Applications of circular dichroism for structural analysis of gelatin and antimicrobial peptides

International Journal of Molecular Sciences

Volumn 13, Issue 3, 2012, Pages 3229-3244

  Gopal, Ramamourthy ^a   Park, Jin Soon ^a   Seo, Chang Ho ^b   Park, Yoonkyung ^a  

^a Chosun University   (South Korea)

^b Kongju National University   (South Korea)

Author keywords

Antimicrobial peptides; Cell wall components; Circular dichroism; Gelatin; Lipopolysaccharide; Reduced glutathione; Sodium dodecyl sulfate; Tween 80

Indexed keywords

ANIONIC SURFACTANT; DODECYL SULFATE SODIUM; GELATIN; GLYCYLTRYPTOPHANYLLYSYLLYSYLTRYPTOPHANYLLEUCYLARGINYLLYSYLGLYCYLALANYLLYSYLHISTIDYLLEUCYLGLYCYLGLUTAMINYLALANYLALANYLISOLEUCYLLYSINEAMIDE; LAMINARAN; LIPOPOLYSACCHARIDE; LYSYLTRYPTOPHANYLLYSYLTRYPTOPHANYLLYSYLTRYPTOPHANYLLYSYLTRYPTOPHANAMIDE; MAGAININ 2; MANNAN; PHENYLALANYLLYSYLLYSYLLEUCYLLYSYLLYSYLLEUCYLPHENYLALANYLLYSYLLYSYLISOLEUCYLLEUCYLLYSYLLEUCYLLYSINEAMIDE; POLYPEPTIDE ANTIBIOTIC AGENT; POLYSORBATE 80; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; GLUCAN; POLYSORBATE; SURFACTANT; TRYPTOPHAN;

ALPHA HELIX; ANTIBACTERIAL ACTIVITY; AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; CONFORMATION; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG STRUCTURE; DRUG SYNTHESIS; FEASIBILITY STUDY; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR INTERACTION; NONHUMAN; PSEUDOMONAS AERUGINOSA; AMINO ACID SEQUENCE; CELL LINE; CELL WALL; CHEMISTRY; DRUG EFFECTS; HUMAN; MOLECULAR GENETICS; PROCEDURES; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CELL LINE; CELL WALL; CIRCULAR DICHROISM; GELATIN; GLUCANS; HUMANS; LIPOPOLYSACCHARIDES; MANNANS; MOLECULAR SEQUENCE DATA; POLYSORBATES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS AERUGINOSA; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS; TRYPTOPHAN;

EID: 84858979132     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13033229     Document Type: Article

References (75)

