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Rapid identification of metal‐binding peptoid oligomers by on‐resin X ‐ray fluorescence screening
Author(s) -
Nalband Danielle M.,
Warner Benjamin P.,
Zahler Nathan H.,
Kirshenbaum Kent
Publication year - 2014
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22528
Subject(s) - peptoid , chemistry , pentamer , combinatorial chemistry , fluorescence , metal , metal ions in aqueous solution , solid phase synthesis , nanotechnology , organic chemistry , peptide , biochemistry , physics , materials science , quantum mechanics
N‐Substituted glycine peptoid oligomers have recently attracted attention for their metal binding capabilities. Due to their efficient synthesis on solid phase, peptoids are well suited for generation of compound libraries, followed by screening for molecular recognition and other diverse functional attributes. Ideally, peptoids could be simultaneously screened for binding to a number of metal species. Here, we demonstrate the use of bench‐top X‐ray fluorescence (XRF) instrumentation to screen rapidly, on solid support, a library of peptoid oligomers incorporating metal‐binding functionalities. A subset of the peptoid sequences exhibited significant metal binding capabilities, including a peptoid pentamer and a nonamer that were shown to selectively bind nickel. The binding capabilities were validated by colorimetric assay and by depletion of Ni 2+ ion concentration from solution, establishing bench‐top XRF as a rapid, practicable high‐throughput screening technique for peptoid oligomers. This protocol will facilitate discovery of metallopeptoids with unique material properties. © 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 407–415, 2014.