메뉴 건너뛰기




Volumn 496, Issue 2, 2015, Pages 850-862

Co-encapsulation of lyoprotectants improves the stability of protein-loaded PLGA nanoparticles upon lyophilization

Author keywords

Co encapsulation; Insulin; Lyophilization; Lyoprotectants; PLGA nanoparticles; Protein stability

Indexed keywords

FRUCTOSE; GLUCOSE; NANOPARTICLE; POLYGLACTIN; RECOMBINANT HUMAN INSULIN; SORBITOL; SUCROSE; TREHALOSE; LACTIC ACID; POLYGLYCOLIC ACID; POLYLACTIC ACID-POLYGLYCOLIC ACID COPOLYMER;

EID: 84949571235     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2015.10.032     Document Type: Article
Times cited : (45)

References (37)
  • 1
    • 33646830139 scopus 로고    scopus 로고
    • Investigation of nanocapsules stabilization by amorphous excipients during freeze-drying and storage
    • W. Abdelwahed, G. Degobert, and H. Fessi Investigation of nanocapsules stabilization by amorphous excipients during freeze-drying and storage Eur. J. Pharm. Biopharm. 63 2006 87 94
    • (2006) Eur. J. Pharm. Biopharm. , vol.63 , pp. 87-94
    • Abdelwahed, W.1    Degobert, G.2    Fessi, H.3
  • 2
    • 34547800192 scopus 로고    scopus 로고
    • Freeze-drying of nanoparticles: Formulation, process and storage considerations
    • W. Abdelwahed, G. Degobert, S. Stainmesse, and H. Fessi Freeze-drying of nanoparticles: formulation, process and storage considerations Adv. Drug Deliv. Rev. 58 2006 1688 1713
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , pp. 1688-1713
    • Abdelwahed, W.1    Degobert, G.2    Stainmesse, S.3    Fessi, H.4
  • 3
    • 0029815193 scopus 로고    scopus 로고
    • Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration
    • S. Allison, A. Dong, and J. Carpenter Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration Biophys. J. 71 1996 2022 2032
    • (1996) Biophys. J. , vol.71 , pp. 2022-2032
    • Allison, S.1    Dong, A.2    Carpenter, J.3
  • 4
    • 34249337735 scopus 로고    scopus 로고
    • Review of osmotic pressure driven release of proteins from monolithic devices
    • B. Amsden Review of osmotic pressure driven release of proteins from monolithic devices J. Pharm. Pharm. Sci. 10 2007 129 143
    • (2007) J. Pharm. Pharm. Sci. , vol.10 , pp. 129-143
    • Amsden, B.1
  • 5
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of protein stabilization by sugars during freeze-drying and storage: Native structure preservation, specific interaction, and/or immobilization in a glassy matrix?
    • L. Chang, D. Shepherd, J. Sun, D. Ouellette, K. Grant, X. Tang, and M. Pikal Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix? J. Pharm. Sci. 94 2005 1427 1444
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1427-1444
    • Chang, L.1    Shepherd, D.2    Sun, J.3    Ouellette, D.4    Grant, K.5    Tang, X.6    Pikal, M.7
  • 6
    • 23844461800 scopus 로고    scopus 로고
    • Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state
    • L. Chang, D. Shepherd, J. Sun, X. Tang, and M. Pikal Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: implications for the mechanism of protein stabilization in the solid state J. Pharm. Sci. 94 2005 1445 1455
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1445-1455
    • Chang, L.1    Shepherd, D.2    Sun, J.3    Tang, X.4    Pikal, M.5
  • 7
    • 0002469071 scopus 로고
    • Preserving dry biomaterials: The water replacement hypothesis
    • J. Crowe, L. Crowe, and J. Carpenter Preserving dry biomaterials: the water replacement hypothesis BioPharm 6 1993 28 37
    • (1993) BioPharm , vol.6 , pp. 28-37
    • Crowe, J.1    Crowe, L.2    Carpenter, J.3
  • 8
