1,285
Views
34
CrossRef citations to date
0
Altmetric
Review Articles

A review on parenteral delivery of peptides and proteins

, , &
Pages 1403-1420 | Received 03 Apr 2019, Accepted 20 May 2019, Published online: 28 Jun 2019

References

  • Craik DJ, Fairlie DP, Liras S. The future of peptide-based drugs. Chem Biol Drug Des. 2013;81:136–147.
  • Malik NN. Drug discovery: past, present and future. Drug Discov Today. 2008;13:909–912.
  • Andrade F, Videira M, Ferreira D. Nanocarriers for pulmonary administration of peptide and therapeutic proteins. Nanomedicine. 2011;6:123–141.
  • Vlieghe P, Lisowski V, Martinez J. Synthetic therapeutic peptides: science and market. Drug Discov Today. 2010;15:40–56.
  • Lau JL, Dunn MK. Therapeutic peptides: historical perspectives, current development trends, and future directions. Bioorgan Med Chem. 2018;26:2700–2707.
  • Global peptide therapeutic market Global industry insights, Coherent maret insights. [accessed 2018 Dec 20]. Available from: https://www.coherentmarketinsights.com/market-insight/peptide-therapeutics-market-1837
  • Global Peptide Therapeutics Market, Dosage, Price& Clinical Trials Insight 2024. [accessed 2018 Dec 20]. Available from: https://www.prnewswire.com/news-releases/global-peptide-therapeutics-market-dosage-price–clinical-trials-insight-2024—101-marketed-drugs-with-a-50-billion-opportunity-300708154.html
  • Research and Markets. [accessed 2018 Dec 21]. Available from: https://www.researchandmarkets.com/research/jmm8r4/global_protein?w=4
  • Frokjaer S, Otzen DE. Protein drug stability: a formulation challenge. Nat Rev Drug Discov. 2005;4:298–306.
  • Hilser VJ, Dowdy D, Oas TG, et al. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proc Natl Acad Sci USA. 1998;95:9903–9908.
  • Narhi LO, Philo JS, Sun B, et al. Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor. Pharm Res. 1999;16:799–807.
  • Bell LN, Hageman MJ, Bauer JM. Impact of moisture on thermally induced denaturation and decomposition of lyophilized bovine somatotropin. Biopolymers. 1995;35:201–209.
  • Zhou P, Labuza TP. Effect of water content on glass transition and protein aggregation of whey protein powders during short term storage. Food Biophys. 2007;2:108–116.
  • D’Cruz NM, Bell LN. Thermal unfolding of gelatin in solids as affected by the glass transition. J Food Sci. 2005;70:E64–E68.
  • Privalov PL. Cold denaturation of proteins. Crit Rev Biochem Mol Biol. 1990;25:281–305.
  • Thirumangalathu R, Krishnan S, Bondarenko P, et al. Oxidation of methionine residues in recombinant human interleukin-1 receptor antagonist: implications of conformational stability on protein oxidation kinetics. Biochemistry. 2007;46:6213–6224.
  • Hermeling S, Crommelin DJ, Schellekens H, et al. Structure-immunogenicity relationships of therapeutic proteins. Pharm Res. 2004;21:897–903.
  • Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006;8:E501–507.
  • Kaiser ET, Kezdy FJ. Secondary structures of proteins and peptides in amphiphilic environments. (a review). Proc Natl Acad Sci USA. 1983;80:1137–1143.
  • Patro SY, Freund E, Chang BS. Protein formulation and fill-finish operations. Biotechnol Annu Rev. 2002;8:55–84.
  • Cromwell MEM, Hilario E, Jacobson F. Protein aggregation and bioprocessing. AAPS J. 2006;8:E572–E579.
  • Maa YF, Hsu CC. Effect of high shear on proteins. Biotechnol Bioeng. 1996;51:458–465.
  • Randolph TW, Jones LS. Surfactant-protein interactions. In: Carpenter JF, Manning MC, editor. Rational design of stable protein formulations, pharmaceutical biotechnology. Vol. 13. New York (NY): Springer US; 2002. p. 159–118.
  • Katakam M, Bell LN, Banga AK. Effect of surfactants on the physical stability of recombinant human growth hormone. J Pharm Sci. 1995;84:713–716.
  • Vidanovic D, Askrabic JM, Stankovic M, et al. Effects of nonionic surfactants on the physical stability of immunoglobulin G in aqueous solution during mechanical agitation. Pharmazie. 2003;58:399–404.
  • Valentte JJ, Payne RW, Manning MC, et al. Colloidal behaviour of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr Pharm Biotechnol. 2005;6:427–436.
