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Volumn 4, Issue 4, 2012, Pages 198-202

Cell-penetrating Peptide-biodrug Strategy for Oral and Nasal Delivery: Review of Recent Findings

Author keywords

Cell penetrating peptides; Drug delivery; Pharmaceutical strategy; Therapeutic peptides

Indexed keywords

BIOLOGICAL PRODUCT; CELL PENETRATING PEPTIDE; EXENDIN 4; GALLIUM 68; GASTRIN; GLUCAGON LIKE PEPTIDE 1; INSULIN; OLIGOARGININE; PENETRATIN; RECOMBINANT BETA INTERFERON; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84865739024     PISSN: 18783317     EISSN: 18783325     Source Type: Journal    
DOI: 10.1016/j.jecm.2012.06.013     Document Type: Review
Times cited : (8)

References (55)
  • 1
    • 69249222717 scopus 로고    scopus 로고
    • Advances in predicting and manipulating the immunogenicity of biotherapeutics and vaccines
    • Flower D.R. Advances in predicting and manipulating the immunogenicity of biotherapeutics and vaccines. BioDrugs 2009, 23:231-240.
    • (2009) BioDrugs , vol.23 , pp. 231-240
    • Flower, D.R.1
  • 2
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: a formulation challenge
    • Frokjaer S., Otez D.D. Protein drug stability: a formulation challenge. Nat Rev Drug Discov 2005, 4:298-306.
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otez, D.D.2
  • 3
    • 36248965689 scopus 로고    scopus 로고
    • Current challenges in noninvasive insulin delivery systems: a comparative review
    • El-S Khafagy, Morishita M., Onuki Y., Takayama K. Current challenges in noninvasive insulin delivery systems: a comparative review. Adv Drug Deliv Rev 2007, 59:1521-1546.
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 1521-1546
    • El-S, K.1    Morishita, M.2    Onuki, Y.3    Takayama, K.4
  • 4
    • 33748779049 scopus 로고    scopus 로고
    • Approaches to oral drug delivery for challenging molecules
    • Mustata G., Dinh S.M. Approaches to oral drug delivery for challenging molecules. Crit Rev Ther Drug Carrier Syst 2006, 23:1111-1135.
    • (2006) Crit Rev Ther Drug Carrier Syst , vol.23 , pp. 1111-1135
    • Mustata, G.1    Dinh, S.M.2
  • 5
    • 0036633358 scopus 로고    scopus 로고
    • New horizons-alternative routes for insulin therapy
    • Owens D.R. New horizons-alternative routes for insulin therapy. Nat Rev Drug Discov 2002, 1:529-540.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 529-540
    • Owens, D.R.1
  • 6
    • 1042291852 scopus 로고    scopus 로고
    • Concept, strategies, and feasibility of noninvensive insulin delivery
    • Cefalu W.T. Concept, strategies, and feasibility of noninvensive insulin delivery. Diabetes Care 2004, 27:239-246.
    • (2004) Diabetes Care , vol.27 , pp. 239-246
    • Cefalu, W.T.1
  • 7
    • 33748752402 scopus 로고    scopus 로고
    • Is the oral route possible for peptide and protein drug delivery?
    • Morishita M., Peppas N.A. Is the oral route possible for peptide and protein drug delivery?. Drug Discov Today 2006, 11:905-910.
    • (2006) Drug Discov Today , vol.11 , pp. 905-910
    • Morishita, M.1    Peppas, N.A.2
  • 8
    • 0037393955 scopus 로고    scopus 로고
    • Challenges for the oral delivery of macromolecules
    • Goldberg M., Gomez-Orellana I. Challenges for the oral delivery of macromolecules. Nat Rev Drug Discov 2003, 2:289-295.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 289-295
    • Goldberg, M.1    Gomez-Orellana, I.2
  • 13
    • 0034212973 scopus 로고    scopus 로고
    • Intestinal transport and metabolism of glucose-conjugated kyotorphin and cyclic kyotorphin: metabolic degradation is crucial to intestinal absorption of peptide drugs
    • Mizuma T., Koyanagi A., Awazu S. Intestinal transport and metabolism of glucose-conjugated kyotorphin and cyclic kyotorphin: metabolic degradation is crucial to intestinal absorption of peptide drugs. Biochim Biophys Acta 2000, 1475:90-98.
