Advanced search
Publication Cover
Expert Opinion on Biological Therapy Volume 4, 2004 - Issue 3
Submit an article Journal homepage
793
Views
148
CrossRef citations to date
0
Altmetric
Review

Protein crystals for the delivery of biopharmaceuticals

Sujit K Basu Altus Biologics, Inc., 625 Putnam Avenue, Cambridge, MA 02139, USA. [email protected]
,
Chandrika P Govardhan Altus Biologics, Inc., 625 Putnam Avenue, Cambridge, MA 02139, USA. [email protected]
,
Chu W Jung Altus Biologics, Inc., 625 Putnam Avenue, Cambridge, MA 02139, USA. [email protected]
&
Alexey L Margolin Altus Biologics, Inc., 625 Putnam Avenue, Cambridge, MA 02139, USA. [email protected]
Pages 301-317 | Published online: 03 Mar 2005

Bibliography

  • HANCOCK BC, ZOGRAFI G: Characteristics and significance of the amorphous state in pharmaceutical systems. Pharm. Sci (1997) 86(1):1–12.
  • WALSH G: Biopharmaceutical benchmarks. Nat. Biotechnol (2003) 21(8):865–870.
  • BRANGE J, VOLUND A: Insulin analogs with improved pharmacokinetic profiles. Adv. Drug Deify. Rev (1999) 35:307–335.
  • HAGEDORN HC, JENSEN BN, KRARUP NB, WODSTRUP I: Protamine insulinate. JAMA (1936) 106:177–180.
  • ••Elegant work that demonstrated the effectof protarnine complexation.
  • JEN A, MERKLE HP: Diamonds in the rough: protein crystals from a formulation perspective. Pharm. Res. (2001) 18(11):1483–1488.
  • MARGOLIN AL, NAVIA MA: Protein crystals as novel catalytic materials. Angew Chem. Int. Ed. Engl. (2001) 40(12):2204–2222.
  • ••Detailed review on application ofprotein crystals.
  • HALLAS-MOLLER K, PETERSEN K, SCHLICHTKRULL J: Crystalline and amorphous insulin-zinc compounds with prolonged action. Science (1952) 116:394–399.
  • ••Prolonged acting insulin crystalformulation with excess zinc.
  • SHENOY B, WANG Y, SHAN W, MARGOLIN AL: Stability of crystalline proteins. Biotechnol. Bioeng. (2001) 73: 358–369.
  • •Demonstration of improved stability of protein in the crystalline state.
  • HALBAN PA, MUTKOSKI R, DODSON G, ORCI L: Resistance of the insulin crystal to lysosomal proteases: Implications for pancreatic B-cell crinophagy. Diabetologia (1987) 30:348–353.
  • PARK DH, LEE HJ, KYU E: Crystallization of alkaline protease as a means of purification process. Km: I Chem. Eng. (1997) 14:64–68.
  • DUNLOP KV, HAZES B: When less is more: a more efficient vapour-diffusion protocol. Acta Crys. (2003) D59:1797-1800.
  • KLYUSHNICHENKO V: Protein crystallization: from HTS to kilogram-scale. Carr. Opin. Drug Discov. Dev (2003) 6(6):848–854.
  • ••Large-scale protein crystallisationprocess development.
  • JUDGE RA, JOHNS MR, WHITE ER: Protein purification by bulk crystallization: the recovery of albumin. Biotechnol. Bioeng. (1995) 48(4):316–323.
  • JACOBSEN C, GARSIDE J, HOARE M: Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broth. Biotechnol. Bioeng. (1998) 57(6):666–675.
  • LEE TS, VAGHJIANI JD, LYE GJ, TURNER MK: A systematic approach to the large scale production of protein crystals. Enzyme Microb. Technol (2000) 26:582–592.
  • VUOLANTO A, UOTILA S, LEISOLA M, VISURI K: Solubility and crystallization of xylose isomerase from Streptomyces rubiginosus. I CrysL Growth (2003) 257:403–411.
  • GROVES MJ: Pharmaceutical characterization of Mycobacterium bovis bacillus Calmette-Guerin (BCG) vaccine used for the treatment of superficial bladder cancer. Pharm. Sci (1993) 82(6):555–562.
  • GUIDANCE FOR INDUSTRY: Sterile drug products produced by aseptic processing - Current good manufacturing practice, US Department of Health and Human Services Food and Drug Administration Center for Drug Evaluation and Research (CDER) Center for Biologics Evaluation and Research (CBER) Office of Regulatory Affairs (ORA) (2003).
