Structure-activity relationship study of the plant-derived decapeptide OSIP108 inhibiting Candida albicans biofilm formation
We performed a structure-activity relationship study of the antibiofilm plant-derived decapeptide OSIP108. Introduction of positively charged amino acids R, H, and K resulted in an up-to-5-fold-increased antibiofilm activity against Candida albicans compared to native OSIP108, whereas replacement of...
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| Veröffentlicht in: | Antimicrobial Agents and Chemotherapy 2014-08, Vol.58 (8), p.4974-4977 |
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| container_title | Antimicrobial Agents and Chemotherapy |
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| creator | Delattin, Nicolas De Brucker, Katrijn Craik, David Cheneval, Oivier De Coninck, Barbara Cammue, Bruno Thevissen, Karin |
| description | We performed a structure-activity relationship study of the antibiofilm plant-derived decapeptide OSIP108. Introduction of positively charged amino acids R, H, and K resulted in an up-to-5-fold-increased antibiofilm activity against Candida albicans compared to native OSIP108, whereas replacement of R9 resulted in complete abolishment of its antibiofilm activity. By combining the most promising amino acid substitutions, we found that the double-substituted OSIP108 analogue Q6R/G7K had an 8-fold-increased antibiofilm activity. |
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Introduction of positively charged amino acids R, H, and K resulted in an up-to-5-fold-increased antibiofilm activity against Candida albicans compared to native OSIP108, whereas replacement of R9 resulted in complete abolishment of its antibiofilm activity. 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| source | Lirias (KU Leuven Association); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| title | Structure-activity relationship study of the plant-derived decapeptide OSIP108 inhibiting Candida albicans biofilm formation |
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