Biological activities of histidine-rich peptides; merging biotechnology and nanomedicine

Microbial Cell Factories

Volumn 10, Issue , 2011, Pages

  Ferrer Miralles, Neus ^a,b   Corchero, José L ^a,b   Kumar, Pradeep ^c   Cedano, Juan A ^d   Gupta, Kailash C ^e   Villaverde, Antonio ^a,b   Vazquez, Esther ^a,b  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b BIOMATERIALES Y NANOMEDICINA CIBER BBN   (Spain)

^c CSIR INSTITUTE OF GENOMICS AND INTEGRATIVE BIOLOGY   (India)

^d UNIVERSIDAD DE LA REPÚBLICA   (Uruguay)

^e CSIR INDIAN INSTITUTE OF TOXICOLOGY RESEARCH   (India)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE RICH PEPTIDE; PEPTIDE; UNCLASSIFIED DRUG; HISTIDINE;

BIOLOGICAL ACTIVITY; BIOTECHNOLOGY; ENDOSOME; NANOMEDICINE; NOTE; PROTEIN ENGINEERING; PROTEIN PURIFICATION; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; HUMAN; METABOLISM; METHODOLOGY; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; BIOTECHNOLOGY; HISTIDINE; HUMANS; MOLECULAR SEQUENCE DATA; NANOMEDICINE; PEPTIDES; PROTEIN ENGINEERING;

EID: 82455171791     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-10-101     Document Type: Note

References (55)