  • GUIDANCE FOR INDUSTRY: Sterility requirement for aqueous-based drug products for oral inhalation - Small entity compliance guide, US Department of Health and Human Services Food and Drug Administration Center for Drug Evaluation and Research (CDER) (2001).
  • DEFELIPPIS MR, AKERS MJ: Peptides and proteins as parenteral suspensions: An overview of design, development, and manufacturing considerations. In: Pharmaceutical Formulation Development of Peptides and Proteins. Frokjaer S, Hovgaard L (Eds), Taylor and Francis, Inc., Philadelphia (1999):113–144.
  • •An excellent review on parenteral suspension of peptides and proteins.
  • Physicians' Desk Reference. 57h Ed, Medical Economics Staff, PDR Staff (Eds), (2003).
  • RICHARDS JP, STICKELMEYER MP, FRANK BH et al: Preparation of a microcrystalline suspension formulation of Lys(B28)Pro(B29)-human insulin with ultralente properties. Pharm. Sci (1999) 88(9):861–867.
  • DEFELIPPIS MR, CHANCE RE, FRANK BH: Insulin self-association and the relationship to pharmacokinetics and pharmacodynamics. Crit. Rev Tiler. Drug Carrier. Syst. (2001) 18(2):201–264.
  • Lupron Depots package insert, TAP Pharmaceuticals Products, Inc., Lake Forest, IL, USA.
  • Nutropin Depots package insert, Genentech, Inc., South San Francisco, CA, USA.
  • MCPHERSON A: Crystallization of Biological Macromolecules. Cold Spring Harbor Laboratory Press, New York (1999).
  • •An excellent book on crystallisation of biological macromolecules.
  • DUCRUIX A, GIEGE R: Crystallization of Nucleic Acids and Proteins: A Practical Approach. Ducruix A, Giegé R (Eds), Oxford University Press, Oxford, UK (1999).
  • •An excellent book on crystallisation of nucleic acids and proteins.
  • JANCARIK J, KIM SH: Sparse matrix sampling: a screening method for crystallization of proteins. J Appl Crys. (1991) 24:409–413.
  • LORBER B, CUDNEY R: A modular plate for the optimization of protein crystallization conditions. J Appl Crystr: (2002) 35:509–510.
  • SNOOK CE PURDY MD, WIENER MC: Use of crystallization robot to set up sitting drop vapor diffusion crystallization and in situ crystallization screens. Appl Cryst. (2000) 33:344–349.
  • HANSEN CL, SKORDALAKES E, BERGER JM, QUAKE SR: A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion. Proc. Natl. Acad. Sci. USA (2002) 99(26):16531–16536.
  • WILSON J: Towards the automated evaluation of crystallization trials. Acta Crys. (2002) D58:1907-1914.
  • YANG MX, SHENOY B, DISTLER M et al.: Crystalline monoclonal antibodies for subcutaneous delivery. Proc. Natl Acad. Sci. USA (2003) 100:6934–6939.
  • ••High concentration, low viscosity mAbformulations for subcutaneous delivery.
  • HARRIS LJ, LARSON SB, MCPHERSON A: Comparison of intact antibody structures and the implications for effector function. Adv. Immunol (1999) 72:191–208.
  • KUZNETSOV YG, DAY J, NEWMAN R, MCPHERSON A: Chimeric human-simian anti-CD4 antibodies form crystalline high symmetry particles. I Struct. Biol. (2000) 131:108–115.
  • •Use of AFM to visualise aggregates formation prior to crystallisation.
  • SAPHIRE EO, PARREN PW, BARBAS CF 3RD, BURTON DR, WILSON IA: Crystallization and preliminary structure determination of an intact human immunoglobulin, b12: an antibody that broadly neutralizes primary isolates of HIV-1. Acta Crystallogc D. Biol. Crystallogc (2001) 57:168–171.
  • JILLAVENKATESA A, DAPKUNAS SJ, LUM LSH: Number of particles to count. In: Particle Size Characterization, NIST Recommended Practice Guide, Special Publication (2001) 960–1:74–78.
  • DRENTH J: Principles of Protein X-Ray Crystallography 2nd Ed, Springer-Verlag, New York, USA (1999).
  • MCREE DE: Practical Protein Crystallography 2nd Ed, Academic Press, New York, USA (1999).
