tailieunhanh - Báo cáo khoa học: Structure–activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken

Cationic antimicrobial peptides are naturally occurring antibiotics that are actively being explored as a new class of anti-infective agents. We recently identified three cathelicidin antimicrobial peptides from chicken, which have potent and broad-spectrum antibacterial activitiesin vitro (Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, Gilliland SE & Zhang G (2006)J Biol Chem281, 2858–2867). | ềFEBS Journal Structure-activity relationships of fowlicidin-1 a cathelicidin antimicrobial peptide in chicken Yanjing Xiao1 z Huaien Dai2 z Yugendar R. Bommineni1 Jose L. Soulages3 Yu-Xi Gong2 Om Prakash2 and Guolong Zhang1 1 Department of AnimalScience Oklahoma State University Stillwater OK USA 2 Department of Biochemistry Kansas State University Manhattan KS USA 3 Department of Biochemistry and Molecular Biology Oklahoma State University Stillwater OK USA Keywords antibiotic resistance antimicrobial peptide cathelicidin chicken structure-activity relationship Correspondence O. Prakash Department of Biochemistry Kansas State University Manhattan KS 66506 USA Fax 1 785 532 7278 Tel 1 785 532 2345 E-mail omp@ G. Zhang Department of AnimalScience Oklahoma State University Stillwater OK 74078 USA Fax 1 405 744 7390 Tel 1 405 744 6619 E-mail zguolon@ These authors contributed equally to this paper Received 4 February 2006 revised 21 March 2006 accepted 5 April2006 doi Cationic antimicrobial peptides are naturally occurring antibiotics that are actively being explored as a new class of anti-infective agents. We recently identified three cathelicidin antimicrobial peptides from chicken which have potent and broad-spectrum antibacterial activities in vitro Xiao Y Cai Y Bommineni YR Fernando SC Prakash O Gilliland SE Zhang G 2006 J Biol Chem 281 2858-2867 . Here we report that fowlicidin-1 mainly adopts an a-helical conformation with a slight kink induced by glycine close to the center in addition to a short flexible unstructured region near the N terminus. To gain further insight into the structural requirements for function a series of truncation and substitution mutants of fow-licidin-1 were synthesized and tested separately for their antibacterial cytolytic and lipopolysaccharide LPS -binding activities. The short C-ter-minal helical segment after the kink consisting of a stretch of eight amino acids residues 16-23 .