Cn‐AMP1: A new promiscuous peptide with potential for microbial infections treatment
Abstract
The antimicrobial peptides (AMPs) are evolutionarily ancient molecules that act as components of the innate immune system. Recently, it was demonstrated that a single AMP can perform various functions; this ability is known as “peptide promiscuity.” However, little is known about promiscuity in plant AMPs without disulfide bonds. This study was carried out to evaluate the promiscuity of Cn‐AMP1: a promising disulfide‐free plant peptide with reduced size and cationic and hydrophobic properties. Its activity against human pathogenic bacteria and fungal pathogens, as well as its in vitro immunostimulatory activity and effects on cancerous and healthy mammalian cell proliferation were studied here. Cn‐AMP1 exerts antimicrobial effects against Gram‐positive bacteria, Gram‐negative bacteria, and fungi. Moreover, tumor cell viability activity in Caco‐2 cells, as well as immunostimulatory activity by evaluating upregulated inflammatory‐cytokine secretion by monocytes was also positively observed. Cn‐AMP1 does not exhibit a well‐defined conformation in aqueous solution and probably undergoes a 3 10‐helix transition in hydrophobic environments. The experimental results support the promiscuous activity of Cn‐AMP1, presenting a wide range of activities, including antibacterial, antifungal, and immunostimulatory activity. In the future, Cn‐AMP1 should be used in the development of novel biopharmaceuticals, mainly due to its reduced size and broad spectrum of activity. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 322–331, 2012.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
CnAMP1 reduced cell viability in a dose-dependent manner in nondifferentiated Caco-2 cells.
“In nondifferentiated Caco-2 cells, however, they observed that CnAMP1 reduced cell viability in a dose-dependent manner [12].”
From The Coconut Water Antimicrobial Peptide CnAMP1 Is Taken up into Intestinal Cells but Does Not Alter P-Glycoprotein Expression and Activity (2020) · cites this paper as [12]
Cn-AMP1 is a promiscuous peptide with activity against bacteria, fungi, cancer cells, and immunostimulatory activity.
“These features give the peptide Cn-AMP1 a promiscuous character, even not presenting disulfide bond connection [9,11].”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [11]
The data reported here corroborate the theoretical data presented for Cn-AMP1 by molecular modeling.
“Indeed, data reported here corroborate the theoretical data presented for Cn-AMP1 by using molecular modeling [9,11].”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [11]
Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works
Electrostatics of nanosystems: Application to microtubules and the ribosome
Baker, N., Sept, D., Joseph, S., Holst, M., & McCammon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181342398 · Cited by 7,125 · see citing works
Wiegand, I., Hilpert, K., & Hancock, R. E. W. (2008) · Nature Protocols · doi:10.1038/nprot.2007.521 · Cited by 6,156 · see citing works
Wiederstein, M., & Sippl, M. J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm290 · Cited by 5,909 · see citing works
Clinical and Laboratory Standards Institute
Gressner, A. M., & Arndt, T. (2019) · Springer Reference Medizin · doi:10.1007/978-3-662-48986-4_300416 · Cited by 5,092 · see citing works
Protein homology detection by HMM–HMM comparison
Söding, J. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bti125 · Cited by 2,381 · see citing works
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305 · see citing works
Determination of the helix and β form of proteins in aqueous solution by circular dichroism
Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,071 · see citing works
(2000) · Cited by 1,342 · see citing works
Pollock, J. S., Förstermann, U., Mitchell, J. A., Warner, T. D., Schmidt, H. H. H. W., Nakane, M., & Murad, F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10480 · Cited by 979 · see citing works
APD2: the updated antimicrobial peptide database and its application in peptide design.
