Conformational Study of the Antimicrobial Peptide Melectin by Circular Dichroism Methods

被引：0

作者：

Kykal, Stanislav ^{[1
]}

Cerovsky, Vaclav ^{[2
]}

Setnicka, Vladimir ^{[1
]}

机构：

[1] Inst Chem Technol, Fak Chem Inzenyrska, Ustav Analyt Chem, CR-16628 Prague 6, Czech Republic

[2] Ustav Organ Chem & Biochem AV CR, Prague 16610 6, Czech Republic

来源：

CHEMICKE LISTY | 2013年 / 107卷 / 03期

关键词：

RANDOM-COIL; SECONDARY STRUCTURE; POLYPEPTIDES; TRIFLUOROETHANOL; OLIGOPEPTIDES; HELIX; FTIR; CD;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Antimicrobial peptides are considered as promising supplements to or substitutes for conventional antibiotics due to their different mechanisms of action. Biological activities of antimicrobial peptides are influenced by their conformations. The solution conformations of 18 amino acid residues peptide melectin (MEP) and its synthetic analogues including C-terminal and N-terminal fragments were studied using electronic and vibrational circular dichroism spectroscopies.

引用

页码：250 / 254

页数：5

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