Kinetic and thermodynamic analyses of adhesion of a peptide, Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm), and human formyl peptide receptor (hFPR)

Jeong Ho Cho, Kilwon Cho, Hwa Sung Shin

Research output: Contribution to journalArticlepeer-review

Abstract

The kinetic and thermodynamic properties of a peptide-receptor interaction was investigated by measuring the adhesion force in the reaction via atomic force microscopy (AFM). Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm), considered as a model system in the present study, is a potent neutrophil chemo-attractant. Since being identified as an agonist for formyl peptide receptor (FPR), WKYMVm's high affinity to FPR has been verified through investigation of its kinetic and physiological behaviors via conventional methods. However, there have been no reports on the adhesion force of WKYMVm-FPR. In this research, we measured the adhesion force of WKYMVm-FPR using AFM. Kinetic parameters obtained from the relationship between the adhesion force and loading rate were used to characterize the thermodynamic properties of WKYMVm-hFPR binding.

Original languageEnglish
Pages (from-to)773-779
Number of pages7
JournalBiotechnology Letters
Volume32
Issue number6
DOIs
Publication statusPublished - 2010

Bibliographical note

Funding Information:
Acknowledgement H.S. Shin acknowledges support from Inha University’s internal research fund.

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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