Please use this identifier to cite or link to this item:
|Title:||Human pIgR mimetic peptidic ligand for affinity purification of IgM: Part I: Ligand design and binding mechanism||Authors:||Gautam, S.
Biomimetic peptidic ligand
|Issue Date:||4-Jan-2013||Citation:||Gautam, S., Loh, K.-C. (2013-01-04). Human pIgR mimetic peptidic ligand for affinity purification of IgM: Part I: Ligand design and binding mechanism. Separation and Purification Technology 102 : 173-179. ScholarBank@NUS Repository. https://doi.org/10.1016/j.seppur.2012.09.023||Abstract:||Synthetic peptides incorporating the complementarity determining region 2 (CDR2)-like loop of domain 1 of human polymeric immunoglobulin receptor (hpIgR-D1) were investigated for their interactions with human Immunoglobulin-M (hIgM) and other hIgs. pep14, a 14mer peptide, emerged as a unique biomimetic ligand with specificity to interact with hIgM and negligible affinity for hIgG, hIgE, hIgA1 and bovine serum albumin. Surface plasmon resonance-based binding studies between immobilized pep14 and fragments of hIgM molecule, namely Fc5μ and Fab, suggested that pep14 was binding to a motif in the constant domain 2 of hIgM. Modified peptides, pep13, pep5A and pep14A were investigated for their interaction with hIgM/ hIgG1 to elucidate the binding mechanism of pep14. Cysteine in pep14 was identified to be crucial for inducing thiophilic-like interactions between the ligand and hIgM while glutamic acid had a significant role in attributing specificity to the ligand to interact with hIgM. Circular dichroism studies suggested the absence of native β-hairpin structure in pep14. The ligand exhibited a more flexible conformation consisting mainly of a mixture of coil and turn. © 2012 Elsevier B.V. All rights reserved.||Source Title:||Separation and Purification Technology||URI:||http://scholarbank.nus.edu.sg/handle/10635/64040||ISSN:||13835866||DOI:||10.1016/j.seppur.2012.09.023|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.