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • L. Crowe, D. Reid, and J. Crowe Is trehalose special for preserving dry biomaterials? Biophys. J. 71 1996 2087 2093
    • (1996) Biophys. J. , vol.71 , pp. 2087-2093
    • Crowe, L.1    Reid, D.2    Crowe, J.3
  • 10
    • 0033019164 scopus 로고    scopus 로고
    • Formulation and lyoprotection of poly(lactic acid-co-ethylene oxide) nanoparticles: Influence on physical stability and in vitro cell uptake
    • F. De Jaeghere, E. Allemann, J. Leroux, W. Stevels, J. Feijen, E. Doelker, and R. Gurny Formulation and lyoprotection of poly(lactic acid-co-ethylene oxide) nanoparticles: influence on physical stability and in vitro cell uptake Pharm. Res. 16 1999 859 866
    • (1999) Pharm. Res. , vol.16 , pp. 859-866
    • De Jaeghere, F.1    Allemann, E.2    Leroux, J.3    Stevels, W.4    Feijen, J.5    Doelker, E.6    Gurny, R.7
  • 11
    • 84886728300 scopus 로고    scopus 로고
    • Effect of cryoprotectants on the porosity and stability of insulin-loaded PLGA nanoparticles after freeze-drying
    • P. Fonte, S. Soares, A. Costa, J. Andrade, V. Seabra, S. Reis, and B. Sarmento Effect of cryoprotectants on the porosity and stability of insulin-loaded PLGA nanoparticles after freeze-drying Biomatter 2 2012 329 339
    • (2012) Biomatter , vol.2 , pp. 329-339
    • Fonte, P.1    Soares, S.2    Costa, A.3    Andrade, J.4    Seabra, V.5    Reis, S.6    Sarmento, B.7
  • 12
    • 84907968489 scopus 로고    scopus 로고
    • Stability study perspective of the effect of freeze-drying using cryoprotectants on the structure of insulin loaded into PLGA nanoparticles
    • P. Fonte, S. Soares, F. Sousa, A. Costa, V. Seabra, S. Reis, and B. Sarmento Stability study perspective of the effect of freeze-drying using cryoprotectants on the structure of insulin loaded into PLGA nanoparticles Biomacromolecules 15 2014 3753 3765
    • (2014) Biomacromolecules , vol.15 , pp. 3753-3765
    • Fonte, P.1    Soares, S.2    Sousa, F.3    Costa, A.4    Seabra, V.5    Reis, S.6    Sarmento, B.7
  • 13
    • 0032078241 scopus 로고    scopus 로고
    • Freeze-drying of bioproducts: Putting principles into practice
    • F. Franks Freeze-drying of bioproducts: putting principles into practice Eur. J. Pharm. Biopharm. 45 1998 221 229
    • (1998) Eur. J. Pharm. Biopharm. , vol.45 , pp. 221-229
    • Franks, F.1
  • 14
    • 0028847040 scopus 로고
    • Lyophilization-induced reversible changes in the secondary structure of proteins
    • K. Griebenow, and A. Klibanov Lyophilization-induced reversible changes in the secondary structure of proteins Proc. Natl. Acad. Sci. U. S. A. 92 1995 10969 10976
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.2
  • 15
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • K. Griebenow, and A. Klibanov On protein denaturation in aqueous-organic mixtures but not in pure organic solvents J. Am. Chem. Soc. 118 1996 11695 11700
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.2
  • 16
    • 0033586786 scopus 로고    scopus 로고
    • Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation
    • M. Heller, J. Carpenter, and T. Randolph Protein formulation and lyophilization cycle design: prevention of damage due to freeze-concentration induced phase separation Biotechnol. Bioeng. 63 1999 166 174
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 166-174
    • Heller, M.1    Carpenter, J.2    Randolph, T.3
  • 17
    • 33750060454 scopus 로고    scopus 로고
    • Freeze-drying of low molecular weight poly(l-lactic acid) nanoparticles: Effect of cryo- and lyoprotectants
