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https://doi.org/10.1016/j.seppur.2012.09.023
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 Immunoglobulin-M pIgR |
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 |
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