Early Engineering Approaches to Improve Peptide Developability and Manufacturability

AAPS Journal

Volumn 17, Issue 1, 2015, Pages 111-120

  Furman, Jennifer L ^a   Chiu, Mark ^a   Hunter, Michael J ^a  

^a JANSSEN RESEARCH AND DEVELOPMENT   (Belgium)

Author keywords

developability; peptide; proteolysis; PTM risk

Indexed keywords

AMINO ACID; ASPARAGINE; ASPARTIC ACID; COLONY STIMULATING FACTOR 1; CORTICOTROPIN RELEASING FACTOR RECEPTOR; CYCLOSPORIN; CYSTEINE; DESMOPRESSIN; DIPEPTIDYL PEPTIDASE IV; G PROTEIN COUPLED RECEPTOR; GLUCAGON LIKE PEPTIDE 1; LINACLOTIDE; LIRAGLUTIDE; MEMBRANE METALLOENDOPEPTIDASE; MEMBRANE PROTEIN; METHIONINE; MONOCLONAL ANTIBODY; OCTREOTIDE; PEPTIDE; POLYMER; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; TESAMORELIN; TRYPTOPHAN; VOLTAGE GATED POTASSIUM CHANNEL;

AMINO ACID SEQUENCE; ARTICLE; CELL FREE SYSTEM; DEAMINATION; DECISION MAKING; DISULFIDE BOND; DOWNSTREAM PROCESSING; DRUG BIOAVAILABILITY; DRUG CLEARANCE; DRUG DEVELOPMENT; DRUG EFFICACY; DRUG HALF LIFE; DRUG SOLUBILITY; ENTROPY; HIV ASSOCIATED LIPODYSTROPHY; HYDROLYSIS; IC50; IMMUNOGENICITY; ISOMERIZATION; KIDNEY CLEARANCE; OXIDATION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; SEQUENCE ANALYSIS; CHEMISTRY; DRUG DESIGN; HALF LIFE TIME; HUMAN; PROCEDURES; PROTEIN ENGINEERING;

ANTIBODIES, MONOCLONAL; DRUG DESIGN; HALF-LIFE; HUMANS; PEPTIDES; PROTEIN ENGINEERING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; SEQUENCE ANALYSIS;

EID: 84922090937     PISSN: None     EISSN: 15507416     Source Type: Journal    
DOI: 10.1208/s12248-014-9681-9     Document Type: Article

References (71)