1. Greenfield, N.J. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 1996, 235, 1-10.
2. Johnson, W.C. Secondary structure of proteins through circular dichroism spectroscopy. Annu. Rev. Biophys. Biophys. Chem. 1988, 17, 145-166.
3. Johnson, W.C. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 1999, 35, 307-312.
4. Yeaman, M.R.; Yount, N.Y. Mechanism of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003, 55, 27-55.
5. Hancock, R.E.; Chapple, D.S. Peptide antibiotics. Antimicrob. Agents Chemother. 1999, 43, 1317-1323.
6. Powers, J.P.; Hancock, R.E. The relationship between peptide structure and antibacterial activity. Peptides 2003, 24, 1681-1691.
7. Greenfield, N.J. Applications of circular dichroism in protein and peptide analysis. Trend Anal. Chem. 1999, 18, 236-244.
8. Gopal, R.; Kim, Y.J.; Seo, C.H.; Hahm, K.S.; Park, Y. Reversed sequence enhances antimicrobial activity of a synthetic peptide. J. Peptide Sci. 2011, 17, 329-334.
9. Gopal, R.; Park, S.C.; Ha, K.J.; Cho, S.J.; Kim, S.W.; Song, P.I.; Nah, J.W.; Park, Y.; Hahm, K.S. Effect of leucine and lysine substitution on the antimicrobial activity and evaluation of the mechanism of the HPA3NT3 analog peptide. J. Peptide Sci. 2009, 15, 589-594.
10. Patrzykat, A.; Gallant, J.W.; Seo, J.K.; Pytyck, J.; Douglas, S.E. Novel antimicrobial peptides derived from flatfish genes. Antimicrob. Agents Chemother. 2003, 47, 2464-2470.
11. Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 1987, 84, 5449-5453.
12. Kawanishi, N.; Christenson, H.K.; Ninham, B.W.J. Measurement of the interaction between adsorbed polyelectrolytes: Gelatin on mica surfaces. J. Phys. Chem. 1990, 94, 4611-4617.
13. Likos, C.N.; Vaynberg, K.A.; Lowen, H.; Wagner, N.J. Colloidal stabilization by adsorbed gelatin. Langmuir 2000, 16, 4100-4108.
14. Tabata, Y.; Ikada, Y. Protein release from gelatin matrices. Adv. Drug Deliv. Rev. 1998, 31, 287-301.
15. Wetzel, R.; Buder, E.; Hermel, H.; Hütter, A. Conformations of different gelatins in solutions and in films an analysis of circular dichroism (CD) measurements. Colloid Polym. Sci. 1987, 265, 1036-1045.
16. Gardi, A.; Nischmann, H.S. Intracatenar cross-linking in gelatin with carbodiimide. Helv. Chim. Acta. 1972, 55, 2468-2486.
17. Wustneck, R.; Buder, E.; Wetzel, R.; Hermel, H. The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of cationic surfactants. Colloid Polym. Sci. 1989, 267, 429-433.
18. Wustneck, R.; Buder, E.; Wetzel, R.; Hermel, H. The modification of the triple helical structure of gelatin in aqueous solution 1. The influence of anionic surfactants, pH-value, and temperature. Colloid Polym. Sci. 1988, 266, 1061-1067.
19. Guillen, M.C.G.; Turnay, J.; Fernandez-Diaz, M.D.; Ulmo, N.; Lizarbe, M.A.; Montero, P. Structural and physical properties of gelatin extracted from different marine species: A comparative study. Food Hydrocoll. 2002, 16, 25-34.
20. Engel, J; Prockop, D.J. The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Annu. Rev. Biophys. Biophys. Chem. 1991. 20, 137-152.
21. Gayatri, R.; Sharma, A.K.; Rajaram, R.; Ramasami, T. Chromium (III)-induced structural changes and self-assembly of collagen. Biochem. Biophys. Res. Commun. 2001, 283, 229-235.
22. Leikina, E.; Mertts, M.V.; Kuznetsova, N.; Leikin, S. Type 1 collagen is thermally unstable at body temperature. Proc. Natl. Acad. Sci. USA 2002, 99, 1314-1318.
23. Goo, H.C.; Hwang, Y.S.; Choi, Y.R.; Cho, H.N.; Suh, H. Development of collagenase-resistant collagen and its interaction with adult human dermal fibroblasts. Biomaterials 2003, 24, 5099-5113.
24. Madhan, B.; Subramanian, V.; Rao, J.R.; Nair, B.U.; Ramasami, T. Stabilization of collagen using plant polyphenol: Role of catechin. Int. J. Biol. Macromol. 2005, 37, 47-53.
25. Fathima, N.N.; Devi, R.S.; Rekha, K.B.; Dhathathreyan, A. Collagen-curcumin interaction-A physico-chemical study. J. Chem. Sci. 2009, 121, 509-514.
26. Rosenblum, G.; Van den Steen, P.E.; Cohen, S.R.; Bitler, A.; Brand, D.D.; Opdenakker, G.; Sagi, I. Direct visualization of protease action on collagen triple helical structure. Plos One 2010, 5, doi:10.1371/journal.pone.0011043.
27. Mitra, T.; Sailakshmi, G.; Gnanamani, A.; Mandal, A.B. Di-carboxylic acid cross-linking interactions improves thermal stability and mechanical strength of reconstituted type I collagen. Part I. Oxalic acid. J. Therm. Anal. Calorim. 2011, 105, 325-330.