Wang, G., Li, X., & Wang, Z. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn823 · Cited by 941 · see citing works
Campylobacter spp. as a Foodborne Pathogen: A Review
Silva, J. G. L., Leite, D., Fernandes, M., Mena, C., Gibbs, P., & Teixeira, P. (2011) · Front. Microbio. · doi:10.3389/fmicb.2011.00200 · Cited by 632 · see citing works
Host defense peptides as new weapons in cancer treatment
Papo, N., & Shai, Y. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-4560-2 · Cited by 501 · see citing works
Optimization of the antimicrobial activity of magainin peptides by modification of charge
Dathe, M., Nikolenko, H., Meyer, J., Beyermann, M., & Bienert, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02648-5 · Cited by 433 · see citing works
Antiviral and antitumor peptides from insects
Chernysh, S. I., Kim, S. I., Bekker, G., Pleskach, V. A., Filatova, N. A., Anikin, V. B., Vg, P., & Bulet, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192301899 · Cited by 376 · see citing works
Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells
Laakkonen, P. M., Åkerman, M. E., Biliran, H., Yang, M., Ferrer, F. A., Kärpänen, T., Hoffman, R. M., & Ruoslahti, E. I. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403317101 · Cited by 276 · see citing works
Stotz, H. U., Thomson, J. G., & Wang, Y. (2009) · Plant Signaling & Behavior · doi:10.4161/psb.4.11.9755 · Cited by 270 · see citing works
Hwang, P. M., Zhou, N., Shan, X., Arrowsmith, C. H., & Vogel, H. J. (1998) · Biochemistry · doi:10.1021/bi972323m · Cited by 252 · see citing works
A linguistic model for the rational design of antimicrobial peptides
Loose, C. R., Jensen, K. L., Rigoutsos, I., & Stephanopoulos, G. N. (2006) · Nature · doi:10.1038/nature05233 · Cited by 248 · see citing works
Antitumor Activity of the Antimicrobial Peptide Magainin II against Bladder Cancer Cell Lines
Lehmann, J., Retz, M. M., Sidhu, S., Suttmann, H., Sell, M., Paulsen, F. P., Harder, J., Unteregger, G., & Stöckle, M. (2006) · European Urology · doi:10.1016/j.eururo.2005.12.043 · Cited by 229 · see citing works
Chaly, Y., Paleolog, E. M., Kolesnikova, T. S., Tikhonov, I. I., Petratchenko, E. V., & Voitenok, N. N. (2000) · PubMed · Cited by 210 · see citing works
Carmen, J. C., & Sinai, A. P. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00001 · Cited by 184 · see citing works
Suttmann, H., Retz, M. M., Paulsen, F. P., Harder, J., Zwergel, U., Kamradt, J., Wullich, B., Unteregger, G., Stöckle, M., & Lehmann, J. (2008) · BMC Urology · doi:10.1186/1471-2490-8-5 · Cited by 173 · see citing works
Proteolysis of Human Thrombin Generates Novel Host Defense Peptides
Papareddy, P., Rydengård, V., Pasupuleti, M., Walse, B., Mörgelin, M., Chalupka, A., Malmsten, M., & Schmidtchen, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000857 · Cited by 167 · see citing works
Antimicrobial activity studies on a trypsin–chymotrypsin protease inhibitor obtained from potato
Kim, J., Park, S., Kim, M.-H., Lim, H., Park, Y., & Hahm, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.057 · Cited by 156 · see citing works
The role of the multifunctional peptide LL-37 in host defense
Kai-Larsen, Y. (2008) · Frontiers in bioscience · doi:10.2741/2964 · Cited by 141 · see citing works
Wu, W. K. K., Wang, G., Coffelt, S. B., Betancourt, A. M., Lee, C. W., Fan, D., Wu, K., Yu, J. Q., Sung, J. J. �., & Cho, C. H. (2010) · International Journal of Cancer · doi:10.1002/ijc.25489 · Cited by 136 · see citing works