1. Waugh DS. Making the most of affinity tags. Trends Biotechnol 2005, 23:316-320. 10.1016/j.tibtech.2005.03.012, 15922084.
2. Kimple ME, Sondek J. Overview of affinity tags for protein purification. Curr Protoc Protein Sci 2004, Chapter 9. Unit 9.9.
3. Arnau J, Lauritzen C, Petersen GE, Pedersen J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr Purif 2006, 48:1-13. 10.1016/j.pep.2005.12.002, 16427311.
4. Waugh DS. An overview of enzymatic reagents for the removal of affinity tags. Protein Expr Purif 2011, 80:283-293. 10.1016/j.pep.2011.08.005, 21871965.
5. Li Y. Self-cleaving fusion tags for recombinant protein production. Biotechnol Lett 2011, 33:869-881. 10.1007/s10529-011-0533-8, 21267760.
6. Fong BA, Wood DW. Expression and purification of ELP-intein-tagged target proteins in high cell density E. coli fermentation. Microb Cell Fact 2010, 9:77. 10.1186/1475-2859-9-77, 2978133, 20959011.
7. Wood DW, Wu W, Belfort G, Derbyshire V, Belfort M. A genetic system yields self-cleaving inteins for bioseparations. Nat Biotechnol 1999, 17:889-892. 10.1038/12879, 10471931.
8. Wu WY, Mee C, Califano F, Banki R, Wood DW. Recombinant protein purification by self-cleaving aggregation tag. Nat Protoc 2006, 1:2257-2262. 10.1038/nprot.2006.314, 17406465.
9. Carson M, Johnson DH, McDonald H, Brouillette C, Delucas LJ. His-tag impact on structure. Acta Crystallogr D Biol Crystallogr 2007, 63:295-301. 10.1107/S0907444906052024, 17327666.
10. Wang Z, Li H, Guan W, Ling H, Wang Z, Mu T, et al. Human SUMO fusion systems enhance protein expression and solubility. Protein Expr Purif 2010, 73:203-208. 10.1016/j.pep.2010.05.001, 20457256.
11. Sun QM, Chen LL, Cao L, Fang L, Chen C, Hua ZC. An improved strategy for high-level production of human vasostatin120-180. Biotechnol Prog 2005, 21:1048-1052.
12. Tang W, Sun ZY, Pannell R, Gurewich V, Liu JN. An efficient system for production of recombinant urokinase-type plasminogen activator. Protein Expr Purif 1997, 11:279-283. 10.1006/prep.1997.0800, 9425632.
13. Nallamsetty S, Waugh DS. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr Purif 2006, 45:175-182. 10.1016/j.pep.2005.06.012, 16168669.
14. Stefan A, Conti M, Rubboli D, Ravagli L, Presta E, Hochkoeppler A. Overexpression and purification of the recombinant diphtheria toxin variant CRM197 in Escherichia coli. J Biotechnol 2011, (156):245-252.
15. Li Y. The tandem affinity purification technology: an overview. Biotechnol Lett 2011, 33:1487-1499. 10.1007/s10529-011-0592-x, 21424840.
16. Li Y. Commonly used tag combinations for tandem affinity purification. Biotechnol Appl Biochem 2010, 55:73-83. 10.1042/BA20090273, 20156193.
17. Hochuli E, Bannwarth W, Dobeli H, Gentz R, Stuber D. Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate Adsorbent. Nat Biotech 1988, 6:1321-1325.
18. Block H, Kubicek J, Labahn J, Roth U, Schafer F. Production and comprehensive quality control of recombinant human Interleukin-1beta: a case study for a process development strategy. Protein Expr Purif 2008, 57:244-254. 10.1016/j.pep.2007.09.019, 18053740.
19. Porath J, Carlsson J, Olsson I, Belfrage G. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 1975, 258:598-599. 10.1038/258598a0, 1678.
20. Porath J. Immobilized metal ion affinity chromatography. Protein Expr Purif 1992, 3:263-281. 10.1016/1046-5928(92)90001-D, 1422221.
21. Gaberc-Porekar V, Menart V. Perspectives of immobilized-metal affinity chromatography. J Biochem Biophys Methods 2001, 49:335-360. 10.1016/S0165-022X(01)00207-X, 11694288.
22. Hochuli E, Dobeli H, Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J Chromatogr 1987, 411:177-184.
23. Knecht S, Ricklin D, Eberle AN, Ernst B. Oligohis-tags: mechanisms of binding to Ni2+-NTA surfaces. J Mol Recognit 2009, 22:270-279. 10.1002/jmr.941, 19235144.
24. Patwardhan AV. Selection of optimum affinity tags from a phage-displayed peptide library Application to immobilized copper(II) affinity chromatography. J Chromatograph A 1997, (787):91-100.
25. Vazquez E, Ferrer-Miralles N, Villaverde A. Peptide-assisted traffic engineering for nonviral gene therapy. Drug Discov Today 2008, 13:1067-1074. 10.1016/j.drudis.2008.08.008, 18801457.
26. Behr JP. The Proton Sponge: a Trick to Enter Cells the Viruses Did Not Exploit. Chimia 1997, 51:34-36.
27. Lo SL, Wang S. An endosomolytic Tat peptide produced by incorporation of histidine and cysteine residues as a nonviral vector for DNA transfection. Biomaterials 2008, 29:2408-2414. 10.1016/j.biomaterials.2008.01.031, 18295328.
28. Midoux P, Kichler A, Boutin V, Maurizot JC, Monsigny M. Membrane permeabilization and efficient gene transfer by a peptide containing several histidines. Bioconjug Chem 1998, 9:260-267. 10.1021/bc9701611, 9548543.
29. Kumar VV, Pichon C, Refregiers M, Guerin B, Midoux P, Chaudhuri A. Single histidine residue in head-group region is sufficient to impart remarkable gene transfection properties to cationic lipids: evidence for histidine-mediated membrane fusion at acidic pH. Gene Ther 2003, 10:1206-1215. 10.1038/sj.gt.3301979, 12858185.
30. Kichler A, Leborgne C, Danos O, Bechinger B. Characterization of the gene transfer process mediated by histidine-rich peptides. J Mol Med 2007, 85:191-201. 10.1007/s00109-006-0119-4, 17111132.
31. Vazquez E, Cubarsi R, Unzueta U, Roldan M, Domingo-Espin J, Ferrer-Miralles N, et al. Internalization and kinetics of nuclear migration of protein-only, arginine-rich nanoparticles. Biomaterials 2010, 31:9333-9339. 10.1016/j.biomaterials.2010.08.065, 20869766.