1. Diao L, Meibohm B. Pharmacokinetics and pharmacokinetic-pharmacodynamic correlations of therapeutic peptides. Clin Pharmacokinet. 2013;52(10):855–68.
2. Bruckdorfer T, Marder O, Albericio F. From production of peptides in milligram amounts for research to multi-tons quantities for drugs of the future. Curr Pharm Biotechnol. 2004;5(1):29–43.
3. Vlieghe P et al. Synthetic therapeutic peptides: science and market. Drug Discov Today. 2010;15(1–2):40–56.
4. Adessi C, Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem. 2002;9(9):963–78.
5. Witt KA et al. Peptide drug modifications to enhance bioavailability and blood–brain barrier permeability. Peptides. 2001;22(12):2329–43.
6. Renukuntla J et al. Approaches for enhancing oral bioavailability of peptides and proteins. Int J Pharm. 2013;447(1–2):75–93.
7. Sato AK et al. Therapeutic peptides: technological advances driving peptides into development. Curr Opin Biotechnol. 2006;17(6):638–42.
8. Latham PW. Therapeutic peptides revisited. Nat Biotechnol. 1999;17(8):755–7.
9. Luckett S et al. High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. J Mol Biol. 1999;290(2):525–33.
10. Kalman K et al. ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem. 1998;273(49):32697–707.
11. Rauer H et al. Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J Biol Chem. 1999;274(31):21885–92.
12. Pennington MW et al. Role of disulfide bonds in the structure and potassium channel blocking activity of ShK toxin. Biochemistry. 1999;38(44):14549–58.
13. Pennington MW et al. Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes. Mol Pharmacol. 2009;75(4):762–73.
14. Grace CR et al. Common and divergent structural features of a series of corticotropin releasing factor-related peptides. J Am Chem Soc. 2007;129(51):16102–14.
15. Fasano A. Innovative strategies for the oral delivery of drugs and peptides. Trends Biotechnol. 1998;16(4):152–7.
16. Patel MM et al. Getting into the brain: approaches to enhance brain drug delivery. CNS Drugs. 2009;23(1):35–58.
17. Lalatsa A, Schatzlein AG, Uchegbu IF. Strategies to deliver peptide drugs to the brain. Mol Pharm. 2014;11(4):1081–93.
18. Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem. 1987;262(2):785–94.
19. Aswad DW. Deamidation and isoaspartate formation in peptides and proteins. In: Aswad DW, editor. CRC series in analytical Biotechnology. Boca Raton: CRC; 1994.
20. Stephenson RC, Clarke S. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem. 1989;264(11):6164–70.
21. Di Donato A, Galletti P, D’Alessio G. Selective deamidation and enzymatic methylation of seminal ribonuclease. Biochemistry. 1986;25(26):8361–8.
22. Di Donato A et al. Selective deamidation of ribonuclease A. Isolation and characterization of the resulting isoaspartyl and aspartyl derivatives. J Biol Chem. 1993;268(7):4745–51.
23. Johnson BA, Aswad DW. Fragmentation of isoaspartyl peptides and proteins by carboxypeptidase Y: release of isoaspartyl dipeptides as a result of internal and external cleavage. Biochemistry. 1990;29(18):4373–80.
24. Blomback B. Derivatives of glutamine in peptides. Methods Enzymol. 1967;11:398–411.
25. Dick Jr LW et al. Determination of the origin of the N-terminal pyro-glutamate variation in monoclonal antibodies using model peptides. Biotechnol Bioeng. 2007;97(3):544–53.
26. Dunkelberger EB et al. Deamidation accelerates amyloid formation and alters amylin fiber structure. J Am Chem Soc. 2012;134(30):12658–67.
27. Ni W et al. Analysis of isoaspartic acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry. Anal Chem. 2010;82(17):7485–91.
28. 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.
29. Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem. 1997;272(33):20313–6.
30. Brot N, Weissbach H. Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch Biochem Biophys. 1983;223(1):271–81.
31. Swaim MW, Pizzo SV. Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors. J Leukoc Biol. 1988;43(4):365–79.
32. Schechter Y. Selective oxidation and reduction of methionine residues in peptides and proteins by oxygen exchange between sulfoxide and sulfide. J Biol Chem. 1986;261:66–70.
33. Hiller KO, Asmus KD. Oxidation of methionine by X2.- in aqueous solution and characterization of some S therefore X three-electron bonded intermediates. A pulse radiolysis study. Int J Radiat Biol Relat Stud Phys Chem Med. 1981;40(6):583–95.
34. Keck RG. The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal Biochem. 1996;236(1):56–62.
35. Creed D. The photophysics and photochemistry of the near-uv absorbing amino acids—I. tryptophan and its simple derivatives. Photochem Photobiol. 1984;39(4):537–62.
36. + channels. Eur J Biochem. 2003;270(17):3583–92.
37. Benham CJ, Jafri MS. Disulfide bonding patterns and protein topologies. Protein Sci. 1993;2(1):41–54.
38. Luo S et al. Characterization of a novel alpha-conotoxin from conus textile that selectively targets alpha6/alpha3beta2beta3 nicotinic acetylcholine receptors. J Biol Chem. 2013;288(2):894–902.
39. Kutchukian PS et al. All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples. J Am Chem Soc. 2009;131(13):4622–7.