Pelegrini, P. B., Murad, A. M., Silva, L. P., dos Santos, R. C. P., Costa, F. T., Tagliari, P. D., Bloch Jr, C., Noronha, E. F., Miller, R. N. G., & Franco, O. L. (2008) · Peptides · doi:10.1016/j.peptides.2008.03.013 · Cited by 136 · see citing works
Self-citationMandal, S. M., Dey, S., Mandal, M., Sarkar, S., Maria-Neto, S., & Franco, O. L. (2009) · Peptides · doi:10.1016/j.peptides.2008.12.001 · Cited by 136 · see citing works
Self-citationPeptide promiscuity: An evolutionary concept for plant defense
Franco, O. L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.03.008 · Cited by 135 · see citing works
Self-citationEnd-Tagging of Ultra-Short Antimicrobial Peptides by W/F Stretches to Facilitate Bacterial Killing
Pasupuleti, M., Schmidtchen, A., Chalupka, A., Ringstad, L., & Malmsten, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005285 · Cited by 111 · see citing works
Wang, G., Li, Y., & Li, X. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410116200 · Cited by 102 · see citing works
Csord�s, A., & Michl, H. (1970) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf00907538 · Cited by 89 · see citing works
Andreu, D., ASCHAUER, H., Kreil, G., & Merrifield, R. B. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb08957.x · Cited by 85 · see citing works
Kristiansen, P. E., Fimland, G., Mantzilas, D., & Nissen-Meyer, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501620200 · Cited by 82 · see citing works
Structure and function of a custom anticancer peptide, CB1a
Wu, J.-M., Jan, P.-S., Yu, H.-C., Haung, H.-Y., Fang, H., Chang, Y., Cheng, J.-W., & Chen, H. M. (2009) · Peptides · doi:10.1016/j.peptides.2009.02.004 · Cited by 77 · see citing works
López‐Abarrategui, C., Alba, A., Silva, O. N., Reyes‐Acosta, O., Vasconcelos, I. M., Oliveira, J. T. A., Migliolo, L., da Costa, M. P., Costa, C. R., Silva, M. R. R., et al. (2011) · Biochimie · doi:10.1016/j.biochi.2011.12.016 · Cited by 71 · see citing works
Self-citationHuman α-defensin-1 inhibits growth of human lung adenocarcinoma xenograft in nude mice
Xu, N., Wang, Y., Pan, W., Xiao, B., Wen, Y., Chen, X., Chen, L., Deng, H., You, J., Kan, B., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0010 · Cited by 68 · see citing works
Nijnik, A., & Hancock, R. E. W. (2009) · Emerging Health Threats Journal · doi:10.3402/ehtj.v2i0.7078 · Cited by 68 · see citing works
Mandal, S. M., Migliolo, L., Das, S., Mandal, M., Franco, O. L., & Hazra, T. K. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23343 · Cited by 62 · see citing works
Self-citationA novel proline rich bombesin-related peptide (PR-bombesin) from toad Bombina maxima
Lai, R., Liu, H., Lee, W. H., & Zhang, Y. (2002) · Peptides · doi:10.1016/s0196-9781(01)00642-8 · Cited by 40 · see citing works
Loeffler, S. (2011) · Frontiers A Journal of Women Studies · doi:10.5250/fronjwomestud.32.1.0001 · Cited by 34 · see citing works
Emerging aspects of assessing lead poisoning in childhood
Jones, A. (2008) · Emerging Health Threats Journal · doi:10.3134/ehtj.09.003 · Cited by 27 · see citing works
Mayo, K. H., Haseman, J. R., Young, H. C., & MAYO, J. W. (2000) · Biochemical Journal · doi:10.1042/bj3490717 · Cited by 26 · see citing works
Pinto, M. F. S., de Almeida, R. G., Porto, W. F., Fensterseifer, I. C. M., de Lima, L. A., Dias, S. C., & Franco, O. L. (2011) · Journal of Evidence-Based Complementary & Alternative Medicine · doi:10.1177/2156587211428077 · Cited by 22 · see citing works
