One of the main challenges in oral disease is prevention of bacterial infections considering antibiotic resistance as a result of frequent use of conventional antibiotics. A natural alternative to these chemical antibiotics is antimicrobial peptide (AMP). LL37, a helical and amphipathic peptide with 37 amino acid residues, is the only cathelicidin-derived form of AMPs in humans that has a broad spectrum of antimicrobial activity (Majewski et al. in Cent Eur J immunol 43(4):453–457, https://doi.org/10.5114/ceji.2018.81355, 2018). In this study a bi-functional fusion peptide was designed, which consisted of LL-37 peptide linked to a hydroxyapatite (HA) binding peptide through a GGGGS linker. The fusion peptide antimicrobial activity was assessed against both gram-positive and gram-negative bacteria by the microtiter plate method and minimum inhibitory concentrations of 250 µg/ml and 125 µg/ml were obtained for Streptococcus mutans and Escherichia coli, respectively. The binding affinity of the HABP-LL37 fusion peptide to HA-surfaces was confirmed by the peptide release test using the spectrometer method. The HABP-LL37 fusion peptide immobilization on HA surfaces was done using a simple soaking technique. It was shown that 100 mg of the HA polymer disk could load up to 278 μg (55.6%) of LL37-HABP. Evaluation of the cytotoxic properties of the designed fusion peptide before and after immobilization on HA polymer disks against C2C12 cells showed that immobilization resulted in the reduction of HABP-LL37 cytotoxicity. The use of this bi-functional peptide with HA-based biomaterial can result in the development of novel and safe antimicrobial bone substitutes to manage and reduce the complications of device infection.

中文翻译：

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具有双重功能的新型工程化融合肽：对羟基磷灰石具有抗菌性和强结合力

口腔疾病的主要挑战之一是预防细菌感染，考虑到由于经常使用常规抗生素而产生的抗生素耐药性。这些化学抗生素的天然替代品是抗菌肽（AMP）。LL37是具有37个氨基酸残基的螺旋和两亲性肽，是人类中唯一由cathelicidin衍生的AMP形式，具有广泛的抗菌活性（Majewski等人在Cent Eur Jimmunl 43（4）：453-457 ，https://doi.org/10.5114/ceji.2018.81355，2018）。在本研究中，设计了一种双功能融合肽，该融合肽由通过GGGGS接头与羟基磷灰石（HA）结合肽相连的LL-37肽组成。变形链球菌和大肠杆菌， 分别。HABP-LL37融合肽对HA表面的结合亲和力通过使用光谱仪方法的肽释放测试来证实。使用简单的浸泡技术将HABP-LL37融合肽固定在HA表面上。结果表明，100毫克的HA聚合物圆片可以装载278微克（55.6％）的LL37-HABP。在将固定的融合肽固定在HA聚合物圆盘上针对C2C12细胞之前和之后，对设计的融合肽的细胞毒性进行评估，结果表明固定化导致HABP-LL37细胞毒性的降低。将此双功能肽与基于HA的生物材料一起使用可导致开发出新颖且安全的抗菌骨替代品，以管理并减少装置感染的并发症。