40. Barnham KJ et al. Role of the 6-20 disulfide bridge in the structure and activity of epidermal growth factor. Protein Sci. 1998;7(8):1738–49.
41. Flinn JP et al. Role of disulfide bridges in the folding, structure and biological activity of omega-conotoxin GVIA. Biochim Biophys Acta. 1999;1434(1):177–90.
42. Carrega L et al. The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily. Proteins. 2005;61(4):1010–23.
43. Han TS et al. Structurally minimized mu-conotoxin analogues as sodium channel blockers: implications for designing conopeptide-based therapeutics. ChemMedChem. 2009;4(3):406–14.
44. Khoo KK et al. Structure of the analgesic mu-conotoxin KIIIA and effects on the structure and function of disulfide deletion. Biochemistry. 2009;48(6):1210–9.
45. Hagihara Y et al. Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI). J Biol Chem. 2002;277(52):51043–8.
46. Schrier JA et al. Degradation pathways for recombinant human macrophage colony-stimulating factor in aqueous solution. Pharm Res. 1993;10(7):933–44.
47. Clarke S, Stephenson RC, Lowenson JD. In: Ahern TJ, Manning MC, editors. Stability of protein pharmaceuticals. Part A—chemical and physical pathways of protein degradation. New York: Plenum; 1992.
48. Tyler-Cross R, Schirch V. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J Biol Chem. 1991;266(33):22549–56.
49. Inglis AS. Cleavage at aspartic acid. Methods Enzymol. 1983;91:324–32.
50. Bauer W et al. SMS 201-995: a very potent and selective octapeptide analogue of somatostatin with prolonged action. Life Sci. 1982;31(11):1133–40.
51. Maurer R et al. Opiate antagonistic properties of an octapeptide somatostatin analog. Proc Natl Acad Sci U S A. 1982;79(15):4815–7.
52. Oliyai C, Borchardt RT. Chemical pathways of peptide degradation. IV. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide. Pharm Res. 1993;10(1):95–102.
53. Larsen PJ et al. Systemic administration of the long-acting GLP-1 derivative NN2211 induces lasting and reversible weight loss in both normal and obese rats. Diabetes. 2001;50(11):2530–9.
54. Wang Y, Tomlinson B. Tesamorelin, a human growth hormone releasing factor analogue. Expert Opin Investig Drugs. 2009;18(3):303–10.
55. Ferdinandi ES et al. Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue. Basic Clin Pharmacol Toxicol. 2007;100(1):49–58.
56. Busby RW et al. Pharmacologic properties, metabolism, and disposition of linaclotide, a novel therapeutic peptide approved for the treatment of irritable bowel syndrome with constipation and chronic idiopathic constipation. J Pharmacol Exp Ther. 2013;344(1):196–206.
57. Italia JL et al. PLGA nanoparticles for oral delivery of cyclosporine: nephrotoxicity and pharmacokinetic studies in comparison to Sandimmune Neoral. J Control Release. 2007;119(2):197–206.
58. Ilan E et al. Improved oral delivery of desmopressin via a novel vehicle: mucoadhesive submicron emulsion. Pharm Res. 1996;13(7):1083–7.
59. Henchey LK, Jochim AL, Arora PS. Contemporary strategies for the stabilization of peptides in the alpha-helical conformation. Curr Opin Chem Biol. 2008;12(6):692–7.
60. Veronese FM, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov Today. 2005;10(21):1451–8.
61. Yang BB et al. Polyethylene glycol modification of filgrastim results in decreased renal clearance of the protein in rats. J Pharm Sci. 2004;93(5):1367–73.
62. Webster R et al. PEGylated proteins: evaluation of their safety in the absence of definitive metabolism studies. Drug Metab Dispos. 2007;35(1):9–16.
63. Rudmann DG et al. High molecular weight polyethylene glycol cellular distribution and PEG-associated cytoplasmic vacuolation is molecular weight dependent and does not require conjugation to proteins. Toxicol Pathol. 2013;41(7):970–83.
64. Schellekens H, Hennink WE, Brinks V. The immunogenicity of polyethylene glycol: facts and fiction. Pharm Res. 2013;30(7):1729–34.
65. Kim DM et al. Fc fusion to glucagon-like peptide-1 inhibits degradation by human DPP-IV, increasing its half-life in serum and inducing a potent activity for human GLP-1 receptor activation. BMB Rep. 2009;42(4):212–6.
66. Alters SE et al. GLP2-2G-XTEN: a pharmaceutical protein with improved serum half-life and efficacy in a rat Crohn’s disease model. PLoS One. 2012;7(11):e50630.
67. Haeckel A et al. XTEN-annexin A5: XTEN allows complete expression of long-circulating protein-based imaging probes as recombinant alternative to PEGylation. J Nucl Med. 2014;55(3):508–14.
68. Murray CJ, Baliga R. Cell-free translation of peptides and proteins: from high throughput screening to clinical production. Curr Opin Chem Biol. 2013;17(3):420–6.
69. Harris DC, Jewett MC. Cell-free biology: exploiting the interface between synthetic biology and synthetic chemistry. Curr Opin Biotechnol. 2012;23(5):672–8.
70. Hipolito CJ, Suga H. Ribosomal production and in vitro selection of natural product-like peptidomimetics: the FIT and RaPID systems. Curr Opin Chem Biol. 2012;16(1–2):196–203.
71. Zawada JF et al. Microscale to manufacturing scale-up of cell-free cytokine production—a new approach for shortening protein production development timelines. Biotechnol Bioeng. 2011;108(7):1570–8.