28. Ramachandran, G.N.; Kartha, G. Structure of collagen. Nature 1955, 176, 593-595.
29. Rich, A.; Crick, F.H. The structure of collagen. Nature 1955, 176, 915-916.
30. Cowan, P.M.; McGavin, S.; North, A.C. The polypeptide chain configuration of collagen. Nature 1955, 176, 1062-1064.
31. Fathima, N.N.; Madhan, B.; Rao, J.R.; Nair, B.U. Effect of zirconium (IV) complexes on the thermal and enzymatic stability of type I collagen. J. Inorg. Biochem. 2003, 95, 47-54.
32. Fathima, N.N.; Bose, M.C.; Rao, J.R.; Nair, B.U. Stabilization of type I collagen against collagenases (type I) and thermal degradation using iron complex. J. Inorg. Biochem. 2006, 100, 1774-1780.
33. Fathima, N.N.; Suresh, R.; Rao, J.R.; Nair, B.U. Role of green tea polyphenols cross linking in alleviating UV radiation effect on collagen. J. Appl. Polym. Sci. 2007, 104, 3642-3648.
34. Franzblau, C.; Schmid, K.; Faris, B.; Beldekas, J.; Garvin, P.; Kagan, H.M.; Bruce, J.; Baum, B.J. The interaction of collagen with alpha1-acid glycoprotein. Biochim. Biophys. Acta 1976, 427, 302-314.
35. Madhan, B.; Muralidharan, C.; Jayakumar, R. Study on the stabilisation of collagen with vegetable tannins in the presence of acrylic polymer. Biomaterials 2002, 23, 2841-2847.
36. Fathima, N.N.; Madhan, B.; Rao, R.T.; Nair, B.U.; Ramasami, T. Interaction of aldehydes with collagen: Effect on thermal enzymatic and conformational stability. Int. J. Biol. Macromol. 2004, 4, 241-247.
37. Usha, R.; Rajaram, A.; Ramasami, T. Stability of collagen in the presence of 3,4-dihydroxyphenylalanine (DOPA). J. Photochem. Photobiol. B 2009, 97, 34-39.
38. Ge, Y.; Macdonald, D.L.; Holroyd, K.J.; Thornsberry, C.; Wexler, H.; Zasloff, M. In vitro antibacterial properties of pexiganan, an analog of magainin. Antimicrob. Agents Chemother. 1999, 43, 782-788.
39. Gopinath, D.; Kumar, M.S.; Selvaraj, D.; Jayakumar, R. Pexiganan-incorported collagen matrices for infected wound-healing processes in rat. J. Biomed. Mater. Res. A 2005, 73, 320-331.
40. Townsend, D.M.; Tew, K.D.; Tapiero, H. The importance of glutathione in human disease. Biomed. Pharmacother. 2003, 57, 145-155.
41. Arul, V.; Gopinath, D.; Gomathi, K.; Jayakumar, R. Biotinylated GHK peptide incorporated collagenous matrix: A novel biomaterial for dermal wound healing in rats. J. Biomed. Mater. Res. B Appl. Biomater. 2005, 73, 383-391.
42. Schibli, D.J.; Epand, R.F.; Vogel, H.J.; Epand, R.M. Tryptophan-rich antimicrobial peptides: Comparative properties and membrane interactions. Biochem. Cell Biol. 2002, 80, 667-677.
43. Dathe, M.; Wieprecht, T. Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1999, 1462, 71-87.
44. Tossi, A.; Sandri, L.; Giangaspero, A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 2000, 55, 4-30.
45. Powers, J.P.S.; Hancock, R.E.W. The relationship between peptide structure and antibacterial activity. Peptides 2003, 24, 1681-1691.
46. Huang, Y.; Huang, J.; Chen, Y. Alpha-helical cationic antimicrobial peptides: Relationships of structure and function. Protein Cell 2010, 1, 143-152.
47. Woody, R.W. Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur. Biophys. J. 1994, 23, 253-262.
48. Ladokhin, A.S.; Selsted, M.E.; White, S.H. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys. J. 1997, 72, 794-805.
49. Liu, Z.; Brady, A.; Young, A.; Rasimick, B.; Chen, K.; Zhou, C.; Kallenbach, N.R. Length effects in antimicrobial peptides of the (RW)n series. Antimicrob. Agents Chemother. 2007, 51 597-603.
50. Mollmann, S.H.; Elofsson, U.; Bukrinsky, J.T.; Frokjaer, S. Displacement of adsorbed insulin by tween 80 monitored using total internal reflection fluorescence and ellipsometry. Pharm. Res. 2005, 22, 1931-1941.
51. Torrent, M.; Navarro, S.; Moussaoui, M.; Nogues, M.V.; Boix, E. Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans. Biochemistry 2008, 47, 3544-3555.
52. Ding, L.; Yang, L.; Weiss, T.M.; Waring, A.J.; Lehrer, R.I.; Huang, H.W. Interaction of antimicrobial peptides with lipopolysaccharides. Biochemistry 2003, 42, 12251-12259.
53. Rosenfeld, Y.; Sahl, H.G.; Shai, Y. Parameters involved in antimicrobial and endotoxin detoxification activities of antimicrobial peptides. Biochemistry 2008, 47, 6488-6478.
