메뉴 건너뛰기




Volumn 501, Issue 1-2, 2016, Pages 32-38

pH-responsive PepFect cell-penetrating peptides

Author keywords

Calcein leakage; Cell penetrating peptide; Cellular uptake; Oligonucleotide delivery; PepFect; pH responsive

Indexed keywords

ANTINEOPLASTIC AGENT; CELL PENETRATING PEPTIDE; PEPFECT 131; PEPFECT 132; PEPFECT 133; PEPFECT 14; PEPFECT 141; PEPFECT 142; PEPFECT 143; PEPFECT 3; PEPFECT DERIVATIVE; UNCLASSIFIED DRUG; HISTIDINE; LIPOPEPTIDE; OLIGONUCLEOTIDE;

EID: 84957794364     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2016.01.055     Document Type: Article
Times cited : (28)

References (21)
  • 1
    • 84855457273 scopus 로고    scopus 로고
    • Hydrogen-bond energetics drive helix formation in membrane interfaces
    • P.F. Almeida, A.S. Ladokhin, and S.H. White Hydrogen-bond energetics drive helix formation in membrane interfaces Biochim. Biophys. Acta-Biomembr. 1818 2012 178 182 10.1016/j.bbamem.2011.07.019
    • (2012) Biochim. Biophys. Acta-Biomembr. , vol.1818 , pp. 178-182
    • Almeida, P.F.1    Ladokhin, A.S.2    White, S.H.3
  • 2
    • 0024039744 scopus 로고
    • Mechanism of fluorescence concentration quenching of carboxyfluorescein in liposomes: energy transfer to nonfluorescent dimers
    • R.F. Chen, and J.R. Knutson Mechanism of fluorescence concentration quenching of carboxyfluorescein in liposomes: energy transfer to nonfluorescent dimers Anal. Biochem. 172 1988 61 77 10.1016/0003-2697(88) 90412-5
    • (1988) Anal. Biochem. , vol.172 , pp. 61-77
    • Chen, R.F.1    Knutson, J.R.2
  • 3
    • 84922765691 scopus 로고    scopus 로고
    • Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA
    • D. Chu, W. Xu, R. Pan, Y. Ding, W. Sui, and P. Chen Rational modification of oligoarginine for highly efficient siRNA delivery: structure-activity relationship and mechanism of intracellular trafficking of siRNA Nanomed. Nanotechnol. Biol. Med. 11 2015 435 446 10.1016/j.nano.2014.08.007
    • (2015) Nanomed. Nanotechnol. Biol. Med. , vol.11 , pp. 435-446
    • Chu, D.1    Xu, W.2    Pan, R.3    Ding, Y.4    Sui, W.5    Chen, P.6
  • 4
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • D. Derossi, a.H. Joliot, G. Chassaing, and a. Prochiantz The third helix of the Antennapedia homeodomain translocates through biological membranes J. Biol. Chem. 269 1994 10444 10450
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 10
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell penetrating peptides: from molecular mechanisms to therapeutics
    • F. Heitz Twenty years of cell penetrating peptides: from molecular mechanisms to therapeutics Br. J. Pharmacol. 2009 195 206 10.1111/j.1476-5381.2008.00057.x
    • (2009) Br. J. Pharmacol. , pp. 195-206
    • Heitz, F.1
  • 13
    • 40649085520 scopus 로고    scopus 로고
    • An endosomolytic Tat peptide produced by incorporation of histidine and cysteine residues as a nonviral vector for DNA transfection
    • S.L. Lo, and S. Wang An endosomolytic Tat peptide produced by incorporation of histidine and cysteine residues as a nonviral vector for DNA transfection Biomaterials 29 2008 2408 2414 10.1016/j.biomaterials.2008.01.031
    • (2008) Biomaterials , vol.29 , pp. 2408-2414
    • Lo, S.L.1    Wang, S.2
  • 18
    • 84907829502 scopus 로고    scopus 로고
    • Effects of cargo molecules on membrane perturbation caused by transportan10 based cell-penetrating peptides
    • L. Vasconcelos, F. Madani, P. Arukuusk, L. Pärnaste, A. Gräslund, and Ü. Langel Effects of cargo molecules on membrane perturbation caused by transportan10 based cell-penetrating peptides Biochim. Biophys. Acta-Biomembr. 1838 2014 3118 3129 10.1016/j.bbamem.2014.08.011
    • (2014) Biochim. Biophys. Acta-Biomembr. , vol.1838 , pp. 3118-3129
    • Vasconcelos, L.1    Madani, F.2    Arukuusk, P.3    Pärnaste, L.4    Gräslund, A.5    Langel, Ü.6
  • 19
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • E. Vivès, P. Brodin, and B. Lebleu A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus J. Biol. Chem. 272 1997 16010 16017
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 20
    • 68049089697 scopus 로고    scopus 로고
    • Wasp mastoparans follow the same mechanism as the cell-penetrating peptide transportan 10
    • L.E. Yandek, A. Pokorny, and P.F.F. Almeida Wasp mastoparans follow the same mechanism as the cell-penetrating peptide transportan 10 Biochemistry 48 2009 7342 7351 10.1021/bi9008243
    • (2009) Biochemistry , vol.48 , pp. 7342-7351
    • Yandek, L.E.1    Pokorny, A.2    Almeida, P.F.F.3
  • 21
    • 13844254266 scopus 로고    scopus 로고
    • Cell-penetrating peptides: mechanism and kinetics of cargo delivery
    • M. Zorko, and Ü. Langel Cell-penetrating peptides: mechanism and kinetics of cargo delivery Adv. Drug Deliv. Rev. 57 2005 529 545 10.1016/j.addr.2004.10.010
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 529-545
    • Zorko, M.1    Langel, Ü.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.