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Volumn 33, Issue 33, 2012, Pages 8723-8732

Polycationic peptide guided spherical ordered self-assembly of biomacromolecules

Author keywords

Biomacromolecule; Controllable delivery; Interferon; Polycationic peptide; Self assembly

Indexed keywords

BIOLOGICAL POTENCY; BIOMACROMOLECULE; BIOMACROMOLECULES; BLOOD LEVELS; CONTROLLABLE DELIVERY; DISSOLUTION BEHAVIOR; DURATION TIME; IN-VITRO; MOLAR RATIO; MOLECULAR ENTITIES; MOLECULAR SELF ASSEMBLY; MOLECULAR SIMULATIONS; OPTIMAL REGIONS; ORDERED GROWTH; PHYSICO-CHEMICAL CHARACTERIZATION; POLYCATIONIC PEPTIDES; SEMICRYSTALLINES; THERAPEUTIC PROTEIN; THREE-DIMENSIONAL ORDERED STRUCTURES;

EID: 84866152212     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2012.08.037     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 0033987939 scopus 로고    scopus 로고
    • Protein stability in controlled-release systems
    • Fu K., Klibanov A.M., Langer R. Protein stability in controlled-release systems. Nat Biotechnol 2000, 18:24-25.
    • (2000) Nat Biotechnol , vol.18 , pp. 24-25
    • Fu, K.1    Klibanov, A.M.2    Langer, R.3
  • 2
    • 2642677624 scopus 로고    scopus 로고
    • Improving protein therapeutics with sustained-release formulations
    • Putney S.D., Burke P.A. Improving protein therapeutics with sustained-release formulations. Nat Biotechnol 1998, 16:153-157.
    • (1998) Nat Biotechnol , vol.16 , pp. 153-157
    • Putney, S.D.1    Burke, P.A.2
  • 3
    • 0038445582 scopus 로고    scopus 로고
    • Biodegradable microspheres for protein delivery
    • Sinha V.R., Trehan A. Biodegradable microspheres for protein delivery. J Control Release 2003, 90:261-280.
    • (2003) J Control Release , vol.90 , pp. 261-280
    • Sinha, V.R.1    Trehan, A.2
  • 4
    • 84859308209 scopus 로고    scopus 로고
    • Effect of PEGylation on protein hydrodynamics
    • Gokarn Y.R., McLean M., Laue T.M. Effect of PEGylation on protein hydrodynamics. Mol Pharm 2012, 9:762-773.
    • (2012) Mol Pharm , vol.9 , pp. 762-773
    • Gokarn, Y.R.1    McLean, M.2    Laue, T.M.3
  • 7
    • 0034750040 scopus 로고    scopus 로고
    • Diamonds in the rough: protein crystals from a formulation perspective
    • Jen A., Merkle H.P. Diamonds in the rough: protein crystals from a formulation perspective. Pharm Res 2001, 18:1483-1488.
    • (2001) Pharm Res , vol.18 , pp. 1483-1488
    • Jen, A.1    Merkle, H.P.2
  • 8
    • 34547099363 scopus 로고    scopus 로고
    • The interferons: 50 years after their discovery, there is much more to learn
    • Pestka S. The interferons: 50 years after their discovery, there is much more to learn. J Biol Chem 2007, 282:20047-20051.
    • (2007) J Biol Chem , vol.282 , pp. 20047-20051
    • Pestka, S.1
  • 9
    • 41949111630 scopus 로고    scopus 로고
    • Recent progress and future directions in protein-protein docking
    • Ritchie D.W. Recent progress and future directions in protein-protein docking. Curr Protein Pept Sci 2008, 9:1-15.
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 1-15
    • Ritchie, D.W.1
  • 10
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagopal K., Schneider J.P. Self-assembling peptides and proteins for nanotechnological applications. Curr Opin Struct Biol 2004, 14:480-486.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 11
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat Biotechnol 2003, 21:1171-1178.
