Oh J E, Hong S Y, Lee K H
Protein Chemistry Laboratory, Mogam Biotechnology Research Institute, Yongin-city, Kyunggi-Do, Korea.
J Pept Res. 1999 Jan;53(1):41-6. doi: 10.1111/j.1399-3011.1999.tb01615.x.
Many short antimicrobial peptides (< 18mer) have been identified for the development of therapeutic agents. However, Structure-activity relationship (SAR) studies about short antimicrobial peptides have not been extensively performed. To investigate the relationship between activity and structural parameters such as an alpha-helical structure, a net positive charge and a hydrophobicity, we synthesized and characterized diastereomers, scramble peptides and substituted peptides of the short antimicrobial peptide identified by combinatorial libraries. Circular dichroism (CD) spectra and in vitro activity indicated that an alpha-helical structure correlated with the antimicrobial activity and a beta-sheet structure also satisfied a structural requirement for antimicrobial activity. Most peptides consisting of L-amino acids lost antifungal activity in the presence of heat-inactivated serum, while active diastereomers and a scramble peptide with the beta-sheet structure retained antifungal activity in the same condition.
许多短抗菌肽（<18肽）已被鉴定用于治疗药物的开发。然而，关于短抗菌肽的构效关系（SAR）研究尚未广泛开展。为了研究活性与诸如α-螺旋结构、净正电荷和疏水性等结构参数之间的关系，我们合成并表征了通过组合文库鉴定的短抗菌肽的非对映异构体、乱序肽和取代肽。圆二色性（CD）光谱和体外活性表明，α-螺旋结构与抗菌活性相关，β-折叠结构也满足抗菌活性的结构要求。大多数由L-氨基酸组成的肽在热灭活血清存在下失去抗真菌活性，而具有β-折叠结构的活性非对映异构体和乱序肽在相同条件下保留抗真菌活性。