Self-citationA Kunitz Proteinase Inhibitor from Corms of Xanthosoma blandum with Bactericidal Activity
Lima, T. B., Silva, O. N., Migliolo, L., Souza-Filho, C. R., Gonçalves, E. G., Vasconcelos, I. M., Oliveira, J. T. A., Amaral, A. C., & Franco, O. L. (2011) · Journal of Natural Products · doi:10.1021/np200312r · Cited by 18 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Antimicrobial Peptides from Plants
Tam, J. P., Wang, S., Wong, K. H., & Tan, W. (2015) · Pharmaceuticals · doi:10.3390/ph8040711 · Cited by 491 · see citing works
Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides
Mulder, K. C. L., de Lima, L. A., Miranda, V. D. J., Dias, S. C., & Franco, O. L. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00321 · Cited by 211 · see citing works
Self-citationPlant Antimicrobial Peptides as Potential Anticancer Agents
Guzmán-Rodríguez, J. J., Ochoa‐Zarzosa, A., López-Gómez, R., & López-Meza, J. E. (2015) · BioMed Research International · doi:10.1155/2015/735087 · Cited by 130 · see citing works
The use of versatile plant antimicrobial peptides in agribusiness and human health
de Souza Cândido, E., e Silva Cardoso, M. H., Sousa, D. A., Viana, J. C., de Oliveira-Júnior, N. G., Miranda, V., & Franco, O. L. (2014) · Peptides · doi:10.1016/j.peptides.2014.02.003 · Cited by 124 · see citing works
Self-citationSynthetic Biology and Computer-Based Frameworks for Antimicrobial Peptide Discovery
Torres, M. D. T., Cao, J., Franco, O. L., Lu, T. K., & de la Fuente‐Núñez, C. (2021) · ACS Nano · doi:10.1021/acsnano.0c09509 · Cited by 123 · see citing works
Self-citationAn anti-infective synthetic peptide with dual antimicrobial and immunomodulatory activities
Silva, O. N., de la Fuente‐Núñez, C., Haney, E. F., Fensterseifer, I. C. M., Ribeiro, S. M., Porto, W. F., Brown, P., Faria-Junior, C., Rezende, T. M. B., Moreno, S. E., et al. (2016) · Scientific Reports · doi:10.1038/srep35465 · Cited by 122 · see citing works
Self-citationComputational tools for exploring sequence databases as a resource for antimicrobial peptides
Porto, W. F., Pires, Á. S., & Franco, O. L. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.02.001 · Cited by 122 · see citing works
Self-citationPorto, W. F., Pires, Á. S., & Franco, O. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051444 · Cited by 113 · see citing works
Self-citationJoker: An algorithm to insert patterns into sequences for designing antimicrobial peptides
Porto, W. F., Fensterseifer, I. C. M., Ribeiro, S. M., & Franco, O. L. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.06.011 · Cited by 85 · see citing works
Self-citationMeneguetti, B. T., Machado, L. D. S., Oshiro, K. G. N., Nogueira, M. L., Carvalho, C. M. E., & Franco, O. L. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02136 · Cited by 77 · see citing works
Self-citationInsect antimicrobial peptides: potential tools for the prevention of skin cancer
Tonk, M., Vilcinskas, A., & Rahnamaeian, M. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-7718-y · Cited by 75 · see citing works
Theoretical structural insights into the snakin/GASA family
Porto, W. F., & Franco, O. L. (2013) · Peptides · doi:10.1016/j.peptides.2013.03.014 · Cited by 65 · see citing works
Self-citationIdentification of multifunctional peptides from human milk
Mandal, S. M., Bharti, R., Porto, W. F., Gauri, S. S., Mandal, M., Franco, O. L., & Ghosh, A. K. (2014) · Peptides · doi:10.1016/j.peptides.2014.03.017 · Cited by 54 · see citing works
