The effect of thiol functional group incorporation into cationic helical peptides on antimicrobial activities and spectra

Biomaterials

Volumn 32, Issue 34, 2011, Pages 9100-9108

  Wiradharma, Nikken ^a   Khan, Majad ^a   Yong, Lin Kin ^a   Hauser, Charlotte A E ^a   Seow, See Voon ^b   Zhang, Shuguang ^c   Yang, Yi Yan ^a  

^a INSTITUTE OF BIOENGINEERING AND NANOTECHNOLOGY   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c Massachusetts Institute of Technology Cambridge   (United States)

Author keywords

Helix; Antimicrobial peptides (AMP); Drug resistance; Hemolysis; Membrane lysis; Thiol and sulfhydryl

Indexed keywords

ANTI-MICROBIAL ACTIVITY; ANTI-MICROBIAL AGENT; ANTIMICROBIAL PEPTIDE; BACILLUS SUBTILIS; CANDIDA ALBICANS; CIPROFLOXACIN; CYSTEINE RESIDUES; DRUG RESISTANCE; HELICAL PEPTIDE; HELICAL STRUCTURES; HEMOLYSIS; HIGH SELECTIVITY; HUMAN MONOCYTES; LIPOPOLYSACCHARIDES; MICROBIAL CELLS; MICROBIAL MEMBRANES; PENICILLIN G; RED BLOOD CELL; SAFETY ASPECTS; SHORT TIME SCALE; SULFHYDRYL; THIOL FUNCTIONAL GROUPS; TIME-SCALES;

AMINO ACIDS; ANTIBIOTICS; BACTERIA; BACTERIOLOGY; BLOOD; ESCHERICHIA COLI; FUNCTIONAL GROUPS; YEAST;

PEPTIDES;

CIPROFLOXACIN; GAMMA INTERFERON; LIPOPOLYSACCHARIDE; PENICILLIN G; POLYPEPTIDE ANTIBIOTIC AGENT; TUMOR NECROSIS FACTOR ALPHA;

ANTIBACTERIAL ACTIVITY; ANTIBIOTIC RESISTANCE; ARTICLE; BACILLUS SUBTILIS; BACTERIAL CELL; CANDIDA ALBICANS; CELL DAMAGE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DRUG SELECTIVITY; ERYTHROCYTE; ESCHERICHIA COLI; HEMOLYSIS; HUMAN; HUMAN CELL; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA;

AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; BACILLUS SUBTILIS; BACTERIAL INFECTIONS; CANDIDA ALBICANS; CANDIDIASIS; ESCHERICHIA COLI; HEMOLYSIS; HUMANS; MICROBIAL SENSITIVITY TESTS; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS AERUGINOSA; SULFHYDRYL COMPOUNDS; TUMOR NECROSIS FACTOR-ALPHA;

BACILLUS SUBTILIS; CANDIDA ALBICANS; ESCHERICHIA COLI; NEGIBACTERIA; POSIBACTERIA; PSEUDOMONAS;

EID: 80053117299     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2011.08.020     Document Type: Article

References (35)

1. Hamley I.W. Self-assembly of amphiphilic peptides. Soft Matter 2011, [Advance article, Tutorial Review]. 10.1039/C0SM01218A.
2. Zhao X., Pan F., Xu H., Hauser C.E.A., Zhang S., Lu J.R. Molecular self-assembly and applications of designer peptide amphiphiles. Chem Soc Rev 2010, 39:3480-3498.
3. Liu S.Q., Tian Q., Hedrick J.L., Hui J.H.P., Ee P.L.R., Yang Y.-Y. Biomimetic hydrogels for chondrogenic differentiation of human mesenchymal stem cells to neocartilage. Biomaterials 2010, 31:7298-7307.
4. Khew S.T., Yang Q.J., Tong Y.W. Enzymatically crosslinked collagen-mimetic dendrimers that promote integrin-targeted cell adhesion. Biomaterials 2008, 29:3034-3045.
5. Hauser C.A.E., Deng R., Mishra A., Loo Y., Khoe U., Zhuang F., et al. Natural tri- to hexapeptides self-assembled in water to amiloid β-type fiber aggregates by unexpected α-helical intermediate structures. Proc Natl Acad Sci USA 2011, 108:1361-1366.
6. Mart R.J., Osborne R.D., Stevens M.M., Ulijin R.V. Peptide-based stimuli-responsive biomaterials. Soft Matter 2006, 2:822-835.
7. Wiradharma N., Tong Y.W., Yang Y.-Y. Self-assembled oligopeptide nanostructures for co-delivery of drug and gene with synergistic effect. Biomaterials 2009, 30:3100-3109.
8. Wiradharma N., Khan M., Tong Y.W., Wang S., Yang Y.-Y. Self-assembled cationic oligopeptide as efficient gene delivery in vitro. Adv Func Mater 2008, 18:943-951.
9. Wang W., Yang Z., Patanavanich S., Xu B., Chau Y. Controlling self-assembly within nanospace for peptide nanoparticle fabrication. Soft Matter 2008, 4:1617-1620.
10. Liu L., Xu K., Wang H., Tan P.K.J., Fan W., Venkatraman S.S., et al. Self-assembled cationic peptide nanoparticles as an efficient antimicrobial agent. Nat Nanotechnol 2009, 4:457-463.
11. Wang H., Xu K., Liu L., Tan J.P., Chen Y., Li Y., et al. The efficacy of self-assembled cationic antimicrobial peptide nanoparticles against Cryptococcus neoformans for the treatment of meningitis. Biomaterials 2010, 31:2874-2881.
12. Chen C., Pan F., Zhang S., Hu J., Cao M., Wang J., et al. Antibacterial activities of short designer peptides: a link between propensity for nanostructuring and capacity for membrane destabilization. Biomacromolecules 2010, 11:402-411.
13. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
14. Hancock R.E., Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 2006, 24:1551-1557.
15. Epand R.M., Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim Biophys Acta 1999, 1462:11-28.
16. Dzidic S., Suskovic J., Koz B. Antibiotic resistance mechanisms in bacteria: biochemical and genetic aspects. Food Technol Biotechnol 2008, 46:11-21.
17. Wright G.D. Bacterial resistance to antibiotics: enzymatic degradation and modification. Adv Drug Deliv Rev 2005, 57:1451-1470.
18. Lambert P.A. Bacterial resistance to antibiotics: modified target sites. Adv Drug Deliv Rev 2005, 57:1471-1485.
19. Kumar A., Schweizer H.P. Bacterial resistance to antibiotics: active efflux and reduced uptake. Adv Drug Deliv Rev 2005, 57:1486-1513.
20. Wiradharma N., Khoe U., Hauser C.A.E., Seow S.V., Zhang S., Yang Y.-Y. Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. Biomaterials 2011, 32:2204-2212.
21. Tew G.N., Liu D., Chen B., Doerksen R.J., Kaplan J., Carroll P.J., et al. De novo design of biomimetic antimicrobial polymers. Proc Natl Acad Sci USA 2002, 99:5110-5114.
22. Sellenet P.H., Allison B.C., Applegate B.M., Youngblood J.P. Synergistic activity of hydrophilic modification in antibiotic polymers. Biomacromolecules 2007, 8:19-23.
23. Kenawy E.-R., Abdel-Hay F.I., Abou El-Magd A., Mahmoud Y. Biologically active polymers: VII. Synthesis and antimicrobial activity of some crosslinked copolymers with quaternary ammonium and phosphonium groups. React Funct Polym 2006, 66:419-429.
24. Hancock R.E., Patrzykat A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr Drug Targets Infect Disord 2002, 2:79-83.
25. Navon-Venezia S., Feder R., Gaidukov L., Carmeli Y., Mor A. Antibacterial properties of dermaseptin S4 derivatives with in vivo activity. Antimicrobial Agents Chemother 2002, 46:689-694.
26. Bell G., Gouyon P.H. Arming the enemy: the evolution of resistance to self-proteins. Microbiology 2003, 149:1367-1375.
27. Loose C., Jensen K., Rigoutsos I., Stephanopoulos G. A linguistic model for the rational design of antimicrobial peptides. Nature 2006, 443:867-869.
28. Yomogida S., Nagaoka I., Yamashita T. Involvement of cysteine residues in the biological activity of the active fragments of guinea pig neutrophil cationic peptides. Infect Immun 1995, 63:2344-2346.
29. Domencio P., Salo R.J., Novick S.G., Schoch P.E., van Horn K., Cunha B.A. Enhancement of bismuth antibacterial activity with lipophilic thiol chelators. Antimicrob Agents Chemother 1997, 41:1697-1703.
30. Allcock H.R., Rutt J.S. Synthesis of polyphosphazenes with isothiocyanato, thiourethane and thiourea side groups. Macromolecules 1999, 24:2852-2857.
31. Pandey B.K., Ahmad A., Asthana N., Azmi S., Srivastava R.M., Srivastava S., et al. Cell-selective lysis by novel analogues of melittin against human red blood cells and Escheria coli. Biochemistry 2010, 49:7920-7929.
32. Chou P.Y., Fasman G.D. Empirical predictions of protein conformation. Annu Rev Biochem 1978, 47:251-276.
33. Rossjohn J., Feil S.C., McKinstry W.J., Tweten R.K., Parker M.W. Structure of a cholesterol-binding thiol-activated cytolysin and a model of its membrane form. Cell 1997, 89:685-692.
34. Saluk-Juszczak J., Wachowicz B., Bald E., Gowacki R. Effects of lipopolysaccharides from gram-negative bacteria on the level of thiols in blood platelets. Curr Microbiol 2005, 51:153-155.
35. Williams D.F. On the mechanisms of biocompatibility. Biomaterials 2008, 29:2941-2953.