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Volumn 21, Issue 2, 2015, Pages 77-84

Peptide internalization enabled by folding: Triple helical cell-penetrating peptides

Author keywords

Cell penetrating peptides; Collagen peptides; Enzymatic degradation; Internalization; Intracellular delivery; Triple helix

Indexed keywords

CELL PENETRATING PEPTIDE; GLYCINE; HYDROXYPROLINE; PROLINE;

EID: 84921822526     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2725     Document Type: Article
Times cited : (30)

References (35)
  • 2
    • 79959487372 scopus 로고    scopus 로고
    • Tailoring nanocarriers for intracellular protein delivery
    • Gu Z, Biswas A, ZhaoabM, Tang Y. Tailoring nanocarriers for intracellular protein delivery. Chem. Soc. Rev. 2011; 40: 3638-3655.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 3638-3655
    • Gu, Z.1    Biswas, A.2    Zhaoab, M.3    Tang, Y.4
  • 3
    • 77954645526 scopus 로고    scopus 로고
    • The use of nanocarriers for drug delivery in cancer therapy
    • Khan DR. The use of nanocarriers for drug delivery in cancer therapy. J. Cancer Sci. & Therapy 2010; 2: 58-62.
    • (2010) J. Cancer Sci. & Therapy , vol.2 , pp. 58-62
    • Khan, D.R.1
  • 5
    • 84889970066 scopus 로고    scopus 로고
    • Recent progress of cell-penetrating peptides as new carriers for intracellular cargo delivery
    • Wang F, Wanga Y, Zhanga X, Zhanga W, Guo S, Jin F. Recent progress of cell-penetrating peptides as new carriers for intracellular cargo delivery. J. Controlled Release. 2014; 174: 126-136.
    • (2014) J. Controlled Release. , vol.174 , pp. 126-136
    • Wang, F.1    Wanga, Y.2    Zhanga, X.3    Zhanga, W.4    Guo, S.5    Jin, F.6
  • 7
    • 13844298046 scopus 로고    scopus 로고
    • Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides
    • Gupta B, Levchenko TS, Torchilin VP. Intracellular delivery of large molecules and small particles by cell-penetrating proteins and peptides. Adv. Drug Deliv. Rev. 2005; 57: 637-651.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 637-651
    • Gupta, B.1    Levchenko, T.S.2    Torchilin, V.P.3
  • 8
    • 84908274199 scopus 로고    scopus 로고
    • Cell penetration: Scope and limitations by the application of cell-penetrating peptides
    • Reissmann S. Cell penetration: scope and limitations by the application of cell-penetrating peptides. J. Pept. Sci. 2014; 20: 760-784.
    • (2014) J. Pept. Sci. , vol.20 , pp. 760-784
    • Reissmann, S.1
  • 9
    • 58249095956 scopus 로고    scopus 로고
    • The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake
    • Palm-Apergi C, Lorents A, Padari K, Pooga M, Hallbrink M. The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake. FASEB J. 2009; 23: 214-223.
    • (2009) FASEB J. , vol.23 , pp. 214-223
    • Palm-Apergi, C.1    Lorents, A.2    Padari, K.3    Pooga, M.4    Hallbrink, M.5
  • 10
    • 79651474350 scopus 로고    scopus 로고
    • Biological responses towards cationic peptides and drug carriers
    • Verdurmen WP, Brock R. Biological responses towards cationic peptides and drug carriers. Trends Pharmacol. Sci. 2011; 32: 116-124.
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 116-124
    • Verdurmen, W.P.1    Brock, R.2
  • 12
    • 23944492106 scopus 로고    scopus 로고
    • Cell-penetrating agents based on a polyproline helix scaffolds
    • Fillon YA, Anderson JP, Chmielewski J. Cell-penetrating agents based on a polyproline helix scaffolds. J. Am. Chem. Soc. 2005; 127: 11798-11799.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11798-11799
    • Fillon, Y.A.1    Anderson, J.P.2    Chmielewski, J.3
  • 13
    • 84921710389 scopus 로고    scopus 로고
    • Proline-rich, amphipathic cell-penetrating peptides
    • Pujals S, Giralt E. Proline-rich, amphipathic cell-penetrating peptides. Adv. Drug Delivery Rev. 2003; 55: 1679-1684.
    • (2003) Adv. Drug Delivery Rev. , vol.55 , pp. 1679-1684
    • Pujals, S.1    Giralt, E.2
  • 14
    • 58149101572 scopus 로고    scopus 로고
    • Cationic amphiphilic polyproline helices: Sidechain variations and cell-specific internalization
    • Geisler I, Chmielewski J. Cationic amphiphilic polyproline helices: sidechain variations and cell-specific internalization. Chem. Biol. Drugs Des. 2009; 73: 39-45.
    • (2009) Chem. Biol. Drugs Des. , vol.73 , pp. 39-45
    • Geisler, I.1    Chmielewski, J.2
  • 16
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cellpenetrating peptides for medical and biological applications
    • Fonseca SB, Pereira MP, Kelley SO. Recent advances in the use of cellpenetrating peptides for medical and biological applications. Adv. Drug Deliv. Rev. 2009; 61: 953-964.
