Lecture Antimicrobial peptides .pdf

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signal20-30 aaconserved prepro regionCATHELICIDINSpropiece100-120 aapeptide19-94 aavariable active domainFamily found only in mammals, ca. 40 membersN-terminal highly conserved, identifies cathelicidinsExpressed in bone marrow, stored in peroxidase-negativeneutrophil granules, then exocytosed from activated cellsMost are without antibacterial activity until C-terminalproteolytically removed
Structural diversity of AMPs1-disulphide bondeg bactenecinα-helicaleg cecropin2-disulphide bondseg protegrin3-disulphide bondseg α-defensinlinear non α-helicaleg indolicidinlactoferricin- the smallest known
Page 1: ANTIMICROBIAL PEPTIDES
Page 5: Tried to develop therapeutic usefor
Page 8 and 9: Why the interest?• Increasing int
Page 10 and 11: Emerging Vancomycin-resistant Enter
Page 12 and 13: PREDICTED VALUE OF NEW ANTIBIOTICS(
Page 14 and 15: • Small, 3-4 kDa peptidesMAMMALIA
Page 16: β-DEFENSINSprepropiece20 - 30 aaac
Page 21 and 22: How do AMPs work?eg protegrin
Page 23 and 24: Hydrophobic interactionsANTIMICROBI
Page 25 and 26: SYNERGISM• Mor et al., 1994 demon
Page 27 and 28: Toll receptors• Originally discov
Page 29 and 30: AMPS: ACTIVATION & STIMULATIONDEFEN
Page 31 and 32: AMPs in MytilusAMPs produced in hae
Page 33 and 34: Antibacterial peptides in C. maenas
Page 35 and 36: Penaeidins(shrimps)Destoumieux et a
Page 37 and 38: Summary• Diverse group of low mol

Lecture Antimicrobial peptides .pdf

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