메뉴 건너뛰기




Volumn 8, Issue 2, 2012, Pages 636-645

Engineered peptides with enzymatically cleavable domains for controlling the release of model protein drug from "soft" nanoparticles

Author keywords

BSA; Coacervation; Controlled release strategy; Engineered peptide; MMP 2

Indexed keywords

AMINO ACIDS; BODY FLUIDS; MOLECULES; NANOPARTICLES; PEPTIDES; PROTECTIVE COATINGS; TARGETED DRUG DELIVERY; TISSUE;

EID: 84855449010     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2011.10.028     Document Type: Article
Times cited : (8)

References (18)
  • 1
    • 33750965495 scopus 로고    scopus 로고
    • Production of biological nanoparticles from bovine serum albumin for drug delivery
    • M. Rahimnejad, M. Jahanshahi, and G.D. Najafpour Production of biological nanoparticles from bovine serum albumin for drug delivery Afr J Biotechnol 5 2006 1918 1923 (Pubitemid 44736967)
    • (2006) African Journal of Biotechnology , vol.5 , Issue.20 , pp. 1918-1923
    • Rahimnejad, M.1    Jahanshahi, M.2    Najafpour, G.D.3
  • 2
    • 0032120879 scopus 로고    scopus 로고
    • Anatomy of a coacervate
    • Fredric M. Menger, and Bridget M. Sykes Anatomy of a coacervate Langmuir 14 1998 4131 4137 (Pubitemid 128624876)
    • (1998) Langmuir , vol.14 , Issue.15 , pp. 4131-4137
    • Menger, F.M.1    Sykes, B.M.2
  • 3
    • 57149125027 scopus 로고    scopus 로고
    • Preparation of BMP-2 containing bovine serum albumin (BSA) nanoparticles stabilized by polymer coating
    • Guilin Wang, Kevin Siggers, Sufeng Zhang, Hongxing Jiang, Zhenge Xu, Ronald F. Zernicke, et al. Preparation of BMP-2 containing bovine serum albumin (BSA) nanoparticles stabilized by polymer coating. Pharm Res 2008;25:2896-09.
    • (2008) Pharm Res , vol.25 , pp. 2896-2909
    • Wang, G.1    Siggers, K.2    Zhang, S.3    Jiang, H.4    Xu, Z.5    Zernicke, R.F.6
  • 4
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinase
    • H. Nagase, and F. Woessner Matrix metalloproteinase J Biol Chem 274 1999 21491 21494
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, F.2
  • 6
    • 77951927330 scopus 로고    scopus 로고
    • Plasma matrix metalloproteinase-2 and 9 levels are elevated in patients with acute coronary syndrome and coronary chronic total occlusion
    • Q.D. Tang, P.S. Wu, Y.Q. Hou, Z. Huang, Z.J. Zhou, and Z.G. Guo Plasma matrix metalloproteinase-2 and 9 levels are elevated in patients with acute coronary syndrome and coronary chronic total occlusion J Southern Med Univ 29 2009 1004 1007
    • (2009) J Southern Med Univ , vol.29 , pp. 1004-1007
    • Tang, Q.D.1    Wu, P.S.2    Hou, Y.Q.3    Huang, Z.4    Zhou, Z.J.5    Guo, Z.G.6
  • 7
    • 34948852291 scopus 로고    scopus 로고
    • Acute actions and novel targets of matrix metalloproteinases in the heart and vasculature
    • DOI 10.1038/sj.bjp.0707344, PII 0707344
    • A.K. Chow, J. Cena, and R. Schulz Acute actions and novel targets of matrix metalloproteinase in the heart and vasculature Br J Pharmacol 152 2007 189 205 (Pubitemid 47517601)
    • (2007) British Journal of Pharmacology , vol.152 , Issue.2 , pp. 189-205
    • Chow, A.K.1    Cena, J.2    Schulz, R.3
  • 8
    • 2442462505 scopus 로고    scopus 로고
    • The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia
    • DOI 10.1016/j.critrevonc.2003.09.001, PII S1040842803002270