32. Vazquez E, Roldan M, ez-Gil C, Unzueta U, Domingo-Espin J, Cedano J, et al. Protein nanodisk assembling and intracellular trafficking powered by an arginine-rich (R9) peptide. Nanomedicine (Lond) 2010, 5:259-268.
33. Vazquez E, Villaverde A. Engineering building blocks for self-assembling protein nanoparticles. Microb Cell Fact 2010, 9:101. 10.1186/1475-2859-9-101, 3022712, 21192790.
34. Villaverde A. Nanotechnology, bionanotechnology and microbial cell factories. Microb Cell Fact 2010, 9:53. 10.1186/1475-2859-9-53, 2916890, 20602780.
35. Khan F, He M, Taussig MJ. Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ni-nitrilotriacetic acid surfaces. Anal Chem 2006, 78:3072-3079. 10.1021/ac060184l, 16642995.
36. Jung HJ, Kim SK, Min WK, Lee SS, Park K, Park YC, et al. Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli. Bioprocess Biosyst Eng 2011, (34):833-839.
37. Hofstrom C, Orlova A, Altai M, Wangsell F, Graslund T, Tolmachev V. Use of a HEHEHE purification tag instead of a hexahistidine tag improves biodistribution of affibody molecules site-specifically labeled with (99m)Tc, (111)In, and (125)I. J Med Chem 2011, 54:3817-3826. 10.1021/jm200065e, 21524142.
38. Schaefer G, Haber L, Crocker LM, Shia S, Shao L, Dowbenko D, et al. A Two-in-One Antibody against HER3 and EGFR Has Superior Inhibitory Activity Compared with Monospecific Antibodies. Cancer Cell 2011, 20:472-486. 10.1016/j.ccr.2011.09.003, 22014573.
39. Cheng Z, Biechele T, Wei Z, Morrone S, Moon RT, Wang L, et al. Crystal structures of the extracellular domain of LRP6 and its complex with DKK1. Nat Struct Mol Biol 2011, 18:1204-1210. 10.1038/nsmb.2139, 21984209.
40. Abramczyk O, Tavares CD, Devkota AK, Ryazanov AG, Turk BE, Riggs AF, et al. Purification and characterization of tagless recombinant human elongation factor 2 kinase (eEF-2K) expressed in Escherichia coli. Protein Expr Purif 2011, 79:237-244. 10.1016/j.pep.2011.05.005, 21605678.
41. Yeliseev A, Zoubak L, Gawrisch K. Use of dual affinity tags for expression and purification of functional peripheral cannabinoid receptor. Protein Expr Purif 2007, 53:153-163. 10.1016/j.pep.2006.12.003, 1906715, 17223358.
42. Gehrmann M, Doss BT, Wagner M, Zettlitz KA, Kontermann RE, Foulds G, et al. A novel expression and purification system for the production of enzymatic and biologically active human granzyme B. J Immunol Methods 2011, 371:8-17. 10.1016/j.jim.2011.06.007, 21723287.
43. Das KM, Banerjee S, Shekhar N, Damodaran K, Nair R, Somani S, et al. Cloning, Soluble Expression and Purification of High Yield Recombinant hGMCSF in Escherichia coli. Int J Mol Sci 2011, 12:2064-2076. 10.3390/ijms12032064, 3111651, 21673940.
44. McKenzie DL, Smiley E, Kwok KY, Rice KG. Low molecular weight disulfide cross-linking peptides as nonviral gene delivery carriers. Bioconjug Chem 2000, 11:901-909. 10.1021/bc000056i, 11087340.
45. Midoux P, Kichler A, Boutin V, Maurizot JC, Monsigny M. Membrane permeabilization and efficient gene transfer by a peptide containing several histidines. Bioconjug Chem 1998, 9:260-267. 10.1021/bc9701611, 9548543.
46. Ashley CE, Carnes EC, Phillips GK, Durfee PN, Buley MD, Lino CA, et al. Cell-specific delivery of diverse cargos by bacteriophage MS2 virus-like particles. ACS Nano 2011, 5:5729-5745. 10.1021/nn201397z, 21615170.
47. Moore NM, Sheppard CL, Barbour TR, Sakiyama-Elbert SE. The effect of endosomal escape peptides on in vitro gene delivery of polyethylene glycol-based vehicles. J Gene Med 2008, 10:1134-1149. 10.1002/jgm.1234, 18642401.
48. Tarwadi, Jazayeri JA, Prankerd RJ, Pouton CW. Preparation and in vitro evaluation of novel lipopeptide transfection agents for efficient gene delivery. Bioconjug Chem 2008, 19:940-950. 10.1021/bc700463q, 18333604.
49. Kichler A, Leborgne C, Danos O, Bechinger B. Characterization of the gene transfer process mediated by histidine-rich peptides. J Mol Med 2007, 85:191-201. 10.1007/s00109-006-0119-4, 17111132.
50. Chang KL, Higuchi Y, Kawakami S, Yamashita F, Hashida M. Efficient gene transfection by histidine-modified chitosan through enhancement of endosomal escape. Bioconjug Chem 2010, 21:1087-1095. 10.1021/bc1000609, 20499901.
51. Chang KL, Higuchi Y, Kawakami S, Yamashita F, Hashida M. Development of lysine-histidine dendron modified chitosan for improving transfection efficiency in HEK293 cells. J Control Release 2011, 156:195-202. 10.1016/j.jconrel.2011.07.021, 21802461.
52. Yamano S, Dai J, Yuvienco C, Khapli S, Moursi AM, Montclare JK. Modified Tat peptide with cationic lipids enhances gene transfection efficiency via temperature-dependent and caveolae-mediated endocytosis. J Control Release 2011, 152:278-285. 10.1016/j.jconrel.2011.02.004, 21315780.
53. Gu J, Wang X, Jiang X, Chen Y, Chen L, Fang X, et al. Self-assembled carboxymethyl poly (l-histidine) coated poly (beta-amino ester)/DNA complexes for gene transfection. Biomaterials 2012, 33:644-658. 10.1016/j.biomaterials.2011.09.076, 22030282.
54. Tanaka K, Kanazawa T, Ogawa T, Suda Y, Takashima Y, Fukuda T, et al. A novel, bio-reducible gene vector containing arginine and histidine enhances gene transfection and expression of plasmid DNA. Chem Pharm Bull (Tokyo) 2011, 59:202-207.
55. Hatefi A, Megeed Z, Ghandehari H. Recombinant polymer-protein fusion: a promising approach towards efficient and targeted gene delivery. J Gene Med 2006, 8:468-476. 10.1002/jgm.872, 16416505.