  • KAMP RIVI, CHOLI-PAPADOPOULOU T, WITTMANN-LIEBOLD B: Protein Structure Analysis: Preparation, Characterization, and Microsequencing. Kamp RIVI, Choli-Papadopoulou T, Wittmann-Liebold B (Eds), Springer-Verlag, New York, USA (1997).
  • PIKAL MJ, RIGSBEE DR: The stability of insulin in crystalline and amorphous solids: observation of greater stability for the amorphous form. Pharm. Res. (1997) 14:1379–1387.
  • DRENTH J: The theory of X-ray diffraction by a crystal. In: Principles of Protein X-Ray crystallography (2nd Ed.), Springer Verlag, New York, USA (1999).
  • HOVMOLLER S, ZOU XD, WEIRICH T: Single structure determination on powders by electron crystallography. Applied Crystallography Proceeding of the 17th Conference, Wisl, Poland (1997):18–27.
  • RUTH L, EISENBERG D, NEUFELD EF: Alpha-L-iduronidase forms semi-crystalline spherulites with amyloid-like properties. Acta Crystallogr. (2000) Sect D, 56: 524–528.
  • STAHLBERG H, FOTIADIS D, SCHEURING S et al: Two-dimensional crystals: a powerful approach to assess structure, function and dynamics of membrane proteins. FEBS Lett. (2001) 504:166–172.
  • MCPHERSON A, KUZNETSOV YG, MALKIN A, PLOMP M: Macromolecular crystal growth as revealed by atomic force microscopy. Struct. Biol. (2003) 142:32-46 and references therein.
  • •Use of AFM to study protein crystal growth processes.
  • YIP CM, BRADER ML, FRANK BH, DEFILIPPIS MR, WARD MD: Structural studies of a crystalline insulin analog complex with protamine by atomic force microscopy. Biophys. 1 (2000) 78:466–473.
  • •Study of different insulin crystals using AFM.
  • KARRASCH S, HEGERL R, HOH JH, BAUMEISTER W, ENGEL A: Atomic force microscopy produces faithful high resolution images of protein surfaces in an aqueous environment. Proc. Nati Acad. Sci. USA (1994) 91:836–838.
  • TORRES J, STEVENS TJ, SAMSO M: Membrane proteins: the 'Wild West' of structural biology. Trends Biochem. Sci (2003) 28:137–144.
  • ARRONDO JL, MUGA A, CASTRESANA J, GONI FM: Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Frog. Biophys. Mol. Biol (1993) 59:23–56.
  • FABIAN H, SCHULTZ CP: Fourier transform infrared spectroscopy in peptide and protein analysis. In: Encyclopedia of Analytical Chemistry Meyers RA (Ed.), John Wiley, Chichester (2000):5779–5803.
  • •Micro-ATR FTIR in the study of protein secondary structure.
  • VILENCHIK LZ, GRIFFITH JP, ST CLAIR N, NAVIA MA, MARGOLIN AL: Protein crystals as novel microporous materials. J. Am. Chem. Soc. (1998) 120:4290–4294.
  • ••Study of porous structure of proteincrystals using SEC technique.
  • MEGELSKI S, LIEB A, PAUCHARD M et al.: Orientation of fluorescent dyes in the nano channels of zeolite L. J. Phys. Chem. B (2001) 105:25–35.
  • BENDA A, BENES M, MARECEKV, LHOTSKY A, HERMENS WT, HOF AM: How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy. Langmuir (2003) 19:4120–4126.
  • MACPHERSON JV, JONES CE, BARKERMAND AL, UN WIN PR: Electrochemical imaging of diffusion through single nanoscale pores. Anal. Chein(2002) 74:1841–1848.
  • MARTIN RW, ZILM KW: Preparation of protein nanocrystals and their characterization by solid state NMR. .1. Magn. Reson. (2003) 165:162–174.
  • GINSBERG PL, BHATIA S, MCMINN RL: The road ahead for biologics manufacturing. Guides for the Journey. USBANCORP/Piper Jaffray (2002).
  • HAINSWORTH JD: Rituximab as first-line and maintenance therapy for patients with indolent non-Hodgkin's lymphoma: interim follow-up of a multicenter Phase II trial. Semin. Omni (2002) 29(1 Suppl. 2):25–29.
  • LEYLAND-JONES B, SMITH I: Role of Herceptin in primary breast cancer: views from North America and Europe. Oncology (2001) 61 (Suppl. 2):83–91.
  • KEATING GM, PERRY CM: Infliximab: an updated review of its use in Crohn's disease and rheumatoid arthritis BioDrugs (2002) 16:111–148.
