MISC

2004年4月

Mechanical force analysis of peptide interactions using atomic force microscopy

BIOPOLYMERS
  • C Nakamura
  • ,
  • S Takeda
  • ,
  • M Kageshima
  • ,
  • M Ito
  • ,
  • N Sugimoto
  • ,
  • K Sekizawa
  • ,
  • J Miyake

76
1
開始ページ
48
終了ページ
54
記述言語
英語
掲載種別
DOI
10.1002/bip.10572
出版者・発行元
JOHN WILEY & SONS INC

Some peptides have previously been reported to bind low molecular weight chemicals. One such peptide with the amino acid sequence His-Ala-Ser-Tyr-Ser was selectively screened from a phage library and bound to a cationic porphyrin, 5,10,15,20-tetrakis(N-methylpyridinium-4-yl)21 21H,23H-porphine (TMpyP), with a binding constant of 10(5)M(-1) (J. Kawakami, T Kitano, and N. Sugimoto, Chemical Communications, 1999, pp. 1765-1766). The proposed binding was due to pi-electron stacking from two aromatic amino acids of histidine and tyrosine. In this study, the weak interactions between TMpyP and the peptide were further investigated by force curve analysis using atomic force microscopy (AFM). The mechanical force required to unbind the peptide-porphyrin complex was measured by vertical movement of the AFM tip. Peptide self-assembled monolayers were formed on both a gold-coated mica substrate and a gold-coated AFM tip. The TMpyPs could bind between the two peptide layers when the peptide-immobilized AFM tip contacted the peptide-immobilized substrate in solution containing TMpyP. In the retracting process a force that ruptured the interaction between TMpyPs and peptides was observed. The unbinding force values correlated to the concentration of TMpyP. A detection limit of 100 ng/mL porphyrin was obtained for the force measurement, and was similar to surface plasmon resonance sensor detection limits. Furthermore, we calculated the product of the observed force and the length of the molecular elongation to determine the work required to unbind the complexes. The obtained values of unbinding work were in a reasonable range compared to the binding energy of porphyrin-peptide. (C) 2004 Wiley Periodicals, Inc.

リンク情報
DOI
https://doi.org/10.1002/bip.10572
CiNii Articles
http://ci.nii.ac.jp/naid/80016554006
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/14997474
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000220016100007&DestApp=WOS_CPL
ID情報
  • DOI : 10.1002/bip.10572
  • ISSN : 0006-3525
  • CiNii Articles ID : 80016554006
  • PubMed ID : 14997474
  • Web of Science ID : WOS:000220016100007

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