Structural Properties of Antimicrobial Peptides acting on Bacterial
author:
Boštjan Japelj,
Drug Discovery Department, LEK
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| Slides | |
| 0:00 | STRUCTURAL PROPERTIES OF ANTIMICROBIAL PEPTIDES ACTING ON BACTERIAL MEMBRANES |
| 0:29 | Antibiotics – “miracle drugs” |
| 1:08 | Cationic antimicrobial peptides |
| 1:57 | - act on membranes and intracellular targets, |
| 2:54 | LACTOFERRIN |
| 5:08 | NMR study of LF11 + S-LPS, LF11 + SDS, LF11 + DPC |
| 6:52 | LF11 + S-LPS |
| 7:36 | Comparison of LPS interaction motifs in FhuA (left)1, LF11 (center)2 and polymyxin B (right)3,4 |
| 8:32 | Comparison of structures LF11+S-LPS, LF11+SDS, LF11+DPC |
| 9:25 | N-terminal part of LF11 is protected from fluoresscence quenching |
| 10:35 | C12LF11 |
| 12:18 | P3-55 |
| 12:39 | P3-55 |
| 13:11 | Circular dichroism spectra |
| 13:43 | Structure of P3-55 in DPC and Structure of P3-55 in SDS |
| 14:57 | Positioning and orientation of P3-55 in micelles |
| 15:57 | reference and 5 - DSA |
| 16:29 | Normalized I/Iref ratios of HN-Ha cross peaks in NOESY spectrum |
| 17:25 | Molecular dynamics of P3-55 in DPC |
| 18:46 | Mechanism of interaction of ANEPID peptides with the membrane of Gram-negative bacteria. |
| 20:46 | Acknowledgements |
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