    • (2000) Biochim Biophys Acta , vol.1475 , pp. 90-98
    • Mizuma, T.1    Koyanagi, A.2    Awazu, S.3
  • 14
    • 0020686488 scopus 로고
    • A comparison of thyrotropin-releasing hormone with analogs: influence of disposition upon pharmacology
    • Hichens M. A comparison of thyrotropin-releasing hormone with analogs: influence of disposition upon pharmacology. Drug Metab Rev 1983, 14:77-98.
    • (1983) Drug Metab Rev , vol.14 , pp. 77-98
    • Hichens, M.1
  • 15
    • 0024539595 scopus 로고
    • Synthesis of palmitoyl derivatives of insulin and their biological activities
    • Hashimoto M., Takada K., Kiso Y., Muranishi S. Synthesis of palmitoyl derivatives of insulin and their biological activities. Pharm Res 1989, 6:171-176.
    • (1989) Pharm Res , vol.6 , pp. 171-176
    • Hashimoto, M.1    Takada, K.2    Kiso, Y.3    Muranishi, S.4
  • 16
    • 2942534489 scopus 로고    scopus 로고
    • Development and in vivo evaluation of an oral insulin-PEG delivery system
    • Calceti P., Salmaso S., Walker G., Bernkop-Schnürch A. Development and in vivo evaluation of an oral insulin-PEG delivery system. Eur J Pharm Sci 2004, 22:315-323.
    • (2004) Eur J Pharm Sci , vol.22 , pp. 315-323
    • Calceti, P.1    Salmaso, S.2    Walker, G.3    Bernkop-Schnürch, A.4
  • 17
    • 33646909899 scopus 로고    scopus 로고
    • Structure-function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-PEGylation
    • Basu A., Yang K., Wang M., Liu S., Chintala R., Palm T., Zhao H., et al. Structure-function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-PEGylation. Bioconjugate Chem 2006, 17:618-630.
    • (2006) Bioconjugate Chem , vol.17 , pp. 618-630
    • Basu, A.1    Yang, K.2    Wang, M.3    Liu, S.4    Chintala, R.5    Palm, T.6    Zhao, H.7
  • 18
    • 0037467203 scopus 로고    scopus 로고
    • Reversible lipidization for the oral delivery of salmon calcitonin
    • Wang J., Chow D., Heiati H., Shen W.C. Reversible lipidization for the oral delivery of salmon calcitonin. J Control Release 2003, 26:369-380.
    • (2003) J Control Release , vol.26 , pp. 369-380
    • Wang, J.1    Chow, D.2    Heiati, H.3    Shen, W.C.4
  • 19
    • 3042664192 scopus 로고    scopus 로고
    • Use of targeting agents to increase uptake and localization of drugs to the intestinal epithelium
    • Russell-Jones G.J. Use of targeting agents to increase uptake and localization of drugs to the intestinal epithelium. J Drug Target 2004, 12:113-123.
    • (2004) J Drug Target , vol.12 , pp. 113-123
    • Russell-Jones, G.J.1
  • 20
    • 16344382196 scopus 로고    scopus 로고
    • Folate receptor mediated intracellular protein delivery using PLL-PEG-FOL conjugate
    • Hwa Kim S. Folate receptor mediated intracellular protein delivery using PLL-PEG-FOL conjugate. J Control Release 2005, 103:625-634.
    • (2005) J Control Release , vol.103 , pp. 625-634
    • Hwa Kim, S.1
  • 21
    • 23944439180 scopus 로고    scopus 로고
    • Comparison of monomeric and oligomeric transferrin as potential carrier in oral delivery of protein drugs
    • Lim C.J., Shen W.C. Comparison of monomeric and oligomeric transferrin as potential carrier in oral delivery of protein drugs. J Control Release 2005, 106:273-286.