Self-citationLinear antimicrobial peptides with activity against herpes simplex virus 1 and Aichi virus
Boas, L. C. P. V., de Lima, L. M. P., Migliolo, L., Mendes, G. D. S., de Jesus, M. G., Franco, O. L., & Silva, P. A. (2016) · Biopolymers · doi:10.1002/bip.22871 · Cited by 53 · see citing works
Self-citationMigliolo, L., Silva, O. N., Silva, P. A., Costa, M. P., Costa, C. R., Nolasco, D. O., Barbosa, J. A. R. G., Silva, M. R. R., Bemquerer, M. P., Lima, L. M. P., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047047 · Cited by 48 · see citing works
Self-citationClavanin A Improves Outcome of Complications from Different Bacterial Infections
Silva, O. N., Fensterseifer, I. C. M., Rodrigues, E. A., Holanda, H. H. S., Novaes, N. R. F., Cunha, J. P. A., Rezende, T. M. B., Magalhães, K. G., Moreno, S. E., Jerônimo, M. S., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03732-14 · Cited by 46 · see citing works
Self-citationMultiple roles of ribosomal antimicrobial peptides in tackling global antimicrobial resistance
Xuan, H. L., Ngan, H. D., Phuong, H. B. T., Quoc, T. N., & Tùng, T. T. (2022) · Royal Society Open Science · doi:10.1098/rsos.211583 · Cited by 45 · see citing works
Effects of cyclotides against cutaneous infections caused by Staphylococcus aureus
Fensterseifer, I. C. M., Silva, O. N., Malik, U., Ravipati, A. S., Novaes, N. R. F., Miranda, P. R. R., Rodrigues, E. A., Moreno, S. E., Craik, D. J., & Franco, O. L. (2014) · Peptides · doi:10.1016/j.peptides.2014.10.019 · Cited by 45 · see citing works
Self-citationStructural and functional evaluation of the palindromic alanine-rich antimicrobial peptide Pa -MAP2
Migliolo, L., Felício, M. R., Cardoso, M. H. E. S., Silva, O. N., Xavier, M.-A. E., Nolasco, D. O., de Oliveira, A. S., Roca, I., Estape, J. V., Teixeira, L. D., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.04.003 · Cited by 45 · see citing works
Self-citationThe role of peptide-based therapeutics in oncotherapy
Timur, S. S., & Gürsoy, R. N. (2021) · Journal of drug targeting · doi:10.1080/1061186x.2021.1906884 · Cited by 40 · see citing works
Su, H., Chen, Z.-H., Song, X., Chen, X., Shi, M., Zhou, B., Zhao, X., & Zhang, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045818 · Cited by 39 · see citing works
Bezerra, C. D. S., de Oliveira, C. F. R., Machado, O. L. T., de Mello, G. S. V., Pitta, M. G. D. R., Rêgo, M. J. B. D. M., Napoleão, T. H., Paiva, P. M. G., Ribeiro, S. F. F., Gomes, V. M., et al. (2016) · Process Biochemistry · doi:10.1016/j.procbio.2016.03.008 · Cited by 33 · see citing works
Self-citationCharacterization of a Bioactive Acyclotide from Palicourea rigida
Pinto, M. F. S., Silva, O. N., Viana, J., Porto, W. F., Migliolo, L., da Cunha, N. B., Gomes, N., Fensterseifer, I. C. M., Colgrave, M. L., Craik, D. J., et al. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6b00270 · Cited by 33 · see citing works
Self-citationMandal, S. M., Porto, W. F., Dey, P., Maiti, M. K., Ghosh, A. K., & Franco, O. L. (2013) · Biochimie · doi:10.1016/j.biochi.2013.06.027 · Cited by 26 · see citing works
Self-citationPeptides from plants and their applications
Hayes, M., & Bleakley, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-100736-5.00025-9 · Cited by 26 · see citing works
The biological role of charge distribution in linear antimicrobial peptides
