Synthesis and antibody recognition of cyclic epitope peptides, together with their dimer and conjugated derivatives based on residues 9-22 of herpes simplex virus type 1 glycoprotein D.

Title:

Synthesis and antibody recognition of cyclic epitope peptides, together with their dimer and conjugated derivatives based on residues 9-22 of herpes simplex virus type 1 glycoprotein D.

Dataset

identifier:	1653617
description:	epitope description:LKMADPNRFRGKDL antigen name:Envelope glycoprotein D host organism:Mus musculus antibody name:A16
aggregation:	instance of dataset
availability:	available
primaryPublications:	19271736

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1014901
landingPage:	http://www.iedb.org/assay/1653617

Publication

type:	Literature
publicationVenue:	Bioconjug Chem
dates:	2009

Dimension

study type:	b cell assays
subject species:	Human alphaherpesvirus 1

Person

fullName:	Annamá ria Jakab Gitta Schlosser Matty Feijlbrief Sytske Welling-Wester Marilena Manea Miquel Vila-Perello David Andreu Ferenc Hudecz Gá bor Mezo

Data Type

method:	antigen inhibition

Study

name:	Synthesis and antibody recognition of cyclic epitope peptides, together with their dimer and conjugated derivatives based on residues 9-22 of herpes simplex virus type 1 glycoprotein D.
description:	Dimers of cyclic peptides (without branches) and the cyclic peptide conjugated to an oligotuftsin derivative through the peptide spacer in the branch showed the highest binding activity to the Mab A16. Although a large variety of cyclic peptides and dimers of cyclic peptides were synthesized, a simple linear peptide 9−22 conjugated to OT20 and dimers of the linear peptide had the highest binding activity to the Mab A16.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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