    • (2005) J Control Release , vol.106 , pp. 273-286
    • Lim, C.J.1    Shen, W.C.2
  • 22
    • 18844381354 scopus 로고    scopus 로고
    • Recombinant granulocyte colony-stimulating factor-transferrin fusion protein as an oral myelopoietic agent
    • Bai Y., Ann D.K., Shen W.C. Recombinant granulocyte colony-stimulating factor-transferrin fusion protein as an oral myelopoietic agent. Proc Natl Acad Sci USA 2005, 102:7292-7296.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7292-7296
    • Bai, Y.1    Ann, D.K.2    Shen, W.C.3
  • 24
    • 0037449495 scopus 로고    scopus 로고
    • Mucoadhesive properties of carbopol or chitosan-coated liposomes and their effectiveness in the oral administration of calcitonin to rats
    • Takeuchi H., Matsui Y., Yamamoto H., Kawashima Y. Mucoadhesive properties of carbopol or chitosan-coated liposomes and their effectiveness in the oral administration of calcitonin to rats. J Control Release 2003, 86:235-242.
    • (2003) J Control Release , vol.86 , pp. 235-242
    • Takeuchi, H.1    Matsui, Y.2    Yamamoto, H.3    Kawashima, Y.4
  • 25
    • 25144503019 scopus 로고    scopus 로고
    • Keynote review: intestinal Peyer's patch M cells and oral vaccine targeting
    • Brayden D.J., Jepson M.A., Baird A.W. Keynote review: intestinal Peyer's patch M cells and oral vaccine targeting. Drug Discov Today 2005, 10:1145-1157.
    • (2005) Drug Discov Today , vol.10 , pp. 1145-1157
    • Brayden, D.J.1    Jepson, M.A.2    Baird, A.W.3
  • 26
    • 23244464797 scopus 로고    scopus 로고
    • Poly (lactide-co-glycolide) particles of different physicochemical properties and their uptake by peyer's patches in mice
    • Shakweh M., Besnard M., Nicolas V., Fattal E. Poly (lactide-co-glycolide) particles of different physicochemical properties and their uptake by peyer's patches in mice. Eur J Pharm Biopharm 2005, 61:1-13.
    • (2005) Eur J Pharm Biopharm , vol.61 , pp. 1-13
    • Shakweh, M.1    Besnard, M.2    Nicolas, V.3    Fattal, E.4
  • 27
    • 0031469673 scopus 로고    scopus 로고
    • The mechanism of uptake of biodegradable microparticles in Caco-2 cells is size dependent
    • Desai M.P., Labhasetwar V., Walter E., Levy R.J., Amidon G.L. The mechanism of uptake of biodegradable microparticles in Caco-2 cells is size dependent. Pharm Res 1997, 14:1568-1573.
    • (1997) Pharm Res , vol.14 , pp. 1568-1573
    • Desai, M.P.1    Labhasetwar, V.2    Walter, E.3    Levy, R.J.4    Amidon, G.L.5
  • 28
    • 33645795045 scopus 로고    scopus 로고
    • New loading process and release properties of insulin from polysaccharide microcapsules fabricated through layer-by-layer assembly
    • Ye S., Wang C., Liu X., Tong Z., Ren B., Zeng F. New loading process and release properties of insulin from polysaccharide microcapsules fabricated through layer-by-layer assembly. J Control Release 2006, 112:79-87.
    • (2006) J Control Release , vol.112 , pp. 79-87
    • Ye, S.1    Wang, C.2    Liu, X.3    Tong, Z.4    Ren, B.5    Zeng, F.6
  • 29
    • 0033849510 scopus 로고    scopus 로고
    • Preparation of biodegradable insulin nanocapsules from biocompatible microemulsions
    • Watnasirichaikul S., Davies N.M., Rades T., Tucker I.G. Preparation of biodegradable insulin nanocapsules from biocompatible microemulsions. Pharm Res 2000, 17:684-689.
