Strategy of Fc-recognizable peptide ligand design for oriented immobilization of antibody

NCUIR > Engineering College > Department of Chemical and Materials Engineering > journal & Dissertation > Item 987654321/101024

Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/101024

Title:	Strategy of Fc-recognizable peptide ligand design for oriented immobilization of antibody
Authors:	陳文逸;Tsai, Ching-Wei;Jheng, Siang-Long;Chen, Wen-Yih;Ruaan, Ruoh-Chyu
Contributors:	工學院化學工程與材料工程學系
Keywords:	Affinity;Antibodies;Antibodies - chemistry;binding capacity;Binding sites;Design;Design engineering;dissociation;electrostatic interactions;humans;hydrophobicity;Immunoglobulin Fc Fragments - chemistry;Ligands;mice;molecular dynamics;molecular models;Peptides;Peptides - chemistry;Prostate;Recognition;Residues;Simulation;Site selection;Strategy;Surface Plasmon Resonance;tryptophan
Date:	2014-01-01
Issue Date:	2026-04-21 14:21:31 (UTC+8)
Publisher:	American Chemical Society;United States: American Chemical Society
Abstract:	摘要： A new strategy for designing a short-chain peptide ligand with high affinity to the Fc region of an antibody was proposed. The targeted antibody is human prostate specific antibody (PSA) derived from Mouse IgG2a. The ligand design strategy involves two major parts: binding site selection and peptide ligand design. One of the exposed hydrophobic patches near the bottom of the antibody’s Fc region, identified from the molecular docking of naphthelene and end-capped tryptophan, was selected as the binding site. After examining the charge distribution around the binding site, various peptide ligands were designed according to the possible hydrophobic and electrostatic interactions. A peptide ligand, RRGW, was found to have high Fc binding affinity by the analysis of molecular dynamics (MD) simulation. The first two residues, two arginines, play an important role in electrostatic interaction between the peptide and the Fc region of the antibody. The fourth residue, the tryptophan, provides the VDW force; and the flexibility of peptide is achieved through the help of the third residue, the glycine. The binding affinity, recognition efficiency, and orientation factor were calculated from the results of surface plasmon resonance (SPR) measurements. The result shows that the dissociation constant is 5.56 × 10–10 M–1. We also found that the recognition efficiency and orientation factor on the ligand attached surface were much higher than those on negatively and positively charged surfaces. This approach provides a simple and fast strategy for small ligands design on oriented antibody immobilization. 其他題名： Anal. Chem 出版者： United States: American Chemical Society 出版日期： 2014-03-18 出處： Analytical Chemistry, 2014-03, Vol.86 (6), p.2931-2938 資源來源： American Chemical Society Journals 版權： Copyright © 2014 American Chemical Society 版權： Copyright American Chemical Society Mar 18, 2014 識別號： ISSN: 0003-2700 識別號： ISSN: 1520-6882 識別號： EISSN: 1520-6882 識別號： DOI: 10.1021/ac4029467 識別號： PMID: 24528188 識別號： CODEN: ANCHAM
Appears in Collections:	[Department of Chemical and Materials Engineering] journal & Dissertation

Files in This Item:

File	Description	Size	Format
index.html		0Kb	HTML	15	View/Open

社群 sharing

Loading...