Investigation of Single-Molecule Kinetics Mediated by Weak Hydrogen Bonds within a Biological Nanopore

详细信息    查看全文

• 作者：Alina Asandei ; Aurelia Apetrei ; Yoonkyung Park ; Kyung-Soo Hahm ; Tudor Luchian
• 刊名：Langmuir
• 出版年：2011
• 出版时间：January 4, 2011
• 年：2011
• 卷：27
• 期：1
• 页码：19-24
• 全文大小：889K
• 年卷期：v.27,no.1(January 4, 2011)
• ISSN：1520-5827

文摘

The study of factors essential for protein鈭抪eptide interactions and protein pore-mediated peptide transport are of particular relevance in biology. Wild-type 伪-hemolysin was adopted as a 鈥渘anoreactor鈥?in which perturbations of the current through a protein containing a lumen-residing, aryl-capped antimicrobial peptide were seen for the first time and studied at the single-molecule level. Energy and steric considerations hint that Met-aryl interactions between aromatic residues placed at a peptide鈥檚 extremities and any of the methionines lining the 伪-hemolysin constriction region may be the primary cause of peptide stabilization within the lumen and may be particularly important to the peptide鈭捨?hemolysin interaction.