    • (2000) Pharm Res , vol.17 , pp. 684-689
    • Watnasirichaikul, S.1    Davies, N.M.2    Rades, T.3    Tucker, I.G.4
  • 30
    • 33644612270 scopus 로고    scopus 로고
    • Preparation and improvement of release behavior of chitosan microspheres containing insulin
    • Wang L.Y., Gu Y.H., Su Z.G., Ma G.H. Preparation and improvement of release behavior of chitosan microspheres containing insulin. Int J Pharm 2006, 311:187-195.
    • (2006) Int J Pharm , vol.311 , pp. 187-195
    • Wang, L.Y.1    Gu, Y.H.2    Su, Z.G.3    Ma, G.H.4
  • 31
    • 18044366409 scopus 로고    scopus 로고
    • A comparative study of the potential of solid triglyceride nanostructures coated with chitosan or poly(ethylene glycol) as carriers for oral calcitonin delivery
    • Garcia-fuentes M., Prego C., Torres D., Alonso M.J. A comparative study of the potential of solid triglyceride nanostructures coated with chitosan or poly(ethylene glycol) as carriers for oral calcitonin delivery. Eur J Pharm Sci 2005, 25:133-143.
    • (2005) Eur J Pharm Sci , vol.25 , pp. 133-143
    • Garcia-fuentes, M.1    Prego, C.2    Torres, D.3    Alonso, M.J.4
  • 32
    • 0036804013 scopus 로고    scopus 로고
    • Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms
    • Futaki S. Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms. Int J Pharm 2002, 245:1-7.
    • (2002) Int J Pharm , vol.245 , pp. 1-7
    • Futaki, S.1
  • 33
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki S., Suzuki T., Ohashi W., Yagami T., Tanaka S., Ueda K., Sugiura Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J Biol Chem 2001, 276:5836-5840.
    • (2001) J Biol Chem , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 34
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D., Joliot A.H., Chassaing G., Prochiantz A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J Biol Chem 1994, 269:10444-10450.
    • (1994) J Biol Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 35
    • 38949188925 scopus 로고    scopus 로고
    • Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides
    • Nakase I., Takeuchi T., Tanaka G., Futaki S. Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides. Adv Drug Deliv Rev 2008, 60:598-607.
    • (2008) Adv Drug Deliv Rev , vol.60 , pp. 598-607
    • Nakase, I.1    Takeuchi, T.2    Tanaka, G.3    Futaki, S.4
  • 36
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • Mitchell D.J., Kim D.T., Steinman L., Fathman C.G., Rothbard J.B. Polyarginine enters cells more efficiently than other polycationic homopolymers. J Pept Res 2000, 56:318-325.
    • (2000) J Pept Res , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 37
    • 27744525788 scopus 로고    scopus 로고
    • Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery
    • Massodi I., Bidwell G.L., Raucher D. Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery. J Control Release 2005, 108:396-408.
    • (2005) J Control Release , vol.108 , pp. 396-408
    • Massodi, I.1    Bidwell, G.L.2    Raucher, D.3
  • 38
    • 28444435477 scopus 로고    scopus 로고
    • Nano-carriers for DNA delivery to the lung based upon a TAT-derived peptide covalently coupled to PEG-PEI
    • Kleemann E., Neu M., Jekel N., Fink L., Schmehl T., Gessler T., Seeger W., et al. Nano-carriers for DNA delivery to the lung based upon a TAT-derived peptide covalently coupled to PEG-PEI. J Control Release 2005, 109:299-316.
    • (2005) J Control Release , vol.109 , pp. 299-316
    • Kleemann, E.1    Neu, M.2    Jekel, N.3    Fink, L.4    Schmehl, T.5    Gessler, T.6    Seeger, W.7
  • 39
    • 34548183128 scopus 로고    scopus 로고
    • Assessing the delivery efficacy and internalization route of cell-penetrating peptides
    • El-Andaloussi S., Guterstam P., Langel ü. Assessing the delivery efficacy and internalization route of cell-penetrating peptides. Nat Protoc 2007, 2:2043-2047.