Duque, H. M., Rodrigues, G. R., dos Santos, L. S., & Franco, O. L. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2173736 · Cited by 25 · see citing works
Self-citationAnaya, K., Podszun, M., Franco, O. L., de Almeida Gadelha, C. A., & Frank, J. (2020) · Plant Foods for Human Nutrition · doi:10.1007/s11130-020-00826-y · Cited by 24 · see citing works
Self-citationIn vivo antimicrobial evaluation of an alanine-rich peptide derived from Pleuronectes americanus
Teixeira, L. D., Silva, O. N., Migliolo, L., Fensterseifer, I. C. M., & Franco, O. L. (2013) · Peptides · doi:10.1016/j.peptides.2013.02.001 · Cited by 22 · see citing works
Self-citationUmadevi, P., Soumya, M., George, J. K., & Anandaraj, M. (2018) · Physiology and Molecular Biology of Plants · doi:10.1007/s12298-018-0524-5 · Cited by 22 · see citing works
Santana, M. J., de Oliveira, A. L., Queiroz Júnior, L. H. K., Mandal, S. M., Matos, C. O., de O. Dias, R., Franco, O. L., & Lião, L. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.01.029 · Cited by 21 · see citing works
Self-citationLeite, M. L., de Oliveira, K. B. S., Costa, F. F., Franco, O. L., Dias, S. C., & da Cunha, N. B. (2018) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765201820180124 · Cited by 21 · see citing works
Self-citationLuo, X., Wu, W., Feng, L., Treves, H., & Ren, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111363 · Cited by 21 · see citing works
Mandal, S. M., Khan, J., Mahata, D., Saha, S., Sengupta, J., Silva, O. N., Das, S., Mandal, M., & Franco, O. L. (2017) · Biofouling · doi:10.1080/08927014.2017.1383400 · Cited by 20 · see citing works
Self-citationGreen Antimicrobials as Therapeutic Agents for Diabetic Foot Ulcers
Teixeira, I. D., Carvalho, E., & Leal, E. C. (2023) · Antibiotics · doi:10.3390/antibiotics12030467 · Cited by 14 · see citing works
Antimicrobial peptide selection from Lippia spp leaf transcriptomes
Tavares, L. S., de Souza, V. C., Nunes, V. S., Silva, O. N., de Souza, G. T., Marques, L. F., Goliatt, P. V. Z. C., Viccini, L. F., Franco, O. L., & Santos, M. D. O. (2020) · Peptides · doi:10.1016/j.peptides.2020.170317 · Cited by 13 · see citing works
Self-citationAnticancer Peptides: Prospective Innovation in Cancer Therapy
Gaspar, D., & Castanho, M. A. R. B. (2016) · Springer eBooks · doi:10.1007/978-3-319-32949-9_4 · Cited by 13 · see citing works
Antibiotic combinations for controlling colistin-resistant Enterobacter cloacae
Lima, T. B., Silva, O. N., de Almeida, K. C., Ribeiro, S. M., Motta, D. D. O., Maria-Neto, S., Lara, M. B., Souza-Filho, C. R., Ombredane, A. S., Faria-Junior, C., et al. (2016) · The Journal of Antibiotics · doi:10.1038/ja.2016.77 · Cited by 12 · see citing works
Self-citationComposition, Properties and Reactions of Coconut Water
Rethinam, P., & Krishnakumar, V. (2022) · Coconut Water · doi:10.1007/978-3-031-10713-9_4 · Cited by 9 · see citing works
Anurans against SARS-CoV-2: A review of the potential antiviral action of anurans cutaneous peptides
de Amaral, M., & Ienes-Lima, J. (2022) · Virus Research · doi:10.1016/j.virusres.2022.198769 · Cited by 8 · see citing works
Porto, W. F., Nolasco, D. O., & Franco, O. L. (2014) · Peptides · doi:10.1016/j.peptides.2014.02.010 · Cited by 8 · see citing works
Self-citationEvaluation of a Novel Synthetic Peptide Derived from Cytolytic Mycotoxin Candidalysin