  • Avanti C, Amorij JP, Setyaningsih D, et al. A new strategy to stabilize oxytocin in aqueous solutions: I. The effects of divalent metal ions and citrate buffer. AAPS J. 2011;13:284–290.
  • Svilenov H, Markoja U, Winter G. Isothermal chemical denaturation as a complementary tool to overcome limitations of thermal differential scanning fluorimetry in predicting physical stability of protein formulations. Eur J Pharm Biopharm. 2018;125:106–113.
  • Mahler HC, Muller R, Frie W, et al. Induction and analysis of aggregates in a liquid IgG1-antibody formulation. Eur J Pharm Biopharm. 2005;59:407–417.
  • Johnson CM. Differential scanning calorimetry as a tool for protein folding and stability. Arch Biocam Biophys. 2013;531:100–109.
  • Ericsson UB, Hallberg BM, Detitta GT, et al. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem. 2006;357:289–298.
  • Wanner R, Breitsprecher D, Duhr S, et al. Themo-optical protein characterization for straight forward preformulation development. J Pharm Sci. 2017;106:2955–2958.
  • Menzen TA. Temperature induced unfolding, aggregation, and interaction of therapeutic monoclonal antibodies [PhD thesis]. München, Germany: Ludwig Maximilian University of Munich; 2014.
  • Freire E, Schon A, Hutchins BM, et al. Chemical denaturation as a tool in the formulation optimization of biologics. Drug Discov Today. 2013;18:1007–1013.
  • Pace CN, Shaw KI. Linear extrapolation method of analyzing solvent denaturation curves. Proteins. 2007;4:1–7.
  • Niklasson M, Andresen C, Helander S, et al. Robust and convenient analysis of protein thermal and chemical stability. Protein Sci. 2015;24:2055–2062.
  • Lazar KI, Patapoff TW, Sharma VK. Cold denaturation of monoclonal antibodies. MAbs. 2010;2:42–52.
  • Svilenov H, Gentiluomo L, Friess W, et al. A new approach to study the physical stability of monoclonal antibody formulations - dilution from a denaturant. J Pharm Sci. 2018;107:3007–3013.
  • Manning MC, Patel K, Borchardt RT. Stability of protein pharmaceuticals. Pharm Res. 1989;6:903–918.
  • Aswad DW. Deamidation and isoaspartate formation in peptides and proteins. Boca Raton (FL): CRC Press; 2001.
  • Robinson NE, Robinson AB. Molecular clocks: deamidation of asparaginyl and glutaminyl residues in peptides and proteins. Cave Junction (OR): Althouse Press; 2004.
  • Kossiakoff AA. Tertiary structure is a principal determinant to protein deamidation. Science. 1988;240:191–194.
  • Capasso S, Salvadori S. Effect of the three-dimensional structure on the deamidation reaction of ribonuclease A. J Pept Res. 1999;54:377–382.
  • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem. 1993;62:797–821.
  • Hovorka S, Schöneich C. Oxidative degradation of pharmaceuticals: theory, mechanisms and inhibition. J Pharm Sci. 2001;90:253–269.
  • Li S, Schöneich C, Borchardt RT. Chemical instability of protein pharmaceuticals: mechanisms of oxidation and strategies for stabilization. Biotechnol Bioeng. 1995;48:490–500.
  • Davies MJ. The oxidative environment and protein damage. Biochim Biophys Acta. 2005;1703:93–109.
  • Kerwin BA, Remmele RL. Protect from light: photodegradation and protein biologics. J Pharm Sci. 2007;96:1468–1479.
  • Chu JW, Yin J, Brooks BR, et al. A comprehensive picture of non-site specific oxidation of methionine residues by peroxides in protein pharmaceuticals. J Pharm Sci. 2004;93:3096–3102.
  • Roy S, Mason BD, Schöneich CS, et al. Light-induced aggregation of type I soluble tumor necrosis factor receptor. J Pharm Sci. 2009;98:3182–3199.
  • Manning MC, Chou DK, Murphy BM, et al. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27:544–575.
  • Yan Q, Huang M, Lewis ML, et al. Structure based prediction of asparagine deamidation propensity in monoclonal antibodies. MAbs. 2018;10:901–912.
  • Liu H, Ponniah G, Neill A, et al. Accurate determination of protein methionine oxidation by stable isotope labeling and lc-ms analysis. Anal Chem. 2013;85:11705–11709.