    • (2007) Nat Protoc , vol.2 , pp. 2043-2047
    • El-Andaloussi, S.1    Guterstam, P.2    Langel, Ü.3
  • 41
    • 34249820576 scopus 로고    scopus 로고
    • Multifunctional nanocarriers
    • Torchilin V.P. Multifunctional nanocarriers. Adv Drug Deliv Rev 2006, 58:1532-1555.
    • (2006) Adv Drug Deliv Rev , vol.58 , pp. 1532-1555
    • Torchilin, V.P.1
  • 42
    • 33847281527 scopus 로고    scopus 로고
    • A novel approach using functional peptides for efficient intestinal absorption of insulin
    • Morishita M., Kamei N., Ehara J., Isowa K., Takayama K. A novel approach using functional peptides for efficient intestinal absorption of insulin. J Control Release 2007, 118:177-184.
    • (2007) J Control Release , vol.118 , pp. 177-184
    • Morishita, M.1    Kamei, N.2    Ehara, J.3    Isowa, K.4    Takayama, K.5
  • 43
    • 54849439914 scopus 로고    scopus 로고
    • Usefulness of cell-penetrating peptides to improve intestinal insulin absorption
    • Kamei N., Morishita M., Eda Y., Ida N., Nishio R., Takayama K. Usefulness of cell-penetrating peptides to improve intestinal insulin absorption. J Control Release 2008, 132:21-25.
    • (2008) J Control Release , vol.132 , pp. 21-25
    • Kamei, N.1    Morishita, M.2    Eda, Y.3    Ida, N.4    Nishio, R.5    Takayama, K.6
  • 44
    • 70349198899 scopus 로고    scopus 로고
    • Efficiency of cell-penetrating peptides on the nasal and intestinal absorption of therapeutic peptides and proteins
    • El-S Khafagy, Morishita M., Kamei N., Eda Y., Ikeno Y., Takayama K. Efficiency of cell-penetrating peptides on the nasal and intestinal absorption of therapeutic peptides and proteins. Int J Pharm 2009, 381:49-55.
    • (2009) Int J Pharm , vol.381 , pp. 49-55
    • El-S, K.1    Morishita, M.2    Kamei, N.3    Eda, Y.4    Ikeno, Y.5    Takayama, K.6
  • 45
    • 57349182296 scopus 로고    scopus 로고
    • Effect of c ell-penetrating peptides on the nasal absorption of insulin
    • El-S Khafagy, Morishita M., Isowa K., Imai J., Takayama K. Effect of c ell-penetrating peptides on the nasal absorption of insulin. J Control Release 2009, 133:103-108.
    • (2009) J Control Release , vol.133 , pp. 103-108
    • El-S, K.1    Morishita, M.2    Isowa, K.3    Imai, J.4    Takayama, K.5
  • 46
    • 53049085052 scopus 로고    scopus 로고
    • Permeation characteristics of oligoarginine through intestinal epithelium and its usefulness for intestinal peptide drug delivery
    • Kamei N., Morishita M., Ehara J., Takayama K. Permeation characteristics of oligoarginine through intestinal epithelium and its usefulness for intestinal peptide drug delivery. J Control Release 2008, 131:94-99.
    • (2008) J Control Release , vol.131 , pp. 94-99
    • Kamei, N.1    Morishita, M.2    Ehara, J.3    Takayama, K.4
  • 47
    • 67349268446 scopus 로고    scopus 로고
    • Importance of intermolecualr interaction on the improvement of intestinal therapeutic peptide/protein absorption using cell-penetrating peptides
    • Kamei N., Morishita M., Takayama K. Importance of intermolecualr interaction on the improvement of intestinal therapeutic peptide/protein absorption using cell-penetrating peptides. J Control Release 2009, 136:179-186.