    • S. Hirsjarvi, L. Peltonen, L. Kainu, and J. Hirvonen Freeze-drying of low molecular weight poly(l-lactic acid) nanoparticles: effect of cryo- and lyoprotectants J. Nanosci. Nanotecnhol. 6 2006 3110 3117
    • (2006) J. Nanosci. Nanotecnhol. , vol.6 , pp. 3110-3117
    • Hirsjarvi, S.1    Peltonen, L.2    Kainu, L.3    Hirvonen, J.4
  • 18
    • 24044452577 scopus 로고    scopus 로고
    • Effect of counterions on the physical properties of l-arginine in frozen solutions and freeze-dried solids
    • K. Izutsu, Y. Fujimaki, A. Kuwabara, and N. Aoyagi Effect of counterions on the physical properties of l-arginine in frozen solutions and freeze-dried solids Int. J. Pharm. 301 2005 161 169
    • (2005) Int. J. Pharm. , vol.301 , pp. 161-169
    • Izutsu, K.1    Fujimaki, Y.2    Kuwabara, A.3    Aoyagi, N.4
  • 19
    • 30844437524 scopus 로고    scopus 로고
    • Effect of cryoprotectants on the reconstitution of surfactant-free nanoparticles of poly(dl-lactide-co-glycolide)
    • Y. Jeong, Y. Shim, C. Kim, G. Lim, K. Choi, and C. Yoon Effect of cryoprotectants on the reconstitution of surfactant-free nanoparticles of poly(dl-lactide-co-glycolide) J. Microencapsul. 22 2005 593 601
    • (2005) J. Microencapsul. , vol.22 , pp. 593-601
    • Jeong, Y.1    Shim, Y.2    Kim, C.3    Lim, G.4    Choi, K.5    Yoon, C.6
  • 20
    • 1842865844 scopus 로고    scopus 로고
    • Effect of osmotic pressure in the solvent extraction phase on BSA release profile from PLGA microspheres
    • G. Jiang, B. Thanoo, and P. DeLuca Effect of osmotic pressure in the solvent extraction phase on BSA release profile from PLGA microspheres Pharm. Dev. Technol. 7 2002 391 399
    • (2002) Pharm. Dev. Technol. , vol.7 , pp. 391-399
    • Jiang, G.1    Thanoo, B.2    DeLuca, P.3
  • 22
    • 77649342497 scopus 로고    scopus 로고
    • Physical properties of griseofulvin-lipid nanoparticles in suspension and their novel interaction mechanism with saccharide during freeze-drying
    • S. Kamiya, T. Kurita, A. Miyagishima, S. Itai, and M. Arakawa Physical properties of griseofulvin-lipid nanoparticles in suspension and their novel interaction mechanism with saccharide during freeze-drying Eur. J. Pharm. Biopharm. 74 2010 461 466
    • (2010) Eur. J. Pharm. Biopharm. , vol.74 , pp. 461-466
    • Kamiya, S.1    Kurita, T.2    Miyagishima, A.3    Itai, S.4    Arakawa, M.5
  • 23
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • S. Kelly, T. Jess, and N. Price How to study proteins by circular dichroism Biochim. Biophys. Acta 1751 2005 119 139
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.1    Jess, T.2    Price, N.3
  • 24
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide i infrared spectra to determine the structural similarity of a protein in different states
    • B. Kendrick, A. Dong, S. Allison, M. Manning, and J. Carpenter Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states J. Pharm. Sci. 85 1996 155 158
    • (1996) J. Pharm. Sci. , vol.85 , pp. 155-158
    • Kendrick, B.1    Dong, A.2    Allison, S.3    Manning, M.4    Carpenter, J.5
  • 25
    • 34548049483 scopus 로고    scopus 로고
    • Nanosizing - Oral formulation development and biopharmaceutical evaluation
    • F. Kesisoglou, S. Panmai, and Y. Wu Nanosizing - oral formulation development and biopharmaceutical evaluation Adv. Drug Deliv. Rev. 59 2007 631 644
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , pp. 631-644
    • Kesisoglou, F.1    Panmai, S.2    Wu, Y.3
  • 26
    • 0037148679 scopus 로고    scopus 로고
    • Preparation and characterization of sterile and freeze-dried sub-200 nm nanoparticles
