Primary research on the binding domain and the binding rate between human C5a and C5L2

SONG Rong; LI Yuan-chao; LU Feng-lin; WU Yu-zhang; HU Cheng-xiang; CHEN Yue

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Primary research on the binding domain and the binding rate between human C5a and C5L2

更新时间：2025-01-15

- Primary research on the binding domain and the binding rate between human C5a and C5L2
- Journal of Army Medical University Vol. 29, Issue 6, Pages: 467-470(2007)
- 作者机构：
  
  第三军医大学:大坪医院野战外科研究所第一研究室, 基础医学部全军免疫学研究所
- 作者简介：
- 基金信息：
- DOI：
  CLC： R392-33;R392.11;R318.04
- Published：2007，
  
  Published Online：30 March 2007，
- 稿件说明：
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SONG RONG, LI YUAN-CHAO, LU FENG-LIN, et al. Primary research on the binding domain and the binding rate between human C5a and C5L2. [J]. Journal of army medical university, 2007, 29(6): 467-470.
DOI：

SONG RONG, LI YUAN-CHAO, LU FENG-LIN, et al. Primary research on the binding domain and the binding rate between human C5a and C5L2. [J]. Journal of army medical university, 2007, 29(6): 467-470. DOI：

摘要

目的通过生物信息学分析人C5L2受体的配体结构域，并进一步利用生物分子相互作用测定技术(biomolecular interaction analysis

BIA)研究其与配体C5a分子间的相互作用。方法以人C5L2蛋白的氨基酸序列为基础，利用网络分析软件以及Goldkey计算机分析软件对人C5L2蛋白二级结构及亲水性、抗原性、可及性、柔韧性、表位等参数进行综合分析

确定可能与rhC5a结合的区域肽段序列，Fmoc方法固相多肽合成候选的结合位多肽，采用IAsys Plus生物传感器系统

以rhC5a为固定相，分别以这些候选结合位多肽为流动相，测定与rhC5a的结合力。结果合成多肽N2(第12~22位)、C3(第265~275位)可与C5a 发生特异性结合，结合率分别为53%和23%。结论人C5L2分子第3~22、179~183、190~195、265~275位等区域满足各项指标，最可能是其配体C5a的结合域。

Abstract

Objective To predict binding domains of human C5a like receptor 2(C5L2) and further to detect the affinity between C5a and C5L2 by the technology of bioinformatics and BIA. Methods Based on amino acid sequence

the parameters of secondary structure

hydrophilicity

accessibility

antigenicity

epitope and flexibility were assessed by using ExPASy Proteomics tools and Goldkey. Meanwhile

the binding rate was detected between human C5a and C5L2

the rhC5a was in immobilization

and the synthesized polypeptides were in streaming movement. The synthesized polypeptides were used to identify the predicted results by biosensor technique. Results The synthesized polypeptides (N2 and C3) could bind to C5a specifically and their binding rate was 53% and 23% respectively. Conclusion Domains between 3-22

179-183

190-195

265-275 were most likely to be the binding domains of C5L2.

关键词

C5aC5L2蛋白配体结合域生物分子相互作用生物传感器

Keywords

C5aC5L2binding domainbiomolecular interactionbiosensor

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Related Institution

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