54. van der Weerden, N.L.; Hancock, R.E.; Anderson, M.A. Permeabilization of fungal hyphae by the plant defension NAD1 occurs through a cell wall dependent process. J. Biol. Chem. 2010, 285, 37513-37520.
55. Lee, D.G.; Kim, D.H.; Park, Y.; Kim, H.K.; Shin, Y.K.; Choi, C.H.; Hahm, K.S. Fungicidal effect of antimicrobial peptides, PMAP-23, isolated from porcine myeloid against Candida albicans. Biochem. Biophys. Res. Commun. 2001, 282, 570-574.
56. Zhao, H.; Kinnunen, P.K.J. Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 2002, 277, 25170-25177.
57. Swamy, R.N.; Gnanamani, A.; Shanmugasamy, S.; Gopal, R.K.; Mandal, A.B. Bioinformatics in crosslinking chemistry of collagen with selective cross linkers. BMC Res. Notes 2011, 4, doi:10.1186/1756-0500-4-399.
58. Chan, D.I.; Prenner, E.J.; Vogel, H.J. Tryptophan- and arginine-rich antimicrobial peptides: Structure and mechanism of action. Biochim. Biophys. Acta 2006, 1758, 1184-1202.
59. Chen, C.C.; Hsu, W.; Hwang, K.C.; Hwu, J.R.; Lin, C.C.; Horng, J.C. Contributions of cation-π interactions to the collagen triple helix stability. Arch. Biochem. Biophys. 2011, 508, 46-53.
60. Edwards, R.; Harding, K.G. Bacteria and wound healing. Curr. Opin. Infect. Dis. 2004, 17, 91-96.
61. Kustos, T.; Kustos, I.; Kilar, F.; Rappai, G.; Kocsis, B. Effect of antibiotics on cell surface hydrophobicity of bacteria using orthopedic wound infections. Chemotherapy 2003, 9, 237-242.
62. Gomathi, K.; Gopinath, D.; Rafiuddin Ahmed, M.; Jayakumar, R. Quercetin incorported collagen matrices for dermal wound healing processes in rat. Biomaterials 2003, 24, 2767-2772.
63. Hima Bindu, T.V.L.; Vidyavathi, M.; Kavitha, K.; Sastry, T.P.; Suresh Kumar, R.V. Preparation and evaluation of chitosan-gelatin composite films for wound healing activity. Trends Biomater. Artif. Organs 2010, 24, 123-130.
64. Hima Bindu, T.V.L.; Vidyavathi, M.; Kavitha, K.; Sastry, T.P. Preparation and evaluation of gentamicin loaded chitosan-gelatin composite films for wound healing activity. Int. J. Appl. Biol. Pharm. Technol. 2011, 2, 453-463.
65. Iwakura, A.; Tabata, Y.; Tamura, N.; Doi, K.; Nishimura, K.; Nakamura, T.; Shimizu, Y.; Fujita, M.; Komeda, M. Gelatin sheet incorporating basic fibroblast growth factor enhances healing of devascularized sternum in diabetic rats. Circulation 2001, 104, I325-I329.
66. Hima Bindu, T.V.L.; Vidyavathi, M.; Kavitha, K.; Sastry, T.P.; Suresh Kumar, R.V. Preparation and evaluation of ciprofloxacin loaded chitosan-gelatin composite films for wound healing activity. Int. J. Drug. Deliv. 2010, 2, 173-182.
67. Thakur, G.; Mitra, A.; Rousseau, D.; Basak, A.; Sarkar, S.; Pal, K. Crosslinking of gelatin-based drug carriers by genipin induces changes in drug kinetic profiles in vitro. J. Mater. Sci. Mater. Med. 2011, 22, 115-123.
68. Gomez-Guillen, M.C.; Perez-Mateos, M.; Gomez-Estaca, J.; Lopez-Caballero, E.; Gimenez, B.; Montero, P. Fish gelatin: A renewable material for developing active biodegradable film. Trends Food Sci. Technol. 2009, 20, 3-16.
69. Akane, T.; Toshiaki, N.; Hiroshi, M. Acceleration of wound healing by gelatin film dressings with epidermal growth factor. J. Vet. Med. Sci. 2005, 67, 909-913.
70. Baker, M.A.; Maloy, W.L.; Zasloff, M.; Jacob, L.S. Anticancer efficacy of magainin 2 and analogue peptides. Cancer Res. 1993, 53, 3052-3057.
71. Johnstone, S.A.; Gelmon, K.; Mayer, L.D.; Hancock, R.E.W.; Bally, M.B. In vitro characterization of the anticancer activity of membrane-active cationic peptides. I. Peptide-mediated cytotoxicity and peptide-enhanced cytotoxic activity of doxorubicin against wild-type and p-glycoprotein over-expressing tumor cell lines. Anticancer Drug Des. 2000, 15, 151-160.
72. Gallo, R.L.; Ono, M.; Povsic, T.; Page, C.; Eriksson, E.; Klagsbrun, M.; Bernfield, M. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc. Natl. Acad. Sci. USA 1994, 91, 11035-11039.
73. Hancock, R.E.; Sahl, H.G. Antimicrobial and host defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24, 1551-1557.
74. Atherton, E.; Sheppard, R.C. Solid Phase Peptide Synthesis: A Practical Approach; IRL Press: Oxford, UK, 1989.
75. Chen, Y.H.; Yang, J.T.; Chau, K.H. Determination of the helix and beta from of proteins in aqueous solution by circular dichroism. Biochemistry 1974, 13, 3350-3359.