    • Y. Konan, R. Gurny, and E. Allémann Preparation and characterization of sterile and freeze-dried sub-200 nm nanoparticles Int. J. Pharm. 233 2002 239 252
    • (2002) Int. J. Pharm. , vol.233 , pp. 239-252
    • Konan, Y.1    Gurny, R.2    Allémann, E.3
  • 28
    • 0029781099 scopus 로고    scopus 로고
    • Effects of reducing sugars on the chemical stability of human relaxin in the lyophilized state
    • S. Li, T. Patapoff, D. Overcashier, C. Hsu, T. Nguyen, and R. Borchardt Effects of reducing sugars on the chemical stability of human relaxin in the lyophilized state J. Pharm. Sci. 85 1996 873 877
    • (1996) J. Pharm. Sci. , vol.85 , pp. 873-877
    • Li, S.1    Patapoff, T.2    Overcashier, D.3    Hsu, C.4    Nguyen, T.5    Borchardt, R.6
  • 29
    • 83655165245 scopus 로고    scopus 로고
    • Poly lactic-co-glycolic acid (PLGA) as biodegradable controlled drug delivery carrier
    • H. Makadia, and S. Siegel Poly lactic-co-glycolic acid (PLGA) as biodegradable controlled drug delivery carrier Polymers 3 2011 1377 1397
    • (2011) Polymers , vol.3 , pp. 1377-1397
    • Makadia, H.1    Siegel, S.2
  • 31
    • 84949555506 scopus 로고
    • Proteins and sugars affecting the zeta potential and stability of dispersed vesicular globules in w/o/w emulsions
    • K. Nishinari, E. Doi, Springer US
    • S. Matsumoto Proteins and sugars affecting the zeta potential and stability of dispersed vesicular globules in w/o/w emulsions K. Nishinari, E. Doi, Food Hydrocoll 1993 Springer US 399 408
    • (1993) Food Hydrocoll , pp. 399-408
    • Matsumoto, S.1
  • 32
    • 0025039869 scopus 로고
    • The relationship between the glass transition temperature and water vapor absorption by poly(vinylpyrrolidone)
    • C. Oksanen, and G. Zografi The relationship between the glass transition temperature and water vapor absorption by poly(vinylpyrrolidone) Pharm. Res. 7 1990 654 657
    • (1990) Pharm. Res. , vol.7 , pp. 654-657
    • Oksanen, C.1    Zografi, G.2
  • 33
    • 34948841373 scopus 로고    scopus 로고
    • Probing insulin's secondary structure after entrapment into alginate/chitosan nanoparticles
    • B. Sarmento, D. Ferreira, L. Jorgensen, and M. van de Weert Probing insulin's secondary structure after entrapment into alginate/chitosan nanoparticles Eur. J. Pharm. Biopharm. 65 2007 10 17
    • (2007) Eur. J. Pharm. Biopharm. , vol.65 , pp. 10-17
    • Sarmento, B.1    Ferreira, D.2    Jorgensen, L.3    Van De Weert, M.4
  • 34
    • 33748934610 scopus 로고    scopus 로고
    • Development and validation of a rapid reversed-phase HPLC method for the determination of insulin from nanoparticulate systems
    • B. Sarmento, A. Ribeiro, F. Veiga, and D. Ferreira Development and validation of a rapid reversed-phase HPLC method for the determination of insulin from nanoparticulate systems Biomed. Chromatogr. 20 2006 898 903
    • (2006) Biomed. Chromatogr. , vol.20 , pp. 898-903
    • Sarmento, B.1    Ribeiro, A.2    Veiga, F.3    Ferreira, D.4
  • 35
    • 0033635054 scopus 로고    scopus 로고
    • Protein instability in poly(lactic-co-glycolic acid) microparticles
    • M. van de Weert, W. Hennink, and W. Jiskoot Protein instability in poly(lactic-co-glycolic acid) microparticles Pharm. Res. 17 2000 1159 1167
    • (2000) Pharm. Res. , vol.17 , pp. 1159-1167
    • Van De Weert, M.1    Hennink, W.2    Jiskoot, W.3
  • 37
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • W. Wang Lyophilization and development of solid protein pharmaceuticals Int. J. Pharm. 203 2000 1 60
    • (2000) Int. J. Pharm. , vol.203 , pp. 1-60
    • Wang, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.