Concentration effects on peptide elution from pendant PEO layers

Colloids and Surfaces B: Biointerfaces

Volumn 118, Issue , 2014, Pages 210-217

  Wu, Xiangming ^a   Ryder, Matthew P ^a   McGuire, Joseph ^a   Schilke, Karl F ^a  

^a Oregon State University   (United States)

Author keywords

Cationic amphiphilic peptides; Circular dichroism (CD); Coiled coils; PEO brush; Peptide elution; Polyarginine; WLBU2; Helix

Indexed keywords

AMINO ACIDS; BRUSHES; DICHROISM; DRUG DELIVERY; HYDROPHOBICITY; MODULATION; POLYETHYLENE OXIDES; POLYETHYLENES; ULTRAVIOLET SPECTROSCOPY;

AMPHIPHILIC PEPTIDES; COILED COIL; PEO-BRUSH; POLYARGININE; WLBU2;

PEPTIDES;

MACROGOL; NANOPARTICLE; PENDANT POLYETHYLENE OXIDE; PEPTIDE; PEPTIDE S WLBU2; PEPTIDE WLBU2; POLYARGININE; SILICA NANOPARTICLE; SILICON DIOXIDE; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; MACROGOL DERIVATIVE; WLBU2 PEPTIDE;

ALPHA HELIX; AMPHOPHILICITY; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DENSITY GRADIENT; DRUG DELIVERY SYSTEM; ELUTION; HYDROPHOBICITY; PEPTIDE ELUTION; PEPTIDE PEPTIDE INTERACTION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; QUARTZ CRYSTAL MICROBALANCE; ULTRAVIOLET SPECTROSCOPY; ADSORPTION; AMINO ACID SEQUENCE; CHEMISTRY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SURFACE PROPERTY;

ADSORPTION; AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; CIRCULAR DICHROISM; MOLECULAR SEQUENCE DATA; NANOPARTICLES; PEPTIDES; POLYETHYLENE GLYCOLS; PROTEIN STRUCTURE, SECONDARY; QUARTZ CRYSTAL MICROBALANCE TECHNIQUES; SURFACE PROPERTIES;

EID: 84900816020     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2014.03.056     Document Type: Article

References (44)