  • Kambieri M, Kim YJ, Jun B, et al. The effects of sucrose on stability of human brain natriuretic peptide [hBNP(1–32)] and human parathyroid hormone [hPTH(1–34)]. J Peptide Res. 2005;66:348–356.
  • Wiśniewski K, Finnman J, Flipo M, et al. On the mechanism of degradation of oxytocin and its analogues in aqueous solution. Biopolymers. 2013;100:408–421.
  • Hawe A, Poole R, Romeijn S, et al. Towards heat-stable oxytocin formulations: analysis of degradation kinetics and identification of degradation products. Pharm Res. 2009;26:1679–1688.
  • Bruno BJ, Miller GD, Lim CS. Basics and recent advances in peptide and protein drug delivery. Ther Deliv. 2013;4:1443–1467.
  • Antosova Z, Mackova M, Kral V, et al. Therapeutic application of peptides and proteins: parenteral forever? Trends Biotechnol. 2009;27:628–635.
  • Ohtake S, Kita Y, Payne R, et al. Structural characteristics of short peptides in solution. Protein Pept Lett. 2013;20:1308–1323.
  • Jitendra, Sharma PK, Bansal S, et al. Noninvasive routes of proteins and peptides drug delivery. Indian J Pharm Sci. 2011;73:367–375.
  • Golovanov AP, Hautbergue GM, Wilson SA, et al. A simple method for improving protein solubility and long-term stability. J Am Chem Soc. 2004;126:8933–8939.
  • Wei G, Lu LF, Lu WY. Stabilization of recombinant human growth hormone against emulsification-induced aggregation by Pluronic surfactants during microencapsulation. Int J Pharm. 2007;338:125–132.
  • Joshi O, McGuire J. Adsorption behavior of lysozyme and Tween 80 at hydrophilic and hydrophobic silica-water interfaces. Appl Biochem Biotechnol. 2009;152:235–248.
  • Malarkani K, Sarkar I, Selvam S. Denaturation studies on bovine serum albumin-bile salt system: bile salt stabilizes bovine serum albumin through hydrophobicity. J Pharm Anal. 2018;8:27–36.
  • Capelle MAH, Gurny R, Arvinte T. A high throughput protein formulation platform: case study of salmon calcitonin. Pharm Res. 2009;26:118–128.
  • McGoff P, Scher DS. Solution formulation of proteins/peptides. In: Mcnally EJ, Hastedt JE, editors. Protein formulation and delivery. 2nd ed. Boca Raton (FL): CRC Press; 2007. p. 135–146.
  • Chang BS, Hershenson S. Practical approaches to protein formulation development. In: Carpenter JF, Manning MC, editors. Rational design of stable protein formulations. New York (NY): Pharmaceutical Biotechnology; 2002. p. 1–25.
  • New Drugs at FDA: CDER’s New Molecular Entities and New Therapeutic Biological Products. [accessed on 2019 Feb 12]. Available from: https://www.fda.gov/Drugs/DevelopmentApprovalProcess/DrugInnovation/default.htm
  • Brazeau GA, Cooper B, Svetic KA, et al. Current perspectives on pain upon injection of drugs. J Pharm Sci. 1998;87:667–677.
  • Brange J, Havelund S, Hougaard P. Chemical instability of insulin. 2. Formation of high molecular weight transformation product during storage of pharmaceutical preparations. Pharma Res. 1992;09:727–734.
  • Katayama DS, Nayar R, Chou DK, et al. Effect of buffer species on the thermally induced aggregation of interferon-tau. J Pharm Sci. 2006;95:1212–1226.
  • McGuire J, Wahlgren MC, Arnebrant T. Structural stability effects on the adsorption and dodecyltrimethylammonium bromide-mediated elutability of bacteriophage T4 lysozyme at silica surfaces. J Colloid Interface Sci. 1995;170:182–192.
  • Arnebrant T, Wahlgren MC. Protein-surfactant interactions at solid surfaces. In: Horbett TA, Brash JL, editors. Proteins at interfaces II: fundamentals and applications. Washington (DC): American Chemical Society; 1995. p 239–254.
  • Cleland JL, Powell MF, Shire SJ. The development of stable protein formulation: a close look at protein aggregation, deamidation and oxidation. Critic Rev Ther Drug Carrier Sys. 1993;10:307–377.
  • Li S, Schoneich C, Borchardt RT. Chemical pathways of peptide degradation. VIII. Oxidation of methionine in small peptides by prooxidant transition metal ion systems: influence of selective scavengers for reactive oxygen intermediates. Pharm Res. 1995;12:348–355.