    • G. Klein, E. Vellenga, M.W. Fraaije, W.A. Kamps, and E.S.J.M. de Bont The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia Crit Rev Oncol Hemat 50 2004 87 100 (Pubitemid 38638736)
    • (2004) Critical Reviews in Oncology/Hematology , vol.50 , Issue.2 , pp. 87-100
    • Klein, G.1    Vellenga, E.2    Fraaije, M.W.3    Kamps, W.A.4    De Bont, E.S.J.M.5
  • 9
    • 0033061405 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors
    • A. Kugler Matrix metalloproteinases and their inhibitors Anticancer Res 19 1999 1589 1592 (Pubitemid 29255653)
    • (1999) Anticancer Research , vol.19 , Issue.C , pp. 1589-1592
    • Kugler, A.1
  • 10
    • 0347475762 scopus 로고    scopus 로고
    • A matrixmetalloproteinase 2 cleavable melittin/avidin conjugate specifically targets tumor cells in vitro and in vivo
    • Wendy Song, Lori Holle, Eric Holle, Yanzhang Wei, Thomas Wagner, Xianzhong Yu. A matrixmetalloproteinase 2 cleavable melittin/avidin conjugate specifically targets tumor cells in vitro and in vivo. Int J Oncol 2003;22:93-98.
    • (2003) Int J Oncol , vol.22 , pp. 93-98
    • Song, W.1    Holle, L.2    Holle, E.3    Wei, Y.4    Wagner, T.5    Yu, X.6
  • 11
    • 0027257103 scopus 로고
    • Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin)
    • Sarah Netzel-Arnett, Qing-Xiang Sang, William G.I. Moore, Marc Navre, Henning Birkedal-Hansen, Harold E, et al. Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin), Biochemistry 1993;32:6427-32. (Pubitemid 23208826)
    • (1993) Biochemistry , vol.32 , Issue.25 , pp. 6427-6432
    • Netzel-Arnett, S.1    Sang, Q.-X.2    Moore, W.G.I.3    Navre, M.4    Birkedal-Hansen, H.5    Van Wart, H.E.6
  • 12
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • DOI 10.1038/90273
    • Benjamin E. Turk, Lisa L. Huang, Elizabeth T. Piro, Lewis C. Cantley. Determination of protease cleavage site motifs using mixture-based oriented peptide libraries, Nat Biotechnol 2001;19:661-67. (Pubitemid 32625438)
    • (2001) Nature Biotechnology , vol.19 , Issue.7 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 13
    • 59449110643 scopus 로고    scopus 로고
    • Inhibition of tumor-cell invasion with chlorotoxin-bound superparamagnetic nanoparticles
    • Omid Veiseh, Jonathan W. Gunn, Forrest M. Kievit, Conroy Sun, Chen Fang, Jerry S.H. Lee, et al. Inhibition of tumor-cell invasion with chlorotoxin-bound superparamagnetic nanoparticles, Small 2008;5:256-64.
    • (2008) Small , vol.5 , pp. 256-264
    • Veiseh, O.1    Gunn, J.W.2    Kievit, F.M.3    Sun, C.4    Fang, C.5    Lee, J.S.H.6
  • 14
    • 84855426699 scopus 로고    scopus 로고
    • Tumor protease triggers self assembly: Nanoparticles
    • Paula Gould. Tumor protease triggers self assembly: nanoparticles. Nanotoday 2006;1:15.
    • (2006) Nanotoday , vol.1 , pp. 15
    • Gould, P.1
  • 15
    • 77956899980 scopus 로고    scopus 로고
    • Poly-L-lysine-coated albumin nanoparticles: Stability, mechanism for increasing in vitro enzymatic resilience, and siRNA release characteristics
    • H.D. Singh, G. Wang, H. Uluda, and L.D. Unsworth Poly-L-lysine-coated albumin nanoparticles: stability, mechanism for increasing in vitro enzymatic resilience, and siRNA release characteristics Acta Biomater 6 2010 4277 4284
    • (2010) Acta Biomater , vol.6 , pp. 4277-4284
    • Singh, H.D.1    Wang, G.2    Uluda, H.3    Unsworth, L.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.