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Mercuric Ion Sensing by an Overlapping β‐turn Containing Peptide
Author(s) -
Tomar Kalpana,
Soni Satyendra,
Bhadauriya Pratibha,
Parihar Rashmi,
Ganesh Subramaniam,
Nair Nisanth N.,
Ramanathan Gurunath
Publication year - 2017
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201701058
Subject(s) - tetrapeptide , peptide , turn (biochemistry) , chemistry , fluorescence , residue (chemistry) , ion , hela , in vivo , biophysics , stereochemistry , in vitro , biochemistry , biology , physics , optics , organic chemistry , microbiology and biotechnology
A tetrapeptide containing dehydrophenylalanine residue exhibits unusual enhanced fluorescence emission intensity for Hg 2+ ions selectively. In vivo studies on HeLa cells revealed that this peptide could be used to study Hg 2+ trafficking in mammalian cells. The results demonstrate that Hg 2+ can interact with sulfurless peptide backbones, if the latter provides the requisite geometry, especially a folded type III/III overlapping beta turn conformation.