Assessment of bioactive peptides derived from laminin-111 as prospective breast cancer-targeting agents

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Tipo de produção
article
Data de publicação
2024
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Editora
SPRINGER WIEN
Autores
MENDONCA, Fernanda Ferreira
SOBRAL, Danielle Vieira
DURANTE, Ana Claudia Ranucci
MIRANDA, Ana Claudia Camargo
MEJIA, Jorge
BARBOZA, Marycel Figols de
FUSCALDI, Leonardo Lima
MALAVOLTA, Luciana
Citação
AMINO ACIDS, v.56, n.1, article ID 1, 13p, 2024
Projetos de Pesquisa
Unidades Organizacionais
Fascículo
Resumo
Breast cancer remains a pressing public health issue primarily affecting women. Recent research has spotlighted bioactive peptides derived from laminin-111, implicated in breast tumor development. Remarkably, the sequences IKVAV, YIGSR, and KAFDITYVRLKF from the alpha 1, beta 1, and gamma 1 chains, respectively, have garnered significant attention. This study aims to assess the potential of these radiolabeled peptides as targeting agents for breast cancer. The three peptides were synthesized using the Fmoc strategy, purified via reversed-phase high-performance liquid chromatography (RP-HPLC), and characterized through mass spectrometry. Iodine-131 (131I) radiolabeling was performed using the chloramine T method, exhibiting high radiochemical yield and stability for [131I]I-YIKVAV and [131I]I-YIGSR. Conversely, [131I]I-KAFDITYVRLKF demonstrated low radiochemical yield and stability and was excluded from the biological studies. The lipophilicity of the compounds ranged from - 2.12 to - 1.10. Serum protein binding assay for [131I]I-YIKVAV and [131I]I-YIGSR reached approximately equal to 48% and approximately equal to 25%, respectively. Affinity for breast cancer cells was evaluated using MDA-MB-231 and MCF-7 tumor cell lines, indicating the affinity of the radiopeptides with these tumor cells. Ex vivo biodistribution profiles of the radiopeptides were assessed in the MDA-MB-231 breast tumor animal model, revealing tumor tissue accumulation, supported by a high tumor-to-contralateral muscle ratio and autoradiography. These results signify the effective penetration of YIKVAV and YIGSR into tumor tissue. Therefore, the synthesized alpha 1 and beta 1 peptide fragments exhibit favorable characteristics as potential breast cancer-targeting agents, promising future exploration as radiopharmaceuticals for breast cancer.
Palavras-chave
Laminin 111-derived peptides, Targeting molecules, Radiolabeled peptides, Breast cancer
Referências
  1. Ahmadpour S, 2018, ANTI-CANCER AGENT ME, V18, P1295, DOI 10.2174/1871520618666180307142027
  2. Ahmadpour S, 2018, J BIOMED SCI, V25, DOI 10.1186/s12929-018-0420-x
  3. Batiston Adriane Pires, 2011, Rev. Bras. Saude Mater. Infant., V11, P163, DOI 10.1590/S1519-38292011000200007
  4. Bosman FT, 2003, J PATHOL, V200, P423, DOI 10.1002/path.1437
  5. de Barros ALB, 2013, J RADIOANAL NUCL CH, V295, P2083, DOI 10.1007/s10967-012-2331-8
  6. BRESALIER RS, 1995, CANCER RES, V55, P2476
  7. Brunton LL., 2010, In: Manual de Farmacologia e Terapeutica de Goodman Gilman, V12a, P04
  8. de Araújo EB, 2009, APPL RADIAT ISOTOPES, V67, P227, DOI 10.1016/j.apradiso.2008.09.009
  9. Durante ACR, 2019, PHARMACEUTICALS-BASE, V12, DOI 10.3390/ph12010025
  10. Ebenhan T, 2018, J NUCL MED, V59, P334, DOI 10.2967/jnumed.117.200048
  11. Faria DD, 2023, NUCL MED BIOL, V122, DOI 10.1016/j.nucmedbio.2023.108362
  12. Ferlay J, 2021, INT J CANCER, V149, P778, DOI 10.1002/ijc.33588
  13. FIELDS GB, 1990, INT J PEPT PROT RES, V35, P161, DOI 10.1111/j.1399-3011.1990.tb00939.x
  14. Hamill KJ, 2009, J CELL SCI, V122, P4409, DOI 10.1242/jcs.041095
  15. Hanahan D, 2011, CELL, V144, P646, DOI 10.1016/j.cell.2011.02.013
  16. He X, 2015, ONCOTARGETS THER, V8, P1483, DOI 10.2147/OTT.S82095
  17. Hu J, 2007, J HUAZHONG U SCI-MED, V27, P471, DOI 10.1007/s11596-007-0432-3
  18. HUNTER R, 1970, P SOC EXP BIOL MED, V133, P989
  19. IWAMOTO Y, 1987, SCIENCE, V238, P1132, DOI 10.1126/science.2961059
  20. JEGHERS O, 1990, EUR J NUCL MED, V17, P101, DOI 10.1007/BF00811433
  21. KAISER E, 1970, ANAL BIOCHEM, V34, P595, DOI 10.1016/0003-2697(70)90146-6
  22. Kikkawa Y, 2013, CELL ADHES MIGR, V7, P150, DOI 10.4161/cam.22827
  23. Lisco G, 2023, NUTRIENTS, V15, DOI 10.3390/nu15041004
  24. Liu F, 2020, TALANTA, V212, DOI 10.1016/j.talanta.2020.120718
  25. Mokotoff M, 1997, J PEPT RES, V49, P510
  26. Montor WR, 2018, MOL CANCER, V17, DOI 10.1186/s12943-018-0792-2
  27. Otagiri D, 2013, BIOPOLYMERS, V100, P751, DOI 10.1002/bip.22303
  28. Ponce ML, 2003, CANCER RES, V63, P5060
  29. Ponce ML, 2001, FASEB J, V15, P1389, DOI 10.1096/fj.00-0736com
  30. Sarfati G, 2011, BIOMATERIALS, V32, P152, DOI 10.1016/j.biomaterials.2010.09.014
  31. Schottelius M, 2009, METHODS, V48, P161, DOI 10.1016/j.ymeth.2009.03.012
  32. Sieni E, 2020, BIOELECTROCHEMISTRY, V136, DOI 10.1016/j.bioelechem.2020.107626
  33. Smuczek B, 2017, EXP CELL RES, V358, P323, DOI 10.1016/j.yexcr.2017.07.005
  34. Sobral DV, 2020, NUCL MED BIOL, V88-89, P14, DOI 10.1016/j.nucmedbio.2020.07.001
  35. SWEENEY TM, 1991, CANCER METAST REV, V10, P245, DOI 10.1007/BF00050795
  36. TASHIRO K, 1989, J BIOL CHEM, V264, P16174