  • Miller BL, Hageman MJ, Thamann TJ, et al. Solid state photodegradation of bovine somatotropin (bovine growth hormone): evidence for tryptophan-mediated photooxidation of disulfide bonds. J Pharm Sci. 2003;92:1698–1709.
  • Lam XM, Yang JY, Cleland JL. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J Pharm Sci. 1997;86:1250–1255.
  • Kerwin BA, Akers MJ, Apostol I, et al. Acute and long-term stability studies of deoxy hemoglobin and characterization of ascorbate-induced modifications. J Pharm Sci. 1999;88:79–88.
  • Joo HS, Koo YM, Choi JW, et al. Stabilization method of an alkaline protease from inactivation by heat, SDS and hydrogen peroxide. Enzyme Microb Technol. 2005;36:766–772.
  • Carpenter JF, Chang BS. Lyophilization of protein pharmaceuticals. In: Avis K, Wu V, editors. Biotechnology and biopharmaceutical manufacturing, processing and preservation. Buffalo Grove (IL): Interpharm Press; 1996. p. 199–264.
  • Pikal MJ. Mechanisms of protein stabilization during freeze-drying and storage: the relative importance of thermodynamic stabilization and glassy state relaxation dynamics. In: Rey L, May JC, editors. Freeze-drying/lyophilization of pharmaceutical and biological products. New York (NY): Marcel Dekker; 2004. p. 63–107.
  • Carpenter JF, Chang BS, Garzon-Rodriguez W, et al. Rationale design of stable lyophilized protein formulations: theory and practice. In: Carpenter JF, Manning, MC, editors. Rationale design of stable protein formulations-theory and practice. New York (NY): Kluwer Academic/Plenum Publishers; 2002. p. 13–115.
  • Pyne A, Surana R, Suryanarayanan R. Crystallization of mannitol below Tg′ during freeze-drying in binary and ternary aqueous systems. Pharm Res. 2002;19:901–908.
  • Lam XM, Costantino HR, Overcashier DE, et al. Replacing succinate with glycolate buffer improves the stability of lyophilized interferon- gamma. Int J Pharm. 1996;142:85–95.
  • Pikal-Cleland KA, Cleland JL, Anchrodoquy TJ, et al. Effect of glycine on pH changes and protein stability during freeze-thawing in phosphate buffer systems. J Pharm Sci. 2002;91:1969–1979.
  • Meyer JD, Nayar R, Manning MC. Impact of bulking agents on the stability of a lyophilized monoclonal antibody. Eur J Pharm Sci. 2009;38:29–38.
  • Pikal MJ. Freeze-drying of proteins. In: Cleland JL, Langer R, editors. Formulation and delivery of proteins and peptides. Vol. 567. Dearborn (MI): American Chemical Society; 1994. p. 120–133.
  • Forney-Stevens KM, Bogner RH, Pikal MJ. Addition of amino acids to further stabilize lyophilized sucrose-based protein formulations: I. Screening of 15 amino acids in two model proteins. J Pharm Sci. 2016;105:697–704.
  • Nail SL, Jiang S, Chongprasert S, et al. Fundamentals of freeze-drying In: Nail SL, Akers MJ, editors. Development and manufacture of protein pharmaceuticals. New York (NY): Pharm Biotechnol, Kluwer Academic/Plenum Publisher; 2002. p. 281–360.
  • Jennings TA. Lyophilization, introduction and basic principles. Englewood (CO): Interpharm Press; 1999.
  • Pikal M, Shah S. The collapse temperature in freeze-drying: dependence on measurement methodology and rate of water removal from the glassy phase. Int J Pharm. 1990;62:165–186.
  • Searles JA, Carpenter JF, Randolph T. The ice nucleation temperature determines the primary drying rate of lyophilization for samples frozen on a temperature-controlled shelf. J Pharm Sci. 2001;90:860–871.
  • Franks F, Hatley RHM, Mathias S. Materials science and the production of shelf-stable biologicals. Bio Pharm. 1994;4:38–42.
  • Cleland JL, Lam X, Kendrick B, et al. A specific molar ratio of stabilizer to protein is required for storage stability of a lyophilized monoclonal antibody. J Pharm Sci. 2001;90:310–321.
  • Hsu CC, Nguyen HM, Yeung DA, et al. Surface denaturation at solid-void interface—a possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperature. Pharm Res. 1995;12:69–77.
  • Patahoff TA, Overcashier DE. The importance of freezing on lyophilization cycle development. Bio Pharm. 2002;3:16–21.
  • Williams NA, Guglielmo J, Polli GP, et al. The effects of cooling rate on solid phase transitions and associated vial breakage occurring in frozen mannitol solutions. J Parenter Sci Technol. 1986;40:135–141.
