Investigation of single-molecule kinetics mediated by weak hydrogen bonds within a biological nanopore.
The study of factors essential for protein-peptide interactions and protein pore-mediated peptide transport are of particular relevance in biology. Wild-type α-hemolysin was adopted as a "nanoreactor" 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's extremities and any of the methionines lining the α-hemolysin constriction region may be the primary cause of peptide stabilization within the lumen and may be particularly important to the peptide-α-hemolysin interaction.
Department of Physics, Laboratory of Molecular Biophysics and Medical Physics, Alexandru I. Cuza University, Blvd. Carol I, No. 11, Iasi 700506, Romania.
Alina
A
Asandei
Aurelia
A
Apetrei
Yoonkyung
Y
Park
Kyung-Soo
KS
Hahm
Tudor
T
Luchian
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism*; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D007700:Kinetics; D008969:Molecular Sequence Data; D058608:Nanopores; D011485:Protein Binding; D013211:Staphylococcus aureus
D023181:Antimicrobial Cationic Peptides; D001427:Bacterial Toxins; D006460:Hemolysin Proteins; C021091:staphylococcal alpha-toxin