    • (2003) Nat Biotechnol , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 12
    • 33646193273 scopus 로고    scopus 로고
    • Optical microscopy of growing insulin amyloid spherulites on surfaces in vitro
    • Rogers S.S., Krebs M.R., Bromley E.H., van der Linden E., Donald A.M. Optical microscopy of growing insulin amyloid spherulites on surfaces in vitro. Biophys J 2006, 90:1043-1054.
    • (2006) Biophys J , vol.90 , pp. 1043-1054
    • Rogers, S.S.1    Krebs, M.R.2    Bromley, E.H.3    van der Linden, E.4    Donald, A.M.5
  • 13
    • 0018803382 scopus 로고
    • Sequence divergence of rainbow trout protamine mRNAs; comparison of coding and non-coding nucleotide sequences in three protamine cDNA plasmids
    • Jenkins J.R. Sequence divergence of rainbow trout protamine mRNAs; comparison of coding and non-coding nucleotide sequences in three protamine cDNA plasmids. Nature 1979, 279:809-811.
    • (1979) Nature , vol.279 , pp. 809-811
    • Jenkins, J.R.1
  • 14
    • 0035042430 scopus 로고    scopus 로고
    • Packaging paternal chromosomes with protamine
    • Braun R.E. Packaging paternal chromosomes with protamine. Nat Genet 2001, 28:10-12.
    • (2001) Nat Genet , vol.28 , pp. 10-12
    • Braun, R.E.1
  • 15
    • 0033301681 scopus 로고    scopus 로고
    • New strategies for protein crystal growth
    • Wiencek J.M. New strategies for protein crystal growth. Annu Rev Biomed Eng 1999, 1:505-534.
    • (1999) Annu Rev Biomed Eng , vol.1 , pp. 505-534
    • Wiencek, J.M.1
  • 17
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: from purified protein to diffraction-quality crystal
    • Chayen N.E., Saridakis E. Protein crystallization: from purified protein to diffraction-quality crystal. Nat Methods 2008, 5:147-153.
    • (2008) Nat Methods , vol.5 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 18
    • 0014855359 scopus 로고
    • Interferon: evidence for subunit structure
    • Carter W.A. Interferon: evidence for subunit structure. Proc Natl Acad Sci U S A 1970, 67:620-628.
    • (1970) Proc Natl Acad Sci U S A , vol.67 , pp. 620-628
    • Carter, W.A.1
  • 19
    • 0032839451 scopus 로고    scopus 로고
    • The effect of temperature and solution pH on the nucleation of tetragonal lysozyme crystals
    • Judge R.A., Jacobs R.S., Frazier T., Snell E.H., Pusey M.L. The effect of temperature and solution pH on the nucleation of tetragonal lysozyme crystals. Biophys J 1999, 77:1585-1593.
    • (1999) Biophys J , vol.77 , pp. 1585-1593
    • Judge, R.A.1    Jacobs, R.S.2    Frazier, T.3    Snell, E.H.4    Pusey, M.L.5
  • 20
    • 80052324379 scopus 로고    scopus 로고
    • On the circular birefringence of polycrystalline polymers: polylactide
    • Ye H.M., Xu J., Freudenthal J., Kahr B. On the circular birefringence of polycrystalline polymers: polylactide. J Am Chem Soc 2011, 133:13848-13851.
    • (2011) J Am Chem Soc , vol.133 , pp. 13848-13851
    • Ye, H.M.1    Xu, J.2    Freudenthal, J.3    Kahr, B.4
  • 21
    • 0037356379 scopus 로고    scopus 로고
    • Polymer spherulites: a modern assessment
    • Bassett D.C. Polymer spherulites: a modern assessment. J Macromol Sci Phys 2003, 42:227-256.
    • (2003) J Macromol Sci Phys , vol.42 , pp. 227-256
    • Bassett, D.C.1
  • 22
    • 21244483188 scopus 로고    scopus 로고
    • The mechanism of amyloid spherulite formation by bovine insulin
    • Krebs M.R.H., Bromley E.H.C., Rogers S.S., Donald A.M. The mechanism of amyloid spherulite formation by bovine insulin. Biophys J 2005, 88:2013-2021.
