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Title: Human pIgR mimetic peptidic ligand for affinity purification of IgM: Part I: Ligand design and binding mechanism
Authors: Gautam, S.
Loh, K.-C. 
Keywords: Binding mechanism
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.
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
ISSN: 13835866
DOI: 10.1016/j.seppur.2012.09.023
Appears in Collections:Staff Publications

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