1. Wu X., Ryder M.P., McGuire J., Schilke K.F. Adsorption, structural alteration and elution of peptides at pendant PEO layers. Colloids Surf. B: Biointerf. 2013, 112:23-29.
2. Costa F., Carvalho I.F., Montelaro R.C., Gomes P., Martins M.C.L. Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces. Acta Biomater. 2011, 7:1431-1440.
3. Deslouches B., Gonzalez I.A., DeAlmeida D., Islam K., Steele C., Montelaro R.C., Mietzner T.A. De novo-derived cationic antimicrobial peptide activity in a murine model of Pseudomonas aeruginosa bacteraemia. J. Antimicrob. Chemother. 2007, 60:669-672.
4. Deslouches B., Islam K., Craigo J.K., Paranjape S.M., Montelaro R.C., Mietzner T.A. Activity of the de novo engineered antimicrobial peptide WLBU2 against Pseudomonas aeruginosa in human serum and whole blood: implications for systemic applications. Antimicrob. Agents Chemother. 2005, 49:3208-3216.
5. Deslouches B., Phadke S.M., Lazarevic V., Cascio M., Islam K., Montelaro R.C., Mietzner T.A. De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. Antimicrob. Agents Chemother. 2005, 49:316-322.
6. Gonzalez I.A., Wong X.X., De Almeida D., Yurko R., Watkins S., Islam K., Montelaro R.C., El-Ghannam A., Mietzner T.A. Peptides as potent antimicrobials Itethered to a solid surface: implications for medical devices. Nature Precedings. Preced. 2008, http://hdl.handle.net/10101/npre.2008.1967.1.
7. Onaizi S.A., Leong S.S.J. Tethering antimicrobial peptides: current status and potential challenges. Biotechnol. Adv. 2011, 29:67-74.
8. Skinner M.C., Kiselev A.O., Isaacs C.E., Mietzner T.A., Montelaro R.C., Lampe M.F. Evaluation of WLBU2 peptide and 3-O-octyl-sn-glycerol lipid as active ingredients for a topical microbicide formulation targeting Chlamydia trachomatis. Antimicrob. Agents Chemother. 2010, 54:627-636.
9. Adzhubei A.A., Sternberg M.J.E., Makarov A.A. Polyproline-II helix in proteins: structure and function. J. Mol. Biol. 2013, 425:2100-2132.
10. Bochicchio B., Tamburro A.M. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality 2002, 14:782-792.
11. 1-helix, and β-sheet Ψ angle energy landscape in poly-l-lysine and Poly-l-glutamic acid. J. Am. Chem. Soc. 2005, 127:7712-7720.
12. Rifkind J.M. Helix-coil transition of poly-l-arginine: a comparison with other basic polypeptides. Biopolymers 1969, 8:685-688.
13. Tiffany M.L., Krimm S. Circular dichroism of the "random" polypeptide chain. Biopolymers 1969, 8:347-359.
14. DeJohng W.H., Borm P.J.A. Drug delivery and nanoparticles: applications and hazards. Int. J. Nanomed. 2008, 3:133-149.
15. Li S.-D., Huang L. Pharmacokinetics and biodistribution of nanoparticles. Mol. Pharm. 2008, 5:496-504.
16. Pisanic T.R., Blackwell J.D., Shubayev V.I., Finones R.R., Jin S. Nanotoxicity of iron oxide nanoparticle internalization in growing neurons. Biomaterials 2007, 28:2572-2581.
17. Ryder M.P., Schilke K.F., Auxier J.A., McGuire J., Neff J.A. Nisin adsorption to polyethylene oxide layers and its resistance to elution in the presence of fibrinogen. J. Colloid Interface Sci. 2010, 350:194-199.
18. Schilke K.F., McGuire J. Detection of nisin and fibrinogen adsorption on poly (ethylene oxide) coated polyurethane surfaces by time-of-flight secondary ion mass spectrometry (TOF-SIMS). J. Colloid Interface Sci. 2011, 358:14-24.
19. MuÈller R.H., MaÈder K., Gohla S. Solid lipid nanoparticles (SLN) for controlled drug delivery - a review of the state of the art. Eur. J. Pharm. Biopharm. 2000, 50:161-177.
20. Huang X., Brazel C.S. On the importance and mechanisms of burst release in matrix-controlled drug delivery systems. J. Control. Release 2001, 73:121-136.
21. Lampi M.C., Wu X., Schilke K.F., McGuire J. Structural attributes affecting peptide entrapment in PEO brush layers. Colloids Surf. B: Biointerf. 2013, 106:79-85.
22. ® F108. J. Colloid Interface Sci. 2008, 322:104-111.
23. Dill J.K., Auxier J.A., Schilke K.F., McGuire J. Quantifying nisin adsorption behavior at pendant PEO layers. J. Colloid Interface Sci. 2013, 395:300-305.
24. Lee H., Kim D.H., Witte K.N., Ohn K., Choi J., Akgun B., Satija S., Won Y.-Y. Water is a poor solvent for densely grafted poly(ethylene oxide) chains: a conclusion drawn from a self-consistent field theory-based analysis of neutron reflectivity and surface pressure - area isotherm data. J. Phys. Chem. B 2012, 116:7367-7378.
25. Parry D.A.D., Fraser R.D.B., Squire J.M. Fifty years of coiled-coils and α-helical bundles: a close relationship between sequence and structure. J. Struct. Biol. 2008, 163:258-269.
26. Zhou N.E., Kay C.M., Hodges R.S. Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 1992, 267:2664-2670.
27. Zhou N.E., Kay C.M., Hodges R.S. Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil. Biochemistry (Mosc.) 1992, 31:5739-5746.
28. Grigoryan G., Keating A.E. Structural specificity in coiled-coil interactions. Curr. Opin. Struct. Biol. 2008, 18:477-483.
29. Rubinov B., Wagner N., Rapaport H., Ashkenasy G. Self-replicating amphiphilic beta-sheet peptides. Angew. Chem. Int. Ed. Engl. 2009, 48:6683-6686.
30. Wang K., Keasling J.D., Muller S.J. Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides. Int. J. Biol. Macromol. 2005, 36:232-240.
31. Greenfield N.J. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 1996, 235:1-10.
32. Greenfield N.J., Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry (Mosc.) 1969, 8:4108-4116.
33. Whitmore L., Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 2004, 32:W668-W673.
34. Whitmore L., Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89:392-400.
35. Cooper T.M., Woody R.W. The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin. Biopolymers 1990, 30:657-676.
36. Cukalevski R., Lundqvist M., Oslakovic C., Dahlback B., Linse S., Cedervall T. Structural changes in apolipoproteins bound to nanoparticles. Langmuir 2011, 27:14360-14369.
37. Fiumara F., Fioriti L., Kandel E.R., Hendrickson W.A. Essential role of coiled coils for aggregation and activity of Q/N-rich prions and polyQ proteins. Cell 2010, 143:1121-1135.
38. Lazo N.D., Downing D.T. Circular dichroism of model peptides emulating the amphipathic α-helical regions of intermediate filaments. Biochemistry (Mosc.) 1997, 36:2559-2565.
39. Potekhin S.A., Melnik T.N., Popov V., Lanina N.F., Vazina A.A., Rigler P., Verdini A.S., Corradin G., Kajava A.V. De novo design of fibrils made of short α-helical coiled coil peptides. Chem. Biol. 2001, 8:1025-1032.
40. Schneider J.P., Kelly J.W. Templates that induce α-helical, β-sheet, and loop conformations. Chem. Rev. 1995, 95:2169-2187.
41. Höök F., Kasemo B., Nylander T., Fant C., Sott K., Elwing H. Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: a quartz crystal microbalance with dissipation monitoring ellipsometry, and surface plasmon resonance study. Anal. Chem. 2001, 73:5796-5804.
42. Höök F., Vörös J., Rodahl M., Kurrat R., Böni P., Ramsden J.J., Textor M., Spencer N.D., Tengvall P., Gold J., Kasemo B. A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation. Colloids Surf. B: Biointerf. 2002, 24:155-170.
43. Binazadeh M., Zeng H., Unsworth L.D. Effect of peptide secondary structure on adsorption and adsorbed film properties on end-grafted polyethylene oxide layers. Acta Biomater. 2014, 10:56-66.
44. Voinova M.V., Jonson M., Kasemo B. 'Missing mass' effect in biosensor's QCM applications. Biosensors Bioelectron. 2002, 17:835-841.