    • (2005) Biophys J , vol.88 , pp. 2013-2021
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Rogers, S.S.3    Donald, A.M.4
  • 23
    • 33748258031 scopus 로고    scopus 로고
    • Fabrication of polymeric microparticles for drug delivery by soft lithography
    • Guan J., Ferrell N., James Lee L., Hansford D.J. Fabrication of polymeric microparticles for drug delivery by soft lithography. Biomaterials 2006, 27:4034-4041.
    • (2006) Biomaterials , vol.27 , pp. 4034-4041
    • Guan, J.1    Ferrell, N.2    James Lee, L.3    Hansford, D.J.4
  • 24
    • 56149109873 scopus 로고    scopus 로고
    • Stabilization of tetanus toxoid encapsulated in PLGA microspheres
    • Jiang W., Schwendeman S.P. Stabilization of tetanus toxoid encapsulated in PLGA microspheres. Mol Pharm 2008, 5:808-817.
    • (2008) Mol Pharm , vol.5 , pp. 808-817
    • Jiang, W.1    Schwendeman, S.P.2
  • 25
    • 0000588546 scopus 로고
    • Crystalline and amorphous insulin-zinc compounds with prolonged action
    • Hallas-Moller K., Petersen K., Schlichtkrull J. Crystalline and amorphous insulin-zinc compounds with prolonged action. Science 1952, 116:394-398.
    • (1952) Science , vol.116 , pp. 394-398
    • Hallas-Moller, K.1    Petersen, K.2    Schlichtkrull, J.3
  • 26
    • 24044485078 scopus 로고    scopus 로고
    • Novel long-acting crystal formulation of human growth hormone
    • Govardhan C., Khalaf N., Jung C.W., Simeone B., Higbie A., Qu S., et al. Novel long-acting crystal formulation of human growth hormone. Pharm Res 2005, 22:1461-1470.
    • (2005) Pharm Res , vol.22 , pp. 1461-1470
    • Govardhan, C.1    Khalaf, N.2    Jung, C.W.3    Simeone, B.4    Higbie, A.5    Qu, S.6
  • 27
  • 28
    • 33846317458 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of donepezil-sustained release microparticles for the treatment of Alzheimer's disease
    • Zhang P., Chen L., Gu W., Xu Z., Gao Y., Li Y. In vitro and in vivo evaluation of donepezil-sustained release microparticles for the treatment of Alzheimer's disease. Biomaterials 2007, 28:1882-1888.
    • (2007) Biomaterials , vol.28 , pp. 1882-1888
    • Zhang, P.1    Chen, L.2    Gu, W.3    Xu, Z.4    Gao, Y.5    Li, Y.6
  • 29
    • 0037290060 scopus 로고    scopus 로고
    • Vancomycin encapsulation in biodegradable poly(epsilon-caprolactone) microparticles for bone implantation. Influence of the formulation process on size, drug loading, in vitro release and cytocompatibility
    • Le Ray A.M., Chiffoleau S., Iooss P., Grimandi G., Gouyette A., Daculsi G., et al. Vancomycin encapsulation in biodegradable poly(epsilon-caprolactone) microparticles for bone implantation. Influence of the formulation process on size, drug loading, in vitro release and cytocompatibility. Biomaterials 2003, 24:443-449.
    • (2003) Biomaterials , vol.24 , pp. 443-449
    • Le Ray, A.M.1    Chiffoleau, S.2    Iooss, P.3    Grimandi, G.4    Gouyette, A.5    Daculsi, G.6
  • 30
    • 0017835737 scopus 로고
    • Molecular morphology in semicrystalline polymers
    • Flory P.J. Molecular morphology in semicrystalline polymers. Nature 1978, 272:226-229.
    • (1978) Nature , vol.272 , pp. 226-229
    • Flory, P.J.1
  • 32
  • 33
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: a formulation challenge
    • Frokjaer S., Otzen D.E. 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    Otzen, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.