicine Unlocked (publishedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- 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
- Physical Sciences › Computer Science › Computational Theory and Mathematics › Computational Drug Discovery Methods
- Keywords
- Ulva lactuca, green seaweed, bioactive peptides, Rubisco, pancreatic elastase, antihypertensive peptides, angiotensin-converting enzyme inhibition, antioxidant peptides, antithrombotic peptides, antidiabetic peptides, marine biotechnology, peptide toxicity prediction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
