Tuning the morphology of mesoscopic structures of porphyrin macrocycles functionalized by an antimicrobial peptide
Tuning the morphology of mesoscopic structures of porphyrin macrocycles functionalized by an antimicrobial peptide
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DOI：
10.1142/s1088424619502006
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发表时间：
2020-05-01
影响因子：
1.5
通讯作者：
Venanzi, Mariano
中科院分区：
文献类型：
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作者：
Cimino, Rita;Grelloni, Elisa;Venanzi, Mariano
利用光学光谱和纳米显微成像技术研究了两种多肽-卟啉复合物的聚集特性。具体地，四苯基卟啉平台通过（L）-爪蟾抗菌肽（一种23个残基长的抗微生物肽）和通过（L）-爪蟾抗菌肽类似物官能化，所述（L）-爪蟾抗菌肽类似物通过单个残基取代（即，在肽链的位置5处Ala相对于Phe的取代）而不同于母体肽。光谱和显微镜的结果表明，这种单一的网站取代所获得的两个肽类似物的二级结构的影响很小，但深刻影响的形态的介观结构沉积在亲水性云母从甲醇/水溶液。特别是，只有Ala取代的肽-卟啉缀合物被证明能够形成微米纤维，均匀地涂覆在亲水性云母表面。这些结果为卟啉-肽类化合物在局部光动力学治疗中的潜在应用以及设计固态立体选择性传感器铺平了道路。
The aggregation properties of two peptide-porphyrin conjugates were investigated by optical spectroscopy and microscopy imaging with nanometer resolution. Specifically, a tetraphenylporphyrin platform was functionalized by (L)-magainin, a 23-residue long antimicrobial peptide, and by a (L)-magainin analogue differing from the parent peptide by a single residue substitution, i.e. an Ala vs. Phe replacement in the position 5 of the peptide chain. Spectroscopic and microscopy results show that this single-site substitution has a small effect on the secondary structure attained by the two peptide analogues, but deeply affects the morphology of the mesoscopic structures deposited on hydrophilic mica from methanol/water solutions. In particular, only the Ala-substituted peptide-porphyrin conjugate was shown to be able to form micrometric fibrils, coating homogeneously a hydrophilic mica surface. These results pave the way for potential applications of porphyrin-peptide compounds in localized photodynamic therapy and for designing solid-state stereoselective sensors.