Serum stability and affinity optimization of an M2 macrophage-targeting peptide (M2pep)

Theranostics

Volumn 6, Issue 9, 2016, Pages 1403-1414

  Ngambenjawong, Chayanon ^a   Gustafson, Heather H ^a   Pineda, Julio M ^a   Kacherovsky, Nataly A ^a   Cieslewicz, Maryelise ^a   Pun, Suzie H ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Binding affinity; Immunomodulation; M2 macrophages; M2pep; Serum stability; Targeted drug delivery

Indexed keywords

ARGINYLTYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLARGINYLTYROSYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSYLLYSINE; BIOTIN DERIVATIVE; CYSTEINYLGLYCYLASPARTYLPROPYLPROPYLGLYCYLVALYLARGINYLTYROSYLTRYPTOPHYLGLYCYLCYSTEINYLLYSYLLYSYLLYSINE; CYSTEINYLGLYCYLASPARTYLPROPYLPROPYLGLYCYLVALYLARGINYLTYROSYLTRYPTOPHYLTYROSYLGLYCYLCYSTEINYLLYSYLLYSYLLYSINE; CYSTEINYLGLYCYLTYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLARGINYLTYROSYLTRYPTOPHYLTYROSYLGLYCYLCYSTEINYLLYSYLLYSYLLYSINE; M2 MACROPHAGE TARGETING PEPTIDE; PEPTIDE DERIVATIVE; TYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLARGINYLTRYPTOPHYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSYLLYSINE; TYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLARGINYLTYROSYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSYLLYSINE; TYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLLYSYLPROPYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSYLLYSINE; TYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLLYSYLTRYPTOPHYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSINE; TYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLLYSYLTRYPTOPHYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSYLLYSINE; TYROSYLGLUTAMYLGLUTAMINYLASPARTYLPROPYLTRYPTOPHYLGLYCYLVALYLLYSYLTYROSYLTRYPTOPHYLTYROSYLGLYCYLGLYCYLGLYCYLSERYLLYSYLLYSYLLYSINE; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; CDK5RAP2 PROTEIN, MOUSE; CELL CYCLE PROTEIN; CYCLOPEPTIDE; DRUG CARRIER;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYCLIZATION; FEMALE; IN VITRO STUDY; IN VIVO STUDY; MACROPHAGE; MOUSE; NONHUMAN; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN STABILITY; TUMOR LOCALIZATION; ANIMAL; BREAST NEOPLASMS; CHEMISTRY; COLONIC NEOPLASMS; DISEASE MODEL; DRUG EFFECTS; METABOLISM; SERUM;

ANIMALS; ANTINEOPLASTIC AGENTS; BREAST NEOPLASMS; CELL CYCLE PROTEINS; COLONIC NEOPLASMS; DISEASE MODELS, ANIMAL; DRUG CARRIERS; MACROPHAGES; MICE; PEPTIDES, CYCLIC; PROTEIN STABILITY; PROTEOLYSIS; SERUM;

EID: 84991573177     PISSN: None     EISSN: 18387640     Source Type: Journal    
DOI: 10.7150/thno.15394     Document Type: Article

References (32)