Cardoso, P. H. D. O., Boleti, A. P. D. A., Silva, P. S. E., Mukoyama, L. T. H., Guindo, A. S., de Moraes, L. F. R. N., de Oliveira, C. F. R., Macedo, M. L. R., Carvalho, C. M. E., de Castro, A. P., et al. (2022) · Toxins · doi:10.3390/toxins14100696 · Cited by 6 · see citing works
Self-citationde Sousa, B. A., Silva, O. N., Porto, W. F., Rocha, T. L., Silva, L. P., Leal, A. P. F., Buccini, D. F., Fajemiroye, J. O., Caldas, R. D. A., Franco, O. L., et al. (2021) · Molecules · doi:10.3390/molecules26103054 · Cited by 5 · see citing works
Self-citationAnaya, K., Sus, N., Gadelha, C., & Frank, J. (2019) · Amino Acids · doi:10.1007/s00726-018-2675-7 · Cited by 5 · see citing works
Ngan, H. D., Huy, B. L., Uyen, C. L., Phuong, H. B. T., & Xuan, H. L. (2025) · European Food Research and Technology · doi:10.1007/s00217-025-04754-6 · Cited by 3 · see citing works
Antimicrobial peptides: Design, chemical synthesis, activity evaluation, and application
Yang, H., Wang, L., Du, H., Zhao, D., Liu, C., & Lu, K. (2023) · International Food Research Journal · doi:10.47836/ifrj.30.4.01 · Cited by 2 · see citing works
Plant Microbe Interface: The Plant Antimicrobial Peptides
Manivannan, S., & Umadevi, P. (2019) · Springer eBooks · doi:10.1007/978-3-030-26657-8_15 · Cited by 1 · see citing works
Lu, J. (2020) · ScholarWorks -A service of University of Vermont Libraries (University of Vermont) · Cited by 1 · see citing works
Peptides from agribusiness to human health
Franco, O. L., & Santos, N. C. (2012) · Biopolymers · doi:10.1002/bip.22113
Self-citationHai, B. T. P., Van, K. D., Dang, T. T., Thi, H. H., Tran, P., Quoc, T. N., Dao, V., & Xuan, H. L. (2026) · Vietnam Journal of Chemistry · doi:10.1002/vjch.70161
Natural and Synthetic AMPs from Latin America across Diversity Engineering and Applications
Brango‐Vanegas, J., Cândido, E. D. S., Carneiro, J. A., Ribeiro, N. A. S., & Franco, O. L. (2026) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6c00394
Self-citationHalictine-II as a Potential Broad-Spectrum Antifungal and Antibacterial Agent
Zhang, N., Kutach, M., Hsieh, L., Vexler, S., & Chen, I. A. (2026) · Pharmaceuticals · doi:10.3390/ph19091379
- Authors
- Silva, O. N., Porto, W. F., Migliolo, L., Mandal, S. M., Gomes, D. G., Holanda, H. H. S., Silva, R. S. P., Dias, S. C., Costa, M. P., Costa, C. R., Silva, M. R., Rezende, T. M. B., & Franco, O. L.
- Affiliations
- Universidade Federal de Juiz de Fora (BR)
- Universidade Católica de Brasília (BR)
- Indian Institute of Technology Kharagpur (IN)
- Universidade Federal de Goiás (BR)
- ORCID
- Venue
- Peptide Science
- Publisher
- Wiley
- Published
- 2012-01
- Volume
- 98
- Issue
- 4
- Pages
- 322-331
- ISSN
- 0006-3525 (ISSN-L)
- OpenAlex
- W2034816905
- Cited by
- 51
- References
- 46
- Citations by year
- 2026: 3 · 2025: 1 · 2023: 3 · 2022: 4 · 2021: 4 · 2020: 3 · 2019: 1 · 2018: 4 · 2017: 4 · 2016: 8 · 2015: 3 · 2014: 5 · 2013: 4 · 2012: 4
- FWCI
- 4.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biopolymers (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Keywords
- antimicrobial peptides, plant antimicrobial peptides, antibacterial activity, antifungal activity, immune enhancement, inflammatory cytokines, monocytes, tumor cell viability, Caco-2 cells, peptide conformation, biopharmaceuticals
- MeSH terms
- Adjuvants, Immunologic, Animals, Anti-Infective Agents, Anti-Bacterial Agents, Antifungal Agents, Cell Survival, Gram-Negative Bacteria, Gram-Positive Bacteria, Humans, Peptides, Cell Line, Tumor, Cell Proliferation
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