  • Williams NA, Dean T. Vial breakage by frozen mannitol solutions: correlation with thermal characteristics and effect of stereoisomerism, additives, and vial configuration. J Parenter Sci Technol. 1990;44:94–100.
  • Williams NA, Guglielmo J. Thermal mechanical analysis of frozen solutions of mannitol and some related stereoisomers: evidence of expansion during warming and correlation with vial breakage during lyophilization. J Parenter Sci Technol. 1993;47:119–123.
  • Bindschaedler C. Lyophilization process validation In: Rey L, May J, editors. Freeze-drying/lyophilization of pharmaceutical and biological products. New York (NY): Marcel Dekker Inc.; 1999. p. 372–408.
  • Oetjen GW, Haseley P. Freeze-drying. Weinheim, Germany: Wiley-VCH-VerlagGmBH & Co. KGaA; 2004.
  • Jaenicke R. Protein structure and function at low temperatures. Philos Trans R Soc Lond B Biol Sci. 1990;326:535–551.
  • Tang XC, Pikal MJ. The effect of stabilizers and denaturants on the cold denaturation temperatures of proteins and implications for freeze-drying. Pharm Res. 2005;22:1167–1175.
  • Strambini GB, Gabellieri E. Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys J. 1996;70:971–976.
  • Timasheff SN, Arakawa T. Mechanism of protein precipitation and stabilization by co-solvents. J Crystal Growth. 1988;90:39.
  • Carpenter JF, Pikal MJ, Chang BS, et al. Rational design of stable lyophilized protein formulation: some practical advice. Pharm Res. 1997;14:969–975.
  • Passot S, Fonseca F, Barbouche N, et al. Effect of product temperature during primary drying on the long-term stability of lyophilized proteins. Pharm Dev Technol. 2007;12:543–553.
  • Chatterjee K, Shalaev EY, Suryanarayanan R. Partially crystalline systems in lyophilization. II. Withstanding collapse at high primary drying temperatures and impact on protein activity recovery. J Pharm Sci. 2005;94:809–820.
  • Chang BS, Fischer NL. Development of an efficient single step freeze-drying cycle for protein formulations. Pharm Res. 1995;12:831–837.
  • Nail SL. The effect of chamber pressure on heat transfer in the freeze drying of parenteral solutions. J Parenter Drug Assoc. 1980;34:358–368.
  • Livesey RG, Rowe TW. A discussion of the effect of chamber pressure on heat and mass transfer in freeze-drying. J Parenter Sci Technol. 1987;41:169–171.
  • Ohori R, Akita T, Yamashita C. Effect of temperature ramp rate during the primary drying process on the properties of amorphous-based lyophilized cake, Part 2: successful lyophilization by adopting a fast ramp rate during primary drying in protein formulations. Eur J Pharm Biopharm. 2018;130:83–95.
  • Patel MS, Doen T, Pikal MJ. Determination of end point of primary drying in freeze-drying process control. AAPS PharmSciTech. 2010;11:73–84.
  • Pikal MJ, Shah S. Intravial distribution of moisture during the secondary drying stage of freeze drying. PDA J Pharm Sci Technol. 1997;51:17–24.
  • Hageman MJ. Stability of protein pharmaceuticals, part A. Chemical and physical pathways of protein degradation. New York (NY): Plenum; 1992. p. 273–309.
  • Costantino HR, Curley JG, Hsu CC. Determining the water sorption monolayer of freeze-dried pharmaceutical proteins. J Pharm Sci. 1997;86:1390–1938.
  • Rowe AJ. Probing hydration and the stability of protein solutions-a colloid science approach. Biophys Chem. 2001;93:93–101.
  • Hageman MJ. The role of moisture in protein stability. Drug Dev Ind Pharm. 1988;14:2047–2070.
  • Tavornvipas S, Tajiri S, Hirayama F, et al. Effects of hydrophilic cyclodextrins on aggregation of recombinant human growth hormone. Pharm Res. 2004;21:2369–2376.
  • Maher S, Brayden DJ. Overcoming poor permeability: translating permeation enhancers for oral peptide delivery. Drug Discov Today Technol. 2012;9:e113–9.
  • Gupta S, Jain A, Chakraborty M, et al. Oral delivery of therapeutic proteins and peptides: a review on recent developments. Drug Deliv. 2013;20:237–246.
  • Biermasz NR. New medical therapies on the horizon: oral octreotide. Pituitary. 2017;20:149–153.

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:

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:

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.