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 18
  • 19
    • 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
  • 20
    • 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
  • 21
    • 84859483195 scopus 로고    scopus 로고
    • Peptides in cancer nanomedicine: Drug carriers, targeting ligands and protease substrates
    • Zhang XX, Eden HS, Chen X. Peptides in cancer nanomedicine: drug carriers, targeting ligands and protease substrates. J. Controlled Release 2012; 159: 2-13.
    • (2012) J. Controlled Release , vol.159 , pp. 2-13
    • Zhang, X.X.1    Eden, H.S.2    Chen, X.3
  • 22
    • 54849425126 scopus 로고    scopus 로고
    • Discovering and improving novel peptide therapeutics
    • McGregor DP. Discovering and improving novel peptide therapeutics. Curr. Opin. Pharm. 2008; 8: 616-619.
    • (2008) Curr. Opin. Pharm. , vol.8 , pp. 616-619
    • McGregor, D.P.1
  • 23
    • 33745107170 scopus 로고    scopus 로고
    • Strategies to improve plasma half life time of peptide and protein drugs
    • Werle M, Bernkop-Schnurch A. Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids 2006; 30: 351-367.
    • (2006) Amino Acids , vol.30 , pp. 351-367
    • Werle, M.1    Bernkop-Schnurch, A.2
  • 25
    • 0027996196 scopus 로고
    • Crystal structure andmolecular structure of a collagen-likepeptideat1.9angstromresolution
    • Bella J, Eaton M, Brodsky B. Crystal structure andmolecular structure of a collagen-likepeptideat1.9angstromresolution. Science 1994;266:74-81.
    • (1994) Science , vol.266 , pp. 74-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3
  • 26
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • Persikov AV, Ramshaw JAM, Brodsky B. Prediction of collagen stability from amino acid sequence. J. Biol. Chem. 2005; 280: 19343-19349.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 28
    • 80052534021 scopus 로고    scopus 로고
    • Collagen mimetic peptides: Progress towards functional applications
    • Yu SM, Li Y, Kim D. Collagen mimetic peptides: progress towards functional applications. Soft Matter 2011; 7: 7927-7938.
    • (2011) Soft Matter , vol.7 , pp. 7927-7938
    • Yu, S.M.1    Li, Y.2    Kim, D.3
  • 30
    • 84859226512 scopus 로고    scopus 로고
    • Self-assembly of collagen peptides into hollow microtubules
    • Reimer AE, Feher K, Hernandez D, Slowinska K. Self-assembly of collagen peptides into hollow microtubules. J. Mater. Chem. 2012; 22: 7701-7703.
    • (2012) J. Mater. Chem. , vol.22 , pp. 7701-7703
    • Reimer, A.E.1    Feher, K.2    Hernandez, D.3    Slowinska, K.4
  • 31
    • 33646164199 scopus 로고    scopus 로고
    • Electrochemical Time-of-Flight in crosslinked collagen matrix solution: Implications of structural changes for drug delivery systems
    • Ky D, Liu CK, Marumoto C, Castaneda L, Slowinska K. Electrochemical Time-of-Flight in crosslinked collagen matrix solution: implications of structural changes for drug delivery systems. J. Controlled Release 2006; 112: 214-222.
    • (2006) J. Controlled Release , vol.112 , pp. 214-222
    • Ky, D.1    Liu, C.K.2    Marumoto, C.3    Castaneda, L.4    Slowinska, K.5
  • 32
    • 22444439952 scopus 로고    scopus 로고
    • Polyarginine as a multifunctional fusion tag
    • Fuchs SM, Raines RT. Polyarginine as a multifunctional fusion tag. Protein Sci. 2005; 14: 1538-1544.
    • (2005) Protein Sci. , vol.14 , pp. 1538-1544
    • Fuchs, S.M.1    Raines, R.T.2
  • 33
    • 0344012169 scopus 로고    scopus 로고
    • Anion-mediated transfer of polyarginine across liquid and bilayer membranes
    • Sakai N, Matile S. Anion-mediated transfer of polyarginine across liquid and bilayer membranes. J. Am. Chem. Soc. 2003; 125: 14348-14356.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14348-14356
    • Sakai, N.1    Matile, S.2
  • 34
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • El-Sayed A, Futaki S, Harashima H. Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment. AAPS J. 2009; 11: 13-22.
    • (2009) AAPS J. , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 35
    • 84856713125 scopus 로고    scopus 로고
    • Folding delay and structural perturbations caused by type IV collagen natural interruptions and nearby Gly missense mutations
    • Hwang E, Brodsky B. Folding delay and structural perturbations caused by type IV collagen natural interruptions and nearby Gly missense mutations. J. Biol. Chem. 2012; 287: 4368-4375.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4368-4375
    • Hwang, E.1    Brodsky, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.