  • MEEKER SP, POON WCK, PUSEY PN: Concentration dependence of the low-shear viscosity of suspensions of hard-sphere colloids. Phys. Rev E(1997) 55:5718–5722.
  • BRANGE J, LANGKJAER L, HAVELUND S, VOLUND A: Chemical stability of insulin. 1. Hydrolytic degradation during storage of pharmaceutical preparations. Pharm. Res. (1992) 9:715–726.
  • KRAYENBUHL C AND ROSENBERG T: Crystalline protamine insulin. Rep. Steno Mem. Hosp. Nord. hasulinlab (1946) 1:60–73.
  • SCHLICHTKRULL J: Insulin crystals IV The preparations of nuclei nuclei, seeds and monodisperse insulin crystal suspensions. Acta Chem. Scand. (1957) 11:299–302.
  • BRANGE J: Calenics of insulin: the physicochemical and pharmaceutical aspects of insulin and insulin preparations. Springer-Verlag, Berlin, Heidelberg (1987).
  • REICHERT P, NAGABHUSAN TL, LONG MM et al.: Macroscale production and analysis of crystalline interferon alpha-2B in microgravity on STS-52. In: Space Technology & Application International Forum (STAIF-96), El-Genk MS (Ed.), American Institute of Physics, Woodbury, NY, USA (1996) 361(1):139–148.
  • JOHNSON OL, CLELAND JL, LEE HJ et al.: A month-long effect from a single injection of microencapsulated human growth hormone. Nat. Med (1996) 2(7):795–799.
  • VANDORPE J, SCHACHT E, DUNN S et al.: Long circulating biodegradable poly(phosphazene) nanoparticles surface modified with poly(phosphazene)- poly(ethylene oxide) copolymer. Biomaterials (1997) 18(17):1147–1152.
  • YEWEY GL et al.: Delivery of proteins from a controlled release injectable implant. In: Protein Delivery: Physical Systems, Sanders LM, Hendren RW (Eds), Plenum Press, New York (1997):93–117.
  • SMITH DA, TIPTON AJ: A novel parenteral delivery system. Pharm. Res. (1996) 13(9):5300.
  • OKUMU FW, DAO LN, FIELDER PJ et al.: Sustained delivery of human growth hormone from a novel gel system: SABER. Biomaterials (2002) 23(22):4353–4358.
  • PECHENOV S, SHENOY B, YANG M, BASU SK, MARGOLIN AL: Crystalline proteins for stabilization and controlled release formulations. Proc. [nt. Symp. Control. Rel. Bioact. Mater. Glasgow, Scotland 30 (2003).
  • BRAUE EH JR: Development of a reactive topical skin protectant. Appl. Toxicol. (1999) 19(Suppl.):47–53.
  • TAM J, FIE GEL J, HANES J: Protein crystals for pulmonary drug delivery. Proc. hat Symp. Control. Rel. Bioact. Mater. San Diego, USA 28 (2001).
  • JOHNSON AJ, GOGER PR, TILLETT WS: The intravenous injection of bovine crystalline pancreatic desoxyribonuclease into patients. j. Clin. Invest. (1954) 33:1670–1685.
  • AYVAZIAN JH, AYVAZIAN LF: Effect of intravenous administration of crystalline pancreatic desoxyribonuclease in patients with gout: N. Engl. J. Med. (1960) 263(20):999–1002.
  • BRADER ML, SUKUMAR M, PEKAR AH et al.: Hybrid insulin cocrystals for controlled release delivery. Nat. Biotechnol. (2002) 20:800–804.
  • •Protein cocrystals for controlled release.

Websites

  • http://www.bmcd.nist.gov:8080/bmcd/ bmcd.html The BMCD version 2.00 (1998).
  • http://www.insulindevice.com/ novofine_features.asp Novo fine needle description at the Novo Nordisk website (2003).
  • http://www.fda.gov/ohrms/dockets/ac/03/ slides/3944s1_05-Hussain.ppt Slides at the FDA website (2003).
  • http://www.fda.gov The FDA website (2003).
  • http://www.emea.eu.int The EMEA website (2003).
  • http://rsb.info.nih.gov/nih-image/ Image available at the NIH website (2003).
  • http://www.stepex.com/ conference_proceedings/ conference_proceedings/pcia_march 192002/ 039_coletica.html Conference INTEX, Shanghai, China; 19th, 20th & 21st March 2002 (2002).
  • http://www.lillydiabetes.com/Products/ TimeActivityProfiles.cfm Time activity profiles at the Eli Lilly website (2003).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.