    • (2009) J Control Release , vol.136 , pp. 179-186
    • Kamei, N.1    Morishita, M.2    Takayama, K.3
  • 48
    • 76549110719 scopus 로고    scopus 로고
    • The role of intermolecular interactions with penetratin and its analogue on the enhancement of absorption of nasal therapeutic peptides
    • El-S Khafagy, Morishita M., Takayama K. The role of intermolecular interactions with penetratin and its analogue on the enhancement of absorption of nasal therapeutic peptides. Int J Pharm 2010, 388:209-212.
    • (2010) Int J Pharm , vol.388 , pp. 209-212
    • El-S, K.1    Morishita, M.2    Takayama, K.3
  • 50
    • 33845694498 scopus 로고    scopus 로고
    • Macropinocytosis: regulated coordination of endocytic and exocytic membrane traffic events
    • Falcone S., Cocucci E., Podini P., Kirchhausen T., Clementi E., Meldolesi J. Macropinocytosis: regulated coordination of endocytic and exocytic membrane traffic events. J Cell Sci 2006, 119:4758-4769.
    • (2006) J Cell Sci , vol.119 , pp. 4758-4769
    • Falcone, S.1    Cocucci, E.2    Podini, P.3    Kirchhausen, T.4    Clementi, E.5    Meldolesi, J.6
  • 52
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • Kaplan I.M., Wadia J.S., Dowdy S.F. Cationic TAT peptide transduction domain enters cells by macropinocytosis. J Control Release 2005, 102:247-253.
    • (2005) J Control Release , vol.102 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 53
    • 59849107620 scopus 로고    scopus 로고
    • FDG-microPET and diffusion-weighted MR image evaluation of early changes after radiofrequency ablation in implanted VX2 tumors in rabbits
    • Ohira T., Okuma T., Matsuoka T., Wada Y., Nakamura K., Watanabe Y., Inoue Y. FDG-microPET and diffusion-weighted MR image evaluation of early changes after radiofrequency ablation in implanted VX2 tumors in rabbits. Cardiovasc Interv Radiol 2009, 32:114-120.
    • (2009) Cardiovasc Interv Radiol , vol.32 , pp. 114-120
    • Ohira, T.1    Okuma, T.2    Matsuoka, T.3    Wada, Y.4    Nakamura, K.5    Watanabe, Y.6    Inoue, Y.7
  • 54
    • 33749061965 scopus 로고    scopus 로고
    • 18F-FDG small-animal PET for monitoring the therapeutic effect of CT-guided radiofrequency ablation on implanted VX2 lung tumors in rabbits
    • Okuma T., Matsuoka T., Okamura T., Wada Y., Yamamoto A., Oyama Y., Koyama K., et al. 18F-FDG small-animal PET for monitoring the therapeutic effect of CT-guided radiofrequency ablation on implanted VX2 lung tumors in rabbits. J Nucl Med 2006, 47:1351-1358.
    • (2006) J Nucl Med , vol.47 , pp. 1351-1358
    • Okuma, T.1    Matsuoka, T.2    Okamura, T.3    Wada, Y.4    Yamamoto, A.5    Oyama, Y.6    Koyama, K.7
  • 55
    • 77955269563 scopus 로고    scopus 로고
    • Molecular imaging analysis of intestinal insulin absorption boosted by cell-penetrating peptides by using positron emission tomography
    • Kamei N., Morishita M., Kanayama Y., Hasegawa K., Nishimura M., Hayashinaka E., Wada Y., et al. Molecular imaging analysis of intestinal insulin absorption boosted by cell-penetrating peptides by using positron emission tomography. J Control Release 2010, 146:16-22.
    • (2010) J Control Release , vol.146 , pp. 16-22
    • Kamei, N.1    Morishita, M.2    Kanayama, Y.3    Hasegawa, K.4    Nishimura, M.5    Hayashinaka, E.6    Wada, Y.7


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