Collagen-like antimicrobial peptides.
Collagen-like antimicrobial peptides.
复制标题
类胶原蛋白抗菌肽。
作者：
Masuda R;Kudo M;Dazai Y;Mima T;Koide T
构建了由具有三螺旋支架的刚性棒状肽组成的组合文库。基于胶原蛋白样（Gly-Pro-Yaa）重复序列，将组分肽设计为具有碱性和中性（或疏水性）氨基酸残基的各种组合，灵感来自天然存在的抗菌肽的碱性和两亲性。肽库的筛选导致抗微生物肽的鉴定。结构-活性关系研究表明，三螺旋中N端的Arg簇和C端的胱氨酸结的位置显著有助于抗菌活性。最有效的肽RO ‐ A显示出对革兰氏阴性大肠杆菌和革兰氏阳性枯草芽孢杆菌的活性。此外，大肠杆菌暴露于RO ‐ A导致细胞异常伸长，RO‐ A在人血清中具有显著的稳定性，对哺乳动物细胞的细胞毒性较低。© 2016 Wiley Periodicals，Inc. Biopolymers（Pept Sci）106：453-459，2016.
Combinatorial library composed of rigid rod‐like peptides with a triple‐helical scaffold was constructed. The component peptides were designed to have various combinations of basic and neutral (or hydrophobic) amino acid residues based on collagen‐like (Gly‐Pro‐Yaa)‐repeating sequences, inspired from the basic and amphiphilic nature of naturally occurring antimicrobial peptides. Screening of the peptide pools resulted in identification of antimicrobial peptides. A structure‐activity relationship study revealed that the position of Arg‐cluster at N‐terminus and cystine knots at C‐terminus in the triple helix significantly contributed to the antimicrobial activity. The most potent peptideRO‐Ashowed activity against Gram‐negativeEscherichia coliand Gram‐positiveBacillus subtilis. In addition,Escherichia coliexposed toRO‐Aresulted in abnormal elongation of the cells.RO‐Awas also shown to have remarkable stability in human serum and low cytotoxicity to mammalian cells. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 453–459, 2016.