1. Siegel RL, Miller KD, Jemal A. Cancer Statistics, 2015. CA Cancer J Clin. 2015; 65:5-29
2. Allen TM. Ligand-targeted therapeutics in anticancer therapy. Nat Rev Cancer. 2002; 2: 750-63
3. Sanna V, Pala N, Sechi M. Targeted therapy using nanotechnology: Focus on cancer. Int J Nanomedicine. 2014; 9: 467-83
4. Bartlett DW, Su H, Hildebrandt IJ, Weber WA, Davis ME. Impact of tumor-specific targeting on the biodistribution and efficacy of siRNA nanoparticles measured by multimodality in vivo imaging. Proc Natl Acad Sci U S A. 2007; 104: 15549-54
5. Chari RVJ, Miller ML, Widdison WC. Antibody-drug conjugates: An emerging concept in cancer therapy. Angew Chemie-Int Ed. 2014; 53: 3796-827
6. Srinivasarao M, Galliford CV, Low PS. Principles in the design of ligand-targeted cancer therapeutics and imaging agents. Nat Rev Drug Discov. 2015; 14: 203-19
7. Khoury GA, Smadbeck J, Kieslich CA, Floudas CA. Protein folding and de novo protein design for biotechnological applications. Trends Biotechnol. 2014; 32: 99-109
8. Brown KC. Peptidic tumor targeting agents: the road from phage display peptide selections to clinical applications. Curr Pharm Des. 2010; 16: 1040-54
9. Yu MK, Park J, Jon S. Targeting strategies for multifunctional nanoparticles in cancer imaging and therapy. Theranostics. 2012; 2: 3-44
10. Bertrand N, Wu J, Xu X, Kamaly N, Farokhzad OC. Cancer nanotechnology: The impact of passive and active targeting in the era of modern cancer biology. Adv Drug Deliv Rev. 2014; 66: 2-25
11. Kim J-W, Kim T-D, Hong BS, Kim OY, Yoon W-H, Chae C-B, et al. A serum-stable branched dimeric anti-VEGF peptide blocks tumor growth via anti-angiogenic activity. Exp Mol Med. 2010; 42: 514-23
12. Akcan M, Stroud MR, Hansen SJ, Clark RJ, Daly NL, Craik DJ, et al. Chemical re-engineering of chlorotoxin improves bioconjugation properties for tumor imaging and targeted therapy. J Med Chem. 2011; 54: 782-7
13. Ngambenjawong C, Cieslewicz M, Schellinger JG, Pun SH. Synthesis and evaluation of multivalent M2pep peptides for targeting alternatively activated M2 macrophages. J Control Release. 2016; 224: 103-11
14. Cieslewicz M, Tang J, Yu JL, Cao H, Zavaljevski M, Motoyama K, et al. Targeted delivery of proapoptotic peptides to tumor-associated macrophages improves survival. Proc Natl Acad Sci U S A. 2013; 110: 15919-24
15. Gajewski TF, Schreiber H, Fu Y-X. Innate and adaptive immune cells in the tumor microenvironment. Nat Immunol. 2013; 14: 1014-22
16. Whiteside TL. The tumor microenvironment and its role in promoting tumor growth. Oncogene. 2008; 27: 5904-12
17. Lamagna C, Aurrand-Lions M, Imhof B a. Dual role of macrophages in tumor growth and angiogenesis. J Leukoc Biol. 2006; 80: 705-13
18. Zheng J-S, Tang S, Qi Y-K, Wang Z-P, Liu L. Chemical synthesis of proteins using peptide hydrazides as thioester surrogates. Nat Protoc. 2013; 8: 2483-95
19. Cochran R, Cochran F. Phage display and molecular imaging: expanding fields of vision in living subjects. Biotechnol Genet Eng Rev. 2010; 27: 57-94
20. McGregor DP. Discovering and improving novel peptide therapeutics. Curr Opin Pharmacol. 2008; 8: 616-9
21. Pollaro L, Heinis C. Strategies to prolong the plasma residence time of peptide drugs. Medchemcomm. 2010; 1: 319-24
22. Walensky LD, Bird GH. Hydrocarbon-Stapled Peptides: Principles, Practice, and Progress. J Med Chem. 2014; 57: 6275-88
23. Sahu A, Soulika AM, Morikis D, Spruce L, Moore WT, Lambris JD. Binding kinetics, structure-activity relationship, and biotransformation of the complement inhibitor compstatin. J Immunol. 2000; 165: 2491-9
24. Nguyen LT, Chau JK, Perry NA, de Boer L, Zaat SAJ, Vogel HJ. Serum stabilities of short tryptophan-and arginine-rich antimicrobial peptide analogs. PLoS One. 2010; 5: 1-8
25. Liu GW, Livesay BR, Kacherovsky NA, Cieslewicz M, Lutz E, Waalkes A, et al. Efficient Identification of Murine M2 Macrophage Peptide Targeting Ligands by Phage Display and Next-Generation Sequencing. Bioconjug Chem. 2015; 26: 1811-7
26. Bordo D, Argos P. Suggestions for "safe" residue substitutions in site-directed mutagenesis. J Mol Biol. 1991; 217: 721-9
27. Gallivan JP, Dougherty DA. Cation-pi interactions in structural biology. Proc Natl Acad Sci U S A. 1999; 96: 9459-64
28. Dougherty DA. Cation-pi Interactions Involving Aromatic Amino Acids. J Nutr. 2007; 137: 1504S-1508
29. Hughes RM, Wiggins KR, Khorasanizadeh S, Waters ML. Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect. Proc Natl Acad Sci U S A. 2007; 104: 11184-8
30. Clark RJ, Fischer H, Dempster L, Daly NL, Rosengren KJ, Nevin ST, et al. Engineering stable peptide toxins by means of backbone cyclization: stabilization of the alpha-conotoxin MII. Proc Natl Acad Sci U S A. 2005; 102: 13767-72
31. Kolodziej AF, Zhang Z, Overoye-Chan K, Jacques V, Caravan P. Peptide optimization and conjugation strategies in the development of molecularly targeted magnetic resonance imaging contrast agents. Methods Mol Biol. 2014; 1088: 185-211
32. Laoui D, Movahedi K, Van Overmeire E, Van den Bossche J, Schouppe E, Mommer C, et al. Tumor-associated macrophages in breast cancer: distinct subsets, distinct functions. Int J Dev Biol. 2011; 55:861-7