摘要
To investigate the effects of disulphide bond position on the salt
resistance and lipopolysaccharide (LPS)-neutralizing activity of
α-helical homo-dimeric antimicrobial peptides (AMPs), we synthesized
an α-helical model peptide (K6L4W1) and its homo-dimeric
peptides (di-K6L4W1-N, di-K6L4W1-M, and di-K6L4W1-C)
with a disulphide bond at the N-terminus, the central position,
and the C-terminus of the molecules, respectively. Unlike K6L4W1
and di-K6L4W1-M, the antimicrobial activity of di-K6L4W1-N and
di-K6L4W1-C was unaffected by 150 mM NaCl. Both di-K6L4W1-N
and di-K6L4W1-C caused much greater inhibitory effects on nitric
oxide (NO) release in LPS-induced mouse macrophage RAW
264.7 cells, compared to di-K6L4W1-M. Taken together, our results
indicate that the presence of a disulphide bond at the N- or
C-terminus of the molecule, rather than at the central position, is
more effective when designing salt-resistant α-helical homo-dimeric
AMPs with potent antimicrobial and LPS-neutralizing
activities. [BMB reports 2011; 44(11): 747-752]
摘要译文
为了研究二硫键位置对α-螺旋同源二聚抗菌肽（AMP）的耐盐性和脂多糖（LPS）中和活性的影响，我们合成了α-螺旋模型肽（K6L4W1）及其同二聚体肽（di-K6L4W1-N，di-K6L4W1-M和di-K6L4W1-C），在N末端具有二硫键，中心位置，和分子的C末端。与K6L4W1和di-K6L4W1-M不同，二抗K6L4W1-N和二-K6L4W1-C的抗菌活性不受150mM NaCl的影响。与di-K6L4W1-M相比，di-K6L4W1-N和di-K6L4W1-C对LPS诱导的小鼠巨噬细胞RAW264.7细胞中的一氧化氮（NO）释放产生更大的抑制作用。总而言之，我们的结果表明，在分子的N-或C-末端存在二硫键，而不是在中心位置，在设计具有强力抗微生物和LPS中和活性的耐盐α-螺旋同二聚体AMP时更有效。 [BMB报告2011; 44（11）：747-752]
Yong Hai Nan[1] & Song Yub Shin[1,2,*]. Effect of disulphide bond position on salt resistance and LPS-neutralizing activity of α-helical homo-dimeric model antimicrobial peptides[J]. BMB Reports, 2011,44(11): 747-752