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Dermaseptin use in a novel drug delivery system has been proposed. The system is based on the affinity of dermaseptins for the plasma membrane of human erythrocytes. After transient loading of the cells with the non-toxic dermaseptin S4 analogue K4–S4(1–13)a, the peptide is transported in the
180:
systemic circulation to distant microbial targets. Upon reaching a microorganism for which it has greater affinity the dermaseptin derivative is spontaneously transferred to the microbial membrane where it exerts its membrane-lytic activity.
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residues in length and were the first vertebrate peptides demonstrated as having a lethal effect on the filamentous fungi implicated in severe opportunistic infections accompanying immunodeficiency syndrome and immunosuppressive drug therapy.
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of the bacterial membrane. Clear separation of two lobes of positive and negative intramolecular electrostatic potential is thought to be important in cytotoxic activity. Dermaseptins are typically 27-34
297:"Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins"
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73:
61:
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Feder R, Nehushtai R, Mor A (October 2001). "Affinity driven molecular transfer from erythrocyte membrane to target cells".
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211:"The dermaseptin precursors: a protein family with a common preproregion and a variable C-terminal antimicrobial domain"
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residues all are cationic and most have the potential to form amphipathic helices in water or when integrated with the
566:
189:
125:
121:
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Mor A (2000). "Peptide-based antibiotics: a potential answer to raging antimicrobial resistance".
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162:. The sequence of the dermaseptins varies greatly but due to the presence of
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Amiche M, Ducancel F, Mor A, Boulain JC, Menez A, Nicolas P (July 1994).
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10.1002/1098-2299(200007/08)50:3/4<440::aid-ddr27>3.3.co;2-w
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Hancock RE, Falla T, Brown M (1995). "Cationic bactericidal peptides".
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Amiche M, Seon AA, Pierre TN, Nicolas P (August 1999).
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156:isolated from skin of the frog genus
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301:The Journal of Biological Chemistry
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252:Advances in Microbial Physiology
447:Antimicrobial cationic peptides
1:
377:10.1016/s0196-9781(01)00504-6
314:10.1016/S0021-9258(17)32386-4
264:10.1016/s0065-2911(08)60145-9
228:10.1016/s0014-5793(99)00964-3
89:Available protein structures:
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338:Drug Development Research
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190:Antimicrobial resistance
434:Pore-forming toxins
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138:structure summary
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567:Amphibian toxins
516:Diphtheria toxin
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307:(27): 17847–52.
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152:are a family of
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504:Other, nonhuman
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371:(10): 1683–90.
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344:(34): 440–447.
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62:OPM superfamily
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168:lipid bilayer
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488:Other, human
455:Cathelicidin
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221:(3): 352–6.
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215:FEBS Letters
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204:
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159:Phyllomedusa
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150:Dermaseptins
149:
148:
546:Pneumolysin
521:Dermaseptin
74:OPM protein
24:Identifiers
19:Dermaseptin
561:Categories
258:: 135–75.
196:References
173:amino acid
101:structures
465:Dermcidin
572:Peptides
536:Melittin
531:Magainin
526:Latarcin
511:Cecropin
495:Perforin
470:Histatin
460:Defensin
385:11587797
365:Peptides
237:10462042
184:See also
154:peptides
118:RCSB PDB
323:8074751
282:8540420
43:PF12121
393:699138
391:
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321:
280:
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235:
164:lysine
133:PDBsum
107:
97:
55:1.C.52
29:Symbol
541:Nisin
438:TC 1C
389:S2CID
478:HTN3
474:HTN1
381:PMID
319:PMID
278:PMID
268:ISBN
233:PMID
126:PDBj
122:PDBe
105:ECOD
95:Pfam
79:2dd6
50:TCDB
38:Pfam
32:DD_K
373:doi
346:doi
309:doi
305:269
260:doi
223:doi
219:456
113:PDB
67:211
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426:e
419:t
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