Kinetic and thermodynamic analyses of adhesion of a peptide, Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm), and human formyl peptide receptor (hFPR).
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.
Cho
Jeong Ho
JH
Department of Organic Materials and Fiber Engineering, Soongsil University, Seoul, 156-743, Korea.
Cho
Kilwon
K
Shin
Hwa Sung
HS
D006801:Humans; D007700:Kinetics; D018625:Microscopy, Atomic Force; D009842:Oligopeptides / Q000378:metabolism*; D011485:Protein Binding; D044042:Receptors, Formyl Peptide / Q000819:agonists* / Q000378:metabolism*; D013816:Thermodynamics
D009842:Oligopeptides; D044042:Receptors, Formyl Peptide; C113617:Trp-